|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-1305 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 871.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 10 PRESAGILSSLMFCFALPILFKGRKQTLQPTDLYKTLNEHEAASLGDEFFQGWEDEVARcrrkgdsgRKPSVLRVIGRVF 89
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK--------PKPWLLRALNNSL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 90 GWRLIMSGItiaaLELGTRATV---PLLLAGLISefSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMR 166
Cdd:PLN03130 300 GGRFWLGGF----FKIGNDLSQfvgPLLLNLLLE--SMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 167 VAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLY 246
Cdd:PLN03130 374 STLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 247 LPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLrGILLSFeiTL 326
Cdd:PLN03130 454 FPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLL-SAFNSF--IL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 327 GRIAIFVSLLGF---VLGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRITNFMMreeanvidmserr 403
Cdd:PLN03130 531 NSIPVLVTVVSFgvfTLLGGDLTPARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLL------------- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 404 dekAEEEQHLLKEVEKRSYPVgigkepdtlVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL 483
Cdd:PLN03130 597 ---AEERVLLPNPPLEPGLPA---------ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 484 GELPPES-GSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHG-DGTIVGERGASLSGG 561
Cdd:PLN03130 665 GELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGgDLTEIGERGVNISGG 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 562 QRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYE 641
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYE 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 642 EMLKSGQDFAQLLvestQNSGGGDEIITSP---NLSRQSSALSTKSSNGSSSSLESMVEKEKPKPSAVSSQESRSGGQIG 718
Cdd:PLN03130 825 ELSNNGPLFQKLM----ENAGKMEEYVEENgeeEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 719 LSMYKKYFGAGCGVLVFVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLDIYY---FTAINVGLVICALLRTLLFFNI 795
Cdd:PLN03130 901 WKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPLFYnliYALLSFGQVLVTLLNSYWLIMS 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 796 TMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDE-VMPAVMLDCIQIFLTLTGIICVLCVTNpwylINT 874
Cdd:PLN03130 981 SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRnVAVFVNMFLGQIFQLLSTFVLIGIVST----ISL 1056
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 875 FAMM---LAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAqqtligqYD-----NYQDLHSSGYYT 946
Cdd:PLN03130 1057 WAIMpllVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKA-------YDrmaeiNGRSMDNNIRFT 1129
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 947 FV--STSRAFGYYLD-----LFCVAYVISVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERV 1019
Cdd:PLN03130 1130 LVnmSSNRWLAIRLEtlgglMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERV 1209
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1020 LEYKDLDPEgdfnSPAE---KQPPKSWPKEGKLVTKDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLIN 1096
Cdd:PLN03130 1210 GTYIDLPSE----APLVienNRPPPGWPSSGSIKFEDVVLRYRPEL--PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1097 ALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSG 1175
Cdd:PLN03130 1284 ALFRIvELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLG 1363
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1176 LQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVL 1255
Cdd:PLN03130 1364 LDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRIL 1443
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 28574259 1256 VMDAGHVVEFGSPYELLTaSKAKVFHGMVMQTGKASFDHLLKVAENTKQN 1305
Cdd:PLN03130 1444 VLDAGRVVEFDTPENLLS-NEGSAFSKMVQSTGAANAQYLRSLVFGGDED 1492
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-1288 |
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: 854.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 8 PNPRESAGILSSLMFCFALPILFKGRKQTLQPTDLYKTLNEHEAASLGDEFFQGWEDEVARCRR---------------K 72
Cdd:TIGR00957 201 PCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKqpvsavygkkdpskpK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 73 GDSG------------------RKPSVLRVIGRVFGWRLIMSGITIAALELGTRATvPLLLAGLIsEFSEHGNGHSYNAQ 134
Cdd:TIGR00957 281 GSSQldaneevealivksphkpRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIG-PQILSLLI-RFVNDPMAPDWQGY 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 135 IYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFL 214
Cdd:TIGR00957 359 FYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 215 WLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPF 294
Cdd:TIGR00957 439 WSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 295 GKLIGQMRRSEMSSIRQMNLLRG------ILLSFEITLGRIAIFVsllgFVLGGGELTAERAFCVTAFYNILRRTVSkFF 368
Cdd:TIGR00957 519 LDKVEGIRQEELKVLKKSAYLHAvgtftwVCTPFLVALITFAVYV----TVDENNILDAEKAFVSLALFNILRFPLN-IL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 369 PSGMSQFAELLVSMRRITNFMMREEANVidmserrdekaeeeqhllKEVEKRSYPVGIGKEpdtlVEIKALRARWGQEQH 448
Cdd:TIGR00957 594 PMVISSIVQASVSLKRLRIFLSHEELEP------------------DSIERRTIKPGEGNS----ITVHNATFTWARDLP 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 449 DlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRY 528
Cdd:TIGR00957 652 P-TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYY 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 529 RTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM--RGFL 605
Cdd:TIGR00957 731 QQVLEACALLPDLEILpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 606 GKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLVE--------------STQNSGGGDEIITSP 671
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqghledswTALVSGEGKEAKLIE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 672 N-----------LSRQSSALSTK---SSNGSSSSLESMVEKEKPKPSAVSSQESRSGGQIGLSMYKKYFGAgCGVLVFVV 737
Cdd:TIGR00957 891 NgmlvtdvvgkqLQRQLSASSSDsgdQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKA-IGLFITFL 969
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 738 LIMLCIGTQILASGGDYFLSYWVKNTASSST-------LDIYYFTAINVGLVIcaLLRTLLFFNITMHSSTELHNTMFQG 810
Cdd:TIGR00957 970 SIFLFVCNHVSALASNYWLSLWTDDPMVNGTqnntslrLSVYGALGILQGFAV--FGYSMAVSIGGIQASRVLHQDLLHN 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 811 LSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLK 890
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA 1127
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 891 TSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDlfCVAYVISVI 970
Cdd:TIGR00957 1128 SSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE--CVGNCIVLF 1205
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 971 LHNFFNPPLH--NAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPEGDFNSpAEKQPPKSWPKEGK 1048
Cdd:TIGR00957 1206 AALFAVISRHslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQI-QETAPPSGWPPRGR 1284
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNspCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN-DGAILIDSLDTNDIGLHDLRSKI 1127
Cdd:TIGR00957 1285 VEFRNYCLRYREDLD--LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKI 1362
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTASkaKVFHGMVMQT 1287
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR--GIFYSMAKDA 1520
|
.
gi 28574259 1288 G 1288
Cdd:TIGR00957 1521 G 1521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-1305 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 809.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 10 PRESAGILSSLMFCFALPILFKGRKQTLQPTDLYKTLNEHEAASLGDEFFQGWEDEVARcrrkgdsgRKPSVLRVIGRVF 89
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRR--------PKPWLLRALNNSL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 90 GWRLIMSGITIAALELgTRATVPLLLAGLISEFSEhgNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAV 169
Cdd:PLN03232 300 GGRFWLGGIFKIGHDL-SQFVGPVILSHLLQSMQE--GDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 170 SSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPL 249
Cdd:PLN03232 377 VAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 250 QTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGiLLSFeiTLGRI 329
Cdd:PLN03232 457 QTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA-FNSF--ILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 330 AIFVSLLGF---VLGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRITNFMMREEanvidmserrdek 406
Cdd:PLN03232 534 PVVVTLVSFgvfVLLGGDLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE------------- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 407 aeeeqhllkEVEKRSYPVgigkEPDT-LVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGE 485
Cdd:PLN03232 600 ---------RILAQNPPL----QPGApAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 486 LPP-ESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHG-DGTIVGERGASLSGGQR 563
Cdd:PLN03232 667 LSHaETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGrDLTEIGERGVNISGGQK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 564 ARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEM 643
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 644 LKSGQDFAQLLvestQNSGGGDEIITSPNLSRQSSALSTKSSNGSSSSLESMVEKEKPKPSAVSSQESRSGGQIGLSMYK 723
Cdd:PLN03232 827 SKSGSLFKKLM----ENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLM 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 724 KYFGAGCGVLVFVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLDIYY---FTAINVGLVICALLRTLLFFNITMHSS 800
Cdd:PLN03232 903 RYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYivvYALLGFGQVAVTFTNSFWLISSSLHAA 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 801 TELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMldciQIFLTLTgiicvlcvtnpWYLINTFAM--- 877
Cdd:PLN03232 983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLM----NMFMNQL-----------WQLLSTFALigt 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 878 ------------MLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAqqtligqYD-----NYQDLH 940
Cdd:PLN03232 1048 vstislwaimplLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKA-------YDrmakiNGKSMD 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 941 SSGYYTFVSTSRAFGYYLDLFCVAYVI-------SVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAM 1013
Cdd:PLN03232 1121 NNIRFTLANTSSNRWLTIRLETLGGVMiwltatfAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSL 1200
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1014 TSVERVLEYKDLDPEgdfnSPA---EKQPPKSWPKEGKLVTKDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAG 1090
Cdd:PLN03232 1201 NSVERVGNYIDLPSE----ATAiieNNRPVSGWPSRGSIKFEDVHLRYRPGL--PPVLHGLSFFVSPSEKVGVVGRTGAG 1274
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1091 KSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEI 1169
Cdd:PLN03232 1275 KSSMLNALFRIvELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVI 1354
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1170 SELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIM 1249
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1250 DSDKVLVMDAGHVVEFGSPYELLTaSKAKVFHGMVMQTGKASFDHLLKVAENTKQN 1305
Cdd:PLN03232 1435 DCDKILVLSSGQVLEYDSPQELLS-RDTSAFFRMVHSTGPANAQYLSNLVFERREN 1489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1273 |
0e+00 |
|
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: 686.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1 MQASklppnPRESAGILSSLMFCFALPILFKGRKQTLQPTDLYKTLNEHEAASLGDEFFQGWEDEVArcrrkgDSGRKPS 80
Cdd:TIGR01271 1 MQRS-----PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELA------SAKKNPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 81 VLRVIGRVFGWRLIMSGITIAALELgTRATVPLLLAGLISEFSEHgngHSYNAQI-YAVLLIACIL--ASVLLTHPYMMG 157
Cdd:TIGR01271 70 LLNALRRCFFWRFVFYGILLYFGEA-TKAVQPLLLGRIIASYDPF---NAPEREIaYYLALGLCLLfiVRTLLLHPAIFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 158 MMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASF 237
Cdd:TIGR01271 146 LHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 238 YGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRG 317
Cdd:TIGR01271 226 CGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 318 ILLSFEITLGRIAIFVSLLGFVLGGGeLTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRITNFMMREEANVI 397
Cdd:TIGR01271 306 FYSSAFFFSGFFVVFLSVVPYALIKG-IILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 398 dmserrdekaeEEQHLLKEVE----KRSYPVGIGkepDTLVEIKALRARWGQEQHDL-------------VLNNVNMSLR 460
Cdd:TIGR01271 385 -----------EYNLTTTEVEmvnvTASWDEGIG---ELFEKIKQNNKARKQPNGDDglffsnfslyvtpVLKNISFKLE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 461 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERD 540
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEED 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 541 LELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQF 619
Cdd:TIGR01271 531 IALFpEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEH 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 620 LEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL--------------------------VESTQNSGGGDE------- 666
Cdd:TIGR01271 611 LKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsiltetlrrvsIDGDSTVFSGPEtikqsfk 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 667 -------------IITSP-NLSRQSSALSTKSSNGSSSSLES-----------------MVEKEKPKPSAVSS------- 708
Cdd:TIGR01271 691 qpppefaekrkqsIILNPiASARKFSFVQMGPQKAQATTIEDavrepserkfslvpedeQGEESLPRGNQYHHglqhqaq 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 709 ----------QESRSGGQI---------------------GLSMYKKYFGAGCGV------------------------- 732
Cdd:TIGR01271 771 rrqsvlqlmtHSNRGENRReqlqtsfrkkssitqqnelasELDIYSRRLSKDSVYeiseeineedlkecfaderenvfet 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 733 ---------------LVFV-VLIMLCIGTQILASGGDYFL--------SYWVKNTASSSTLDI-----------YYFTAI 777
Cdd:TIGR01271 851 ttwntylryittnrnLVFVlIFCLVIFLAEVAASLLGLWLitdnpsapNYVDQQHANASSPDVqkpviitptsaYYIFYI 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 778 NVG----LVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIF 853
Cdd:TIGR01271 931 YVGtadsVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLT 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 854 LTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQY 933
Cdd:TIGR01271 1011 LIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLF 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 934 DNYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVISVIlhnFFNPPLHN--AGQIGLAITQALGMTGMVQWGMRQSAELEN 1011
Cdd:TIGR01271 1091 HKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVT---FIAIGTNQdgEGEVGIILTLAMNILSTLQWAVNSSIDVDG 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1012 AMTSVERVLEYKDLDPE-------GDFNSPAE------KQPPKSWPKEGKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPM 1078
Cdd:TIGR01271 1168 LMRSVSRVFKFIDLPQEeprpsggGGKYQLSTvlvienPHAQKCWPSGGQMDVQGLTAKYTEAGRA--VLQDLSFSVEGG 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1079 EKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWK 1158
Cdd:TIGR01271 1246 QRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWK 1325
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1159 ALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTV 1238
Cdd:TIGR01271 1326 VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTV 1405
|
1450 1460 1470
....*....|....*....|....*....|....*
gi 28574259 1239 LTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:TIGR01271 1406 ILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
110-1300 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 636.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 110 TVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMmHLAMKMRVAVSSAIYRKALRLSRTSLG--G 187
Cdd:PTZ00243 262 TLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISI-RCGLQYRSALNALIFEKCFTISSKSLAqpD 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 188 TTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALR 267
Cdd:PTZ00243 341 MNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 268 TDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTA 347
Cdd:PTZ00243 421 ADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLGHELTP 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 348 ERAFCVTAFYNILRRTvskFF--PSGMSQFAELLVSMRRITNFMMREEA---NVIDMSERRDEKAE-----EEQHLLKEV 417
Cdd:PTZ00243 501 EVVFPTIALLGVLRMP---FFmiPWVFTTVLQFLVSIKRISTFLECDNAtcsTVQDMEEYWREQREhstacQLAAVLENV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 418 EKRSY-PVGIGKEPDTLVEI--KALR-----------------------------------------------------A 441
Cdd:PTZ00243 578 DVTAFvPVKLPRAPKVKTSLlsRALRmlcceqcrptkrhpspsvvvedtdygspssasrhiveggtgggheatptsersA 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 442 RWGQEQHD--------LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASV 513
Cdd:PTZ00243 658 KTPKMKTDdffelepkVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATV 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFGLPMDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLEADLAQLGGGlETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 593 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEemlksgqDFAQLLVESTQNSGGGDeiitSPN 672
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA-------DFMRTSLYATLAAELKE----NKD 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 673 LsRQSSALSTKSSNGSSSSLESMVEKEKPKPSAVSS----------------QESRSGGQIGLSMYKKYFGAGCGVLVFV 736
Cdd:PTZ00243 887 S-KEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEggdgaaldaaagrlmtREEKASGSVPWSTYVAYLRFCGGLHAAG 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 737 VLIMLCIGTQILASGGDYFLSYWVKNTAS-SSTLDIYYFTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTA 815
Cdd:PTZ00243 966 FVLATFAVTELVTVSSGVWLSMWSTRSFKlSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGT 1045
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 816 LYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKTSRDV 895
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREI 1125
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 896 KRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDL-HSSGYYTFVsTSRAFGYYLDLFCVAYVISVILHNF 974
Cdd:PTZ00243 1126 RRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVvYSCSYLENV-ANRWLGVRVEFLSNIVVTVIALIGV 1204
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 975 FNPPL----HNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKD---------LDPEGD-----FNSPAE 1036
Cdd:PTZ00243 1205 IGTMLratsQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevphedmpeLDEEVDalerrTGMAAD 1284
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1037 K---------QPPKSWP---KEGKLVTKDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SY 1103
Cdd:PTZ00243 1285 VtgtvviepaSPTSAAPhpvQAGSLVFEGVQMRYREGL--PLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMvEV 1362
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1104 NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEG 1183
Cdd:PTZ00243 1363 CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEG 1442
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1184 GTNFSVGQRQLVCLARAIL-RENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1262
Cdd:PTZ00243 1443 GSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
1290 1300 1310
....*....|....*....|....*....|....*...
gi 28574259 1263 VEFGSPYELLTaSKAKVFHGMVMQTGKASFDHLLKVAE 1300
Cdd:PTZ00243 1523 AEMGSPRELVM-NRQSIFHSMVEALGRSEAKRFLQLVG 1559
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1047-1268 |
1.12e-129 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 397.63 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN-DGAILIDSLDTNDIGLHDLRS 1125
Cdd:cd03244 1 GDIEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILREN 1205
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1206 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1268
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
735-1275 |
3.97e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 356.01 E-value: 3.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 735 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD-IYYFTAINVGLV----ICALLRTLLFFNITMHSSTELHNTMFQ 809
Cdd:COG1132 23 LILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSaLLLLLLLLLGLAllraLLSYLQRYLLARLAQRVVADLRRDLFE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 810 GLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYL 889
Cdd:COG1132 103 HLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 890 KTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLF---CVAYV 966
Cdd:COG1132 183 RRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 967 ISVILHNFFNPPLhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEYKDLDPEGDfnSPAEKQPPKswPKE 1046
Cdd:COG1132 263 LLVGGLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP--DPPGAVPLP--PVR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLR 1124
Cdd:COG1132 338 GEIEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF-YdpTSGRILIDGVDIRDLTLESLR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1201
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARAL 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1202 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTAS 1275
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
434-632 |
2.95e-106 |
|
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: 334.05 E-value: 2.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA 511
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 SVRDNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILpDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 28574259 591 HVGRHLFDECMRGFLGKQ-LVILVTHQLQFLEDADLIVIMDKG 632
Cdd:cd03250 161 HVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
731-1022 |
3.00e-103 |
|
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: 330.44 E-value: 3.00e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 731 GVLVFVVLIMLCIGTQILASGGDYFLSYWV---------------KNTASSSTLD------IYYFTAINVGLVICALLRT 789
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWAnleeklndttdrvqgENSTNVDIEDldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 790 LLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPW 869
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 870 YLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVS 949
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 950 TSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
112-385 |
1.44e-102 |
|
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: 327.64 E-value: 1.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 112 PLLLAGLISEFSEHGNGHSYN-AQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 190
Cdd:cd18593 17 PIFLGKLIRYFEGNGSSISLTeAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 191 GQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQ 270
Cdd:cd18593 97 GQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 271 RVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTAERA 350
Cdd:cd18593 177 RIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERV 256
|
250 260 270
....*....|....*....|....*....|....*
gi 28574259 351 FCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRI 385
Cdd:cd18593 257 FVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
88-385 |
3.27e-101 |
|
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: 323.67 E-value: 3.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 88 VFGWRLIMSGITIAAlelgtratvPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRV 167
Cdd:cd18579 2 AGLLKLLEDLLSLAQ---------PLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 168 AVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYL 247
Cdd:cd18579 73 ALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 248 PLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLG 327
Cdd:cd18579 153 PLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 328 RIAIFVSLLGFVLGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 385
Cdd:cd18579 233 VLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLL-MLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
735-1022 |
2.10e-98 |
|
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: 316.37 E-value: 2.10e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 735 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD-----IYYFTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQ 809
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSsgyylGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 810 GLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYL 889
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 890 KTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVISV 969
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 970 ILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1043-1268 |
4.48e-97 |
|
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: 308.96 E-value: 4.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1043 WPKEGKLVTKDLSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLH 1121
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEdvhlkeeiselpsglqsiISEGGTNFSVGQRQLVCLARAI 1201
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1202 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1268
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
103-385 |
5.83e-93 |
|
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: 301.09 E-value: 5.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 103 LELGTRATVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSR 182
Cdd:cd18594 8 LEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 183 TSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRL 262
Cdd:cd18594 88 SALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 263 QTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGG 342
Cdd:cd18594 168 KTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 28574259 343 GELTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRI 385
Cdd:cd18594 248 NTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
700-1272 |
8.44e-85 |
|
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: 292.51 E-value: 8.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 700 KPKPSAVSSQESRSGGQ--IGLSM-YKKYFGAGCGVLVFVVLIMLC--IGTQILAsggDYFLSywvknTASSSTLdiyYF 774
Cdd:COG2274 129 EPTPEFDKRGEKPFGLRwfLRLLRrYRRLLLQVLLASLLINLLALAtpLFTQVVI---DRVLP-----NQDLSTL---WV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 775 TAINVGLVICA-----LLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFaNDLGQVDEVMP----AV 845
Cdd:COG2274 198 LAIGLLLALLFegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgsllTA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 846 MLDCIQIFLTLTgiicVLCVTNPW----YLINTFAMMLAFYYWRDFYLKTSRdvKRLEAVARspMYSHFSATLVGLPTIR 921
Cdd:COG2274 277 LLDLLFVLIFLI----VLFFYSPPlalvVLLLIPLYVLLGLLFQPRLRRLSR--EESEASAK--RQSLLVETLRGIETIK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 922 AMGAQQTLIGQYDNYQDLH----------SSGYYTFVSTSRAFGYYLDLFCVAYviSVILHNFfnpplhNAGQ------- 984
Cdd:COG2274 349 ALGAESRFRRRWENLLAKYlnarfklrrlSNLLSTLSGLLQQLATVALLWLGAY--LVIDGQL------TLGQliafnil 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 985 IGLAITQALGMTGMVQwgmrqsaELENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKswpkEGKLVTKDLSLRYEPDtnS 1064
Cdd:COG2274 421 SGRFLAPVAQLIGLLQ-------RFQDAKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGD--S 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1065 PCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMR 1142
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL-YepTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIR 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNL---DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1219
Cdd:COG2274 567 ENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1220 QTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1047-1285 |
1.66e-74 |
|
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: 248.28 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYepDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRS 1125
Cdd:cd03288 18 GEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILREN 1205
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1206 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtASKAKVFHGMVM 1285
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL-AQEDGVFASLVR 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1047-1272 |
3.49e-73 |
|
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: 243.29 E-value: 3.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsYN--DGAILIDSLDTNDIGLHDLR 1124
Cdd:cd03254 1 GEIEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-YDpqKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLW-KALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1203
Cdd:cd03254 77 SMIGVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1204 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1011-1272 |
1.17e-70 |
|
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: 247.75 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1011 NAMTSVERVLEYKDLDPEgdfnSPAEKQPPKSWPKEGKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAG 1090
Cdd:COG4988 303 NGIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1091 KSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLK 1166
Cdd:COG4988 376 KSTLLNLLLGFLPPYsGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1167 EEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLN 1246
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
250 260
....*....|....*....|....*.
gi 28574259 1247 TIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
75-653 |
1.87e-68 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 241.99 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 75 SGRKPSVLRVIGRVFG--WRLIMSGITIAALELGTRATVPLLLAGLISEFSEHGNGHSYNAqiYAVLLIACILASVLLTH 152
Cdd:COG1132 2 SKSPRKLLRRLLRYLRpyRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLL--LLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 153 PYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIH-FHFLWLGPLELLIAS-YFLYE 230
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALvVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 231 QIGMAsFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWE----RPFGKLIGQMRRSEM 306
Cdd:COG1132 160 DWRLA-LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 307 SSIRQMNLLRGILLSFeITLGRIAIFVSLLGFVLGGgELTAERafcVTAFYNILRRTVSKFFPSGM--SQFAELLVSMRR 384
Cdd:COG1132 239 RAARLSALFFPLMELL-GNLGLALVLLVGGLLVLSG-SLTVGD---LVAFILYLLRLFGPLRQLANvlNQLQRALASAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 385 ITNFMMREEanviDMSERRDEKAeeeqhlLKEVEKRsypvgigkepdtlVEIKALRARWGQEQHdlVLNNVNMSLRRGQL 464
Cdd:COG1132 314 IFELLDEPP----EIPDPPGAVP------LPPVRGE-------------IEFENVSFSYPGDRP--VLKDISLTIPPGET 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 465 VAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRT 530
Cdd:COG1132 369 VALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 531 VLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQL 609
Cdd:COG1132 449 AAKAAQAHEFIEALpDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRT 527
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 28574259 610 VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:COG1132 528 TIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARL 571
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
112-385 |
1.72e-67 |
|
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: 229.28 E-value: 1.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 112 PLLLAGLISeFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTG 191
Cdd:cd18595 17 PQLLKLLIN-FVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLSNSARKKSTVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 192 QVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQR 271
Cdd:cd18595 96 EIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 272 VRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGE--LTAER 349
Cdd:cd18595 176 IKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDnvLDAEK 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 28574259 350 AFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 385
Cdd:cd18595 256 AFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
735-1022 |
3.67e-65 |
|
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: 223.12 E-value: 3.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 735 FVVLIMLCIGTQILASGGDYFLSYW----VKNTASSSTLDIYY---FTAINVGLVICALLRTLLFFNITMHSSTELHNTM 807
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWsddpALNGTQDTEQRDYRlgvYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 808 FQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDF 887
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 888 YLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDL------F 961
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFlgnlivL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 962 CVAyVISVILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18603 241 FAA-LFAVLSRDSLSP-----GLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
735-1022 |
4.50e-65 |
|
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: 222.73 E-value: 4.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 735 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSSTLD------IYY---FTAINVGLVICALLRTLLFFNITMHSSTELHN 805
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPpsevsvLYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 806 TMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWR 885
Cdd:cd18604 81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 886 DFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDL----- 960
Cdd:cd18604 161 RLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLlgalf 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 961 --FCVAYVISVilhnffnpPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18604 241 sfATAALLVYG--------PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
735-1022 |
7.80e-64 |
|
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: 218.88 E-value: 7.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 735 FVVLIMLCIGTQILASGGDYFLSYWVKNTASSST---LDIYyfTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGL 811
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQgfyIGIY--AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 812 SRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKT 891
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 892 SRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLD-----------L 960
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDllgsllvlivaL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 961 FCVAYVISVilhnffnpplhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18606 239 LCVTRRFSI-----------SPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
108-385 |
9.47e-64 |
|
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: 218.86 E-value: 9.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 108 RATVPLLLAGLIS-------EFSEHGNGHSYnaqIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRL 180
Cdd:cd18597 13 QVLSPLLLKYLINfvedaylGGPPPSIGYGI---GYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAIYRKSLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 181 SRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKL 260
Cdd:cd18597 90 SGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 261 RLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLgriAIFVSLLGFV- 339
Cdd:cd18597 170 RKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSL---PVLASMLSFIt 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 28574259 340 --LGGGELTAERAFCVTAFYNILRRTVSkFFPSGMSQFAELLVSMRRI 385
Cdd:cd18597 247 yyATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1049-1261 |
3.38e-61 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 206.47 E-value: 3.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKI 1127
Cdd:cd03228 1 IEFKNVSFSY-PGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGH 1261
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1052-1283 |
4.74e-60 |
|
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: 205.93 E-value: 4.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPdtNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISI 1129
Cdd:cd03253 4 ENVTFAYDP--GRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-YdvSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1130 IPQEPVLFSGTMRYNLdpfeQY-----PDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1204
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1205 NRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtaSKAKVFHGM 1283
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL--AKGGLYAEM 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
56-653 |
1.06e-59 |
|
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: 219.32 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 56 DEFFQGWEDEVARCRR----KGDSGRKPSVLRVIGRVFGWRLIMSGITIAALELGTRA-TVPLLLAGLISEFSEHGNGHS 130
Cdd:COG2274 115 EEFAESWTGVALLLEPtpefDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAlATPLFTQVVIDRVLPNQDLST 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 131 YNaqIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLsNDLNRFDRclih 210
Cdd:COG2274 195 LW--VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIRE---- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 211 fhFLWLGPLELLIASYF--LYeqIGMASFYGIS---ILVLYLPLQTYLSRVTSKLRLQTALRT----DQRVRMMNEIISG 281
Cdd:COG2274 268 --FLTGSLLTALLDLLFvlIF--LIVLFFYSPPlalVVLLLIPLYVLLGLLFQPRLRRLSREEseasAKRQSLLVETLRG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 282 IQVIKMY--------TWERPFGKLIGQMRRSEMSSIRQMNLLRGIllsfeITLGRIAIFVslLG--FVLGG----GELTA 347
Cdd:COG2274 344 IETIKALgaesrfrrRWENLLAKYLNARFKLRRLSNLLSTLSGLL-----QQLATVALLW--LGayLVIDGqltlGQLIA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 348 erafcvtaFYNILRRTVSKF--FPSGMSQFAELLVSMRRITNFMmreeanvidmsERRDEKAEEEQHLLKEVEKRSypvg 425
Cdd:COG2274 417 --------FNILSGRFLAPVaqLIGLLQRFQDAKIALERLDDIL-----------DLPPEREEGRSKLSLPRLKGD---- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 426 igkepdtlVEIKALRARWGqEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------ 499
Cdd:COG2274 474 --------IELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqidp 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 -------SYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLAR 570
Cdd:COG2274 545 aslrrqiGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALpMGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 571 AVYRRADVYLLDDPLSAVDTHVGRHlFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDF 650
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAI-ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
...
gi 28574259 651 AQL 653
Cdd:COG2274 704 AEL 706
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1052-1272 |
6.22e-59 |
|
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: 202.85 E-value: 6.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1130
Cdd:cd03251 4 KNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQEPVLFSGTMRYNL---DPFEqyPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1047-1273 |
1.27e-58 |
|
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: 203.55 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDLRSK 1126
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENR 1206
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1207 ILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
452-632 |
1.46e-57 |
|
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: 198.32 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-----------------SYASQEPWLFNASVR 514
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfeatrsrnrysvAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFGLPMDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVG 593
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 28574259 594 RHLFDECMRGFL--GKQLVILVTHQLQFLEDADLIVIMDKG 632
Cdd:cd03290 177 DHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
731-1022 |
1.49e-57 |
|
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: 201.64 E-value: 1.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 731 GVLVFVVLIMLCIGTQILASGGDYFLSYWVK----NTASSSTLDIYYFTAIN----------------VGLVICALLRTL 790
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKqgsgNTTNNVDNSTVDSGNISdnpdlnfyqlvyggsiLVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 791 LFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWY 870
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 871 LINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVST 950
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 951 SRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1052-1286 |
3.65e-57 |
|
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: 197.76 E-value: 3.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRY--EPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKI 1127
Cdd:cd03249 4 KNVSFRYpsRPDVP---ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YdpTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGTMRYNL---DPFEQYPDDKlwKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1204
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKPDATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1205 NRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLtaSKAKVFHGMV 1284
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM--AQKGVYAKLV 235
|
..
gi 28574259 1285 MQ 1286
Cdd:cd03249 236 KA 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
989-1272 |
6.28e-57 |
|
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: 208.91 E-value: 6.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 989 ITQALGMTGMVQWGMRQsaelenAMTSVERVLEYKDLDPEgdfnsPAEK-QPPKSWPKEGKLVTKDLSLRYEPDtnSPcV 1067
Cdd:COG5265 308 LYIPLNFLGFVYREIRQ------ALADMERMFDLLDQPPE-----VADApDAPPLVVGGGEVRFENVSFGYDPE--RP-I 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL 1145
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-YdvTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 dpfeQY-----PDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1220
Cdd:COG5265 453 ----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1221 TDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG5265 529 TERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
734-1022 |
1.09e-56 |
|
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: 198.98 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 734 VFVVLImLCIGTQILASGGDYFLSYW----------VKNTASSSTLD---IYY---FTAINVGLVICALLRTLLFFNITM 797
Cdd:cd18602 1 VALVLA-LALLKQGLRVATDFWLADWteanhdvasvVFNITSSSLEDdevSYYisvYAGLSLGAVILSLVTNLAGELAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 798 HSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAvMLDCI--QIFLTLTGIICVLCVTnPWYLINTF 875
Cdd:cd18602 80 RAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPT-TLERLlrFLLLCLSAIIVNAIVT-PYFLIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 876 AMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFG 955
Cdd:cd18602 158 PIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 956 YYLD------LFCVAYV-ISVILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18602 238 IRLDylgaviVFLAALSsLTAALAGYISP-----SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
83-647 |
3.00e-56 |
|
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: 205.76 E-value: 3.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 83 RVIGRVFGWRLIMSGITIAALelgtratvpLLLAGLISEFSeHGNGHSYNAQIYAVLLIACILASVLLThpYMMGMM--H 160
Cdd:COG4988 17 RWLALAVLLGLLSGLLIIAQA---------WLLASLLAGLI-IGGAPLSALLPLLGLLLAVLLLRALLA--WLRERAafR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 161 LAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFH---FLW-LGPLELLIASYFLYEQIGMas 236
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLpqlFLAaLVPLLILVAVFPLDWLSGL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 237 fygisILVLYLPLqTYLSRVTSKLRLQTALRtDQRVRMMN------EIISGIQVIKMYTWERPFGKLIGQM----RRSEM 306
Cdd:COG4988 163 -----ILLVTAPL-IPLFMILVGKGAAKASR-RQWRALARlsghflDRLRGLTTLKLFGRAKAEAERIAEAsedfRKRTM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 307 SSIRqMNLLRGILLSFEITLGrIAIFVSLLGFVLGGGELTAERAFCV----TAFYNILRrTVSKFFPSGMsqfaELLVSM 382
Cdd:COG4988 236 KVLR-VAFLSSAVLEFFASLS-IALVAVYIGFRLLGGSLTLFAALFVlllaPEFFLPLR-DLGSFYHARA----NGIAAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 383 RRItnfmmreeANVIDMSERRDEKAEEEQHLLKEVEkrsypvgigkepdtlVEIKALRARWGQEQHdlVLNNVNMSLRRG 462
Cdd:COG4988 309 EKI--------FALLDAPEPAAPAGTAPLPAAGPPS---------------IELEDVSFSYPGGRP--ALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 463 QLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRY 528
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASDEEL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 529 RTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGK 607
Cdd:COG4988 444 EAALEAAGLDEFVAALpDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKG 522
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 28574259 608 QLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSG 647
Cdd:COG4988 523 RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
780-1274 |
1.00e-55 |
|
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: 204.57 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 780 GLVICALLRTLLFFNITMH----SSTELHN---TMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQI 852
Cdd:TIGR02203 59 VVIGLAVLRGICSFVSTYLlswvSNKVVRDirvRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 853 FLTLTGIICVLCVTNpWYLINTFAMML-----AFYYWRDFYLKTSRDVKRLEAVArspMYShFSATLVGLPTIRAMGAQQ 927
Cdd:TIGR02203 139 TLTVIGLFIVLLYYS-WQLTLIVVVMLpvlsiLMRRVSKRLRRISKEIQNSMGQV---TTV-AEETLQGYRVVKLFGGQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 928 TLIGQYDNYQDlHSSGYYTFVSTSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGlaiTQALGMTGMVQW--GMRQ 1005
Cdd:TIGR02203 214 YETRRFDAVSN-RNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAG---DFTAFITAMIALirPLKS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1006 SAELENAM----TSVERVLEYKDLDPEGDfnsPAEKQPPKSwpkEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKV 1081
Cdd:TIGR02203 290 LTNVNAPMqrglAAAESLFTLLDSPPEKD---TGTRAIERA---RGDVEFRNVTFRY-PGRDRP-ALDSISLVIEPGETV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1082 GIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfEQYPDDKLW 1157
Cdd:TIGR02203 362 ALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1158 KALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT 1237
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
490 500 510
....*....|....*....|....*....|....*..
gi 28574259 1238 VLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
451-655 |
4.02e-55 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 193.53 E-value: 4.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRT 530
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 531 VLKRCALERDL-ELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL 609
Cdd:cd03291 132 VVKACQLEEDItKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKT 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28574259 610 VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLV 655
Cdd:cd03291 212 RILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM 257
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
164-654 |
4.10e-52 |
|
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: 193.44 E-value: 4.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 164 KMRVAVssaiYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFD----RCLIHFHFLWLGPLELLIASYFLYEQIG--MASF 237
Cdd:COG4987 89 DLRVRL----YRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylRVLLPLLVALLVILAAVAFLAFFSPALAlvLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 238 YGISILVLYLpLQTYLSRVTSklRLQTALRTDQRVRMMnEIISGIQVIKMY----TWERPFGKLIGQMRRSEmssiRQMN 313
Cdd:COG4987 165 LLLAGLLLPL-LAARLGRRAG--RRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ----RRLA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 314 LLRGI---LLSFEITLGRIAIFVSLLGFVLGG---GELTAERAFCVTAFYNILRRtvskfFPSGMSQFAELLVSMRRItn 387
Cdd:COG4987 237 RLSALaqaLLQLAAGLAVVAVLWLAAPLVAAGalsGPLLALLVLAALALFEALAP-----LPAAAQHLGRVRAAARRL-- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 388 fmmreeANVIDMSERRDEKAEEEQHllkevekrsypvgigkEPDTLVEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAV 467
Cdd:COG4987 310 ------NELLDAPPAVTEPAEPAPA----------------PGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 468 IGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVRDNILFGLPM-DKQRYRTVLK 533
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 534 RCALERDLE-LLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVIL 612
Cdd:COG4987 447 RVGLGDWLAaLPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLL 525
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 28574259 613 VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 654
Cdd:COG4987 526 ITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
732-1022 |
6.09e-52 |
|
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: 185.04 E-value: 6.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 732 VLVFVVLIMLCIGTQILasgGDYFLSYWVKNTASSSTLDI-----YY---FTAINVGLVICALLRTLLFFNITMHSSTEL 803
Cdd:cd18605 1 LILILLSLILMQASRNL---IDFWLSYWVSHSNNSFFNFIndsfnFFltvYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 804 HNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYY 883
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 884 WRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQY----DNYQDlhssgyyTFVSTSRA---FGY 956
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYleklENNQR-------AQLASQAAsqwLSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 957 YLDL------FCVAyVISVILHnFFNPPLhNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18605 231 RLQLlgvlivTFVA-LTAVVQH-FFGLSI-DAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
135-385 |
6.38e-52 |
|
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: 184.69 E-value: 6.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 135 IYAVLLIAC-ILASVLLTHPYMMGMmHLAMKMRVAVSSAIYRKALRLSrtSLGGTTTGQVVNLLSNDLNR-FDRCLIhFH 212
Cdd:cd18592 40 LLVLGLFLTeLLRSLFFSLTWAISY-RTGIRLRGAVLGLLYKKILRLR--SLGDKSVGELINIFSNDGQRlFDAAVF-GP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 213 FLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWER 292
Cdd:cd18592 116 LVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 293 PFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGGGELTAERAFCVTAFYNILRRTVSkFFPSGM 372
Cdd:cd18592 196 PFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAV 274
|
250
....*....|...
gi 28574259 373 SQFAELLVSMRRI 385
Cdd:cd18592 275 KALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
112-385 |
3.16e-49 |
|
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: 176.97 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 112 PLLLAGLIsEFSEHGNGHSYNAQIYAVLLIA-CILASVLLTHpYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTT 190
Cdd:cd18598 17 PLLLNKLV-EFLEDSSEPLSDGYLYALGLVLsSLLGALLSSH-YNFQMNKVSLKVRAALVTAVYRKALRVRSSSLSKFST 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 191 GQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLS----RVTSKLRLQtal 266
Cdd:cd18598 95 GEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAkrigALSEKMMKH--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 267 rTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGriaIFVSLLGF---VLGGG 343
Cdd:cd18598 172 -KDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTP---VLISILTFatyVLMGN 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 28574259 344 ELTAERAFCVTAFYNILrrtvskFFPsgMSQFA-------ELLVSMRRI 385
Cdd:cd18598 248 TLTAAKVFTSLALFNML------IGP--LNAFPwvlnglvEAWVSLKRL 288
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
112-385 |
3.43e-49 |
|
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: 177.30 E-value: 3.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 112 PLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRL----------- 180
Cdd:cd18596 17 PFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksse 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 181 --------SRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTY 252
Cdd:cd18596 97 skkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 253 LSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLrGILLSFeITLGrIAIF 332
Cdd:cd18596 177 LAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL-DLLLSL-LWFL-IPIL 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 333 VSLLGF----VLGGGELTAERAF-CVTAFyNILRRTVSkFFPSGMSQFAELLVSMRRI 385
Cdd:cd18596 254 VTVVTFatytLVMGQELTASVAFtSLALF-NMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
793-1273 |
2.21e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 182.23 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 793 FNITM-HSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPavmlDCIQIFL-TLTGIICVLC--VTNP 868
Cdd:TIGR00958 225 FNYTMaRINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLS----LNVNVLLrNLVMLLGLLGfmLWLS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 869 WYL-----INTFAMMLAFYYWRDFYLKTSRDVKrlEAVARSPMYSHfsATLVGLPTIRAMGAQQTligqydnyqdlHSSG 943
Cdd:TIGR00958 301 PRLtmvtlINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFAAEEG-----------EASR 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 944 YYTFVSTSRAFGYYLDLFCVAYV-ISVILHNF-FNPPLHNAGQigLAITQALGMTGMVQWGMRQS-------------AE 1008
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYAGYLwTTSVLGMLiQVLVLYYGGQ--LVLTGKVSSGNLVSFLLYQEqlgeavrvlsyvySG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1009 LENAMTSVERVLEYKDLDPEgdFNSPAEKQPPkswPKEGKLVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTG 1088
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPN--IPLTGTLAPL---NLEGLIEFQDVSFSYPNRPDVP-VLKGLTFTLHPGEVVALVGPSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1089 AGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHL 1165
Cdd:TIGR00958 518 SGKSTVAALLQNL-YqpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1166 KEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATirNKFKDCTVLTIAHRL 1245
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRL 674
|
490 500
....*....|....*....|....*...
gi 28574259 1246 NTIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1008-1273 |
7.56e-47 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 180.52 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1008 ELENAMTSVERVLEYKdLDPEGDFNSPAEKQPPKSWPKEGKLVTKDLSLRYEPdTNSPcVLKGLSFTIQPMEKVGIVGRT 1087
Cdd:TIGR03796 438 ELEGDLNRLDDVLRNP-VDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSP-LEPP-LIENFSLTLQPGQRVALVGGS 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1088 GAGKSS---LINALFRLSynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALE 1161
Cdd:TIGR03796 515 GSGKSTiakLVAGLYQPW--SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1162 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfKDCTVLTI 1241
Cdd:TIGR03796 591 DAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIV 668
|
250 260 270
....*....|....*....|....*....|..
gi 28574259 1242 AHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:TIGR03796 669 AHRLSTIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1054-1274 |
2.09e-46 |
|
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: 166.89 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1054 LSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGLHDLRSKISIIPQ 1132
Cdd:cd03252 6 VRFRYKPD--GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1133 EPVLFSGTMRYNLDPFEQYPD-DKLWKA--LEDVHlkEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILV 1209
Cdd:cd03252 84 ENVLFNRSIRDNIALADPGMSmERVIEAakLAGAH--DFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1210 MDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1047-1263 |
1.49e-44 |
|
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: 160.83 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsY--NDGAILIDSLDTNDIGLHDLR 1124
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL-YkpTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEPVLFSGTMRYNLDPFEQYPDD-KLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1203
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLADDeRILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1204 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVV 1263
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
434-633 |
1.72e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 158.70 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 500
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLFNASVRDNIlfglpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYL 580
Cdd:cd03228 80 YVPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 581 LDDPLSAVDTHvGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGH 633
Cdd:cd03228 120 LDEATSALDPE-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1005-1274 |
1.00e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 169.13 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1005 QSAELENAMTSVERVLEYKDlDPEGDFNSpaEKQPPKSwpkeGKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIV 1084
Cdd:PRK10790 304 QQSMLQQAVVAGERVFELMD-GPRQQYGN--DDRPLQS----GRIDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1085 GRTGAGKSSLINALfrLSY---NDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALE 1161
Cdd:PRK10790 374 GHTGSGKSTLASLL--MGYyplTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1162 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI 1241
Cdd:PRK10790 452 TVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
250 260 270
....*....|....*....|....*....|...
gi 28574259 1242 AHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK10790 532 AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1006-1257 |
1.91e-43 |
|
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: 167.08 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1006 SAELENAMTSVERVLEYKDLdpegdfnsPAEKQPPKSWPKEGKLVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVG 1085
Cdd:TIGR02857 287 RADGVAAAEALFAVLDAAPR--------PLAGKAPVTAAPASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1086 RTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNLDPFEQY-PDDKLWKALEDV 1163
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFvDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1164 HLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH 1243
Cdd:TIGR02857 436 GLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 28574259 1244 RLNTIMDSDKVLVM 1257
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1006-1272 |
6.65e-43 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 166.35 E-value: 6.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1006 SAELENAMTSVERVLEYKDLDPEGDfNSPAEKQPPKswpkeGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVG 1085
Cdd:PRK11176 305 NAQFQRGMAACQTLFAILDLEQEKD-EGKRVIERAK-----GDIEFRNVTFTY-PGKEVP-ALRNINFKIPAGKTVALVG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1086 RTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL--DPFEQYPDDKLWKALED 1162
Cdd:PRK11176 377 RSGSGKSTIANLLTRFyDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARM 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1163 VHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIA 1242
Cdd:PRK11176 457 AYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA 536
|
250 260 270
....*....|....*....|....*....|
gi 28574259 1243 HRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:PRK11176 537 HRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1047-1284 |
1.33e-42 |
|
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: 167.06 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDtnSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalFRL-----SYNDGAILIDSLDTNDIGLH 1121
Cdd:TIGR03797 450 GAIEVDRVTFRYRPD--GPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLllgfeTPESGSVFYDGQDLAGLDVQ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1201
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1202 LRENRILVMDEATANVDPQTDALIQATIrNKFKdCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELltASKAKVFH 1281
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESL-ERLK-VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDEL--MAREGLFA 679
|
...
gi 28574259 1282 GMV 1284
Cdd:TIGR03797 680 QLA 682
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
755-1245 |
3.51e-42 |
|
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: 163.30 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 755 FLSYWVKNTASSSTLDIYYFTAInVGLVICALLRTLLFF-------NITMHSSTELHNTMFQGLSRTALYFFHTNPSGRI 827
Cdd:TIGR02868 34 GVSAWLISRAAEMPPVLYLSVAA-VAVRAFGIGRAVFRYlerlvghDAALRSLGALRVRVYERLARQALAGRRRLRRGDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 828 LNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMML-AFYYWRDFYLKTSRDVKRLEAVARSPM 906
Cdd:TIGR02868 113 LGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLlAGFVAPLVSLRAARAAEQALARLRGEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 907 YSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDlhssgYYTFVSTSRAFGYYLD-----LFCVAYVISVILhnfFNPPLHN 981
Cdd:TIGR02868 193 AAQLTDALDGAAELVASGALPAALAQVEEADR-----ELTRAERRAAAATALGaaltlLAAGLAVLGALW---AGGPAVA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 982 AGQIG-----------LAITQALG-MTGMVQwgmrqsaELENAMTSVERVLEYkdLDPEGDFNSPAEKQPPKSWPKEGKL 1049
Cdd:TIGR02868 265 DGRLApvtlavlvllpLAAFEAFAaLPAAAQ-------QLTRVRAAAERIVEV--LDAAGPVAEGSAPAAGAVGLGKPTL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1050 VTKDLSLRYEPDtnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKIS 1128
Cdd:TIGR02868 336 ELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
490 500 510
....*....|....*....|....*....|....*...
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL 1245
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1071-1274 |
6.18e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 163.48 E-value: 6.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNdGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL--- 1145
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgF-LPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 DPfeQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALI 1225
Cdd:PRK11174 447 NP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 28574259 1226 QATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1046-1262 |
1.36e-41 |
|
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: 152.62 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1046 EGKLVTKDLSLRY--EPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHD 1122
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL---VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1123 LRSKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAI 1201
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 1202 LRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1262
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
450-653 |
4.48e-41 |
|
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: 151.48 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDN 516
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 ILFGLP-MDKQRYRTVLKRC-ALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGR 594
Cdd:cd03252 96 IALADPgMSMERVIEAAKLAgAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 595 HLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:cd03252 175 HAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1046-1272 |
7.93e-40 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 157.04 E-value: 7.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1046 EGKLVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLR 1124
Cdd:PRK13657 332 KGAVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEPVLFSGTMRYNLD-PFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1203
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1204 ENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
444-638 |
9.07e-40 |
|
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: 146.97 E-value: 9.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 444 GQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFN 510
Cdd:cd03245 14 NQEIP--ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFGLPM-DKQRYRTVLKRCALErDLELLHGDG--TIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:cd03245 92 GTLRDNITLGAPLaDDERILRAAELAGVT-DFVNKHPNGldLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 588 VDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACG 638
Cdd:cd03245 171 MDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
722-1022 |
3.15e-39 |
|
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: 149.18 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 722 YKKYFGAGCGVLVFVVLIMLCIGTQILASGGDYFL---SYWVKNTASS-----------STLDIYYFTAINVG----LVI 783
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPesssntyavivTFTSSYYVFYIYVGvadsLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 784 CALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVL 863
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 864 CVTNPWYLINTFAMMLAFYYWRDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSG 943
Cdd:cd18600 166 SILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTAN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 944 YYTFVSTSRAFGYYLDLFCVAYVISV----ILHNFFNPplhnaGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERV 1019
Cdd:cd18600 246 WFLYLSTLRWFQMRIEMIFVIFFTAVtfisIGTTGDGE-----GRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
...
gi 28574259 1020 LEY 1022
Cdd:cd18600 321 FKF 323
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1047-1272 |
1.86e-38 |
|
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: 154.51 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRS 1125
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLKDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSGTMRYNL--DPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1203
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1204 ENRILVMDEATANVDPQTDALIQATIRNkFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1013-1273 |
2.46e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 152.29 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1013 MTSVERVLEYKDLDPEGDFNSPAEKQPpkswpKEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKS 1092
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAA-----DQVSLTLNNVSFTY-PDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1093 SLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTMRYNL---DPfeQYPDDKLWKALEDVHLkEE 1168
Cdd:PRK11160 381 TLLQLLTRaWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1169 ISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTI 1248
Cdd:PRK11160 458 LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
250 260
....*....|....*....|....*
gi 28574259 1249 MDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
434-653 |
2.54e-38 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 143.53 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS------ 503
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrDYTLASlrrqig 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ---QEPWLFNASVRDNILFGLP-MDKQRYRTVLKR-CALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADV 578
Cdd:cd03251 80 lvsQDVFLFNDTVAENIAYGRPgATREEVEEAARAaNAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 579 YLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:cd03251 160 LILDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
114-629 |
2.60e-38 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 151.67 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 114 LLAGLISEFSEHGNG-HSYNAQIYAVLLIACILASVLLTHPYMMgmMHLAMKMRVAVSSAIYRKALRLSRTSLGGTTTGQ 192
Cdd:TIGR02857 25 LLARVVDGLISAGEPlAELLPALGALALVLLLRALLGWLQERAA--ARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 193 VVNLLSNDL----NRFDRCLIHFHFLWLGPLELLIAsyflyeqIGMASFYGISILVLYLPLQTYLSRVTSKlrlQTALRT 268
Cdd:TIGR02857 103 LATLALEGVealdGYFARYLPQLVLAVIVPLAILAA-------VFPQDWISGLILLLTAPLIPIFMILIGW---AAQAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 269 DQRVRMMN-------EIISGIQVIKMY---TWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGrIAIFVSLLGF 338
Cdd:TIGR02857 173 RKQWAALSrlsghflDRLRGLPTLKLFgraKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS-VALVAVYIGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 339 VLGGGELTAERAFCV----TAFYNILRRTVSKFFPS--GMSQFAELlvsmrritnfmmreeANVIDMSERrdEKAEEEqh 412
Cdd:TIGR02857 252 RLLAGDLDLATGLFVlllaPEFYLPLRQLGAQYHARadGVAAAEAL---------------FAVLDAAPR--PLAGKA-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 413 llkevekrsyPVGIGkePDTLVEIKALRARwgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGS 492
Cdd:TIGR02857 313 ----------PVTAA--PASSLEFSGVSVA--YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 493 VQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDL-ELLHGDGTIVGERGAS 557
Cdd:TIGR02857 379 IAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVaALPQGLDTPIGEGGAG 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 558 LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIM 629
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
429-659 |
3.39e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.31 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 429 EPDTLVEIKAlrarwgqeqHDLV---------LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-- 497
Cdd:PRK11174 343 ASNDPVTIEA---------EDLEilspdgktlAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGie 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 -----------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRC-ALERDLELLHGDGTIVGERGASLSGGQRA 564
Cdd:PRK11174 413 lreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAwVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD---ECMRGflgkQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYE 641
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQalnAASRR----QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYA 568
|
250
....*....|....*...
gi 28574259 642 EMLKSGQDFAQLLVESTQ 659
Cdd:PRK11174 569 ELSQAGGLFATLLAHRQE 586
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
138-385 |
3.04e-37 |
|
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: 142.76 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 138 VLLIACILASVLLTHPYMMGMMHlAMKMRVAVSSAIYRKALRLSRTSLGG--TTTGQVVNLLSNDLNRFDRCLIHFHFLW 215
Cdd:cd18591 61 ILFLALLLQATFSQASYHIVIRE-GIRLKTALQAMIYEKALRLSSWNLSSgsMTIGQITNHMSEDANNIMFFFWLIHYLW 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 216 LGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFG 295
Cdd:cd18591 140 AIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 296 KLIGQMRRSEMSSIRQMNLLRgILLSFeITLGrIAIFVSLLGFVL----GGGELTAERAFCVTAFYNILrrTVSKF-FPS 370
Cdd:cd18591 220 DKIQEARRKELKLLLKDAVYW-SLMTF-LTQA-SPILVTLVTFGLypylEGEPLTAAKAFSSLALFNQL--TVPLFiFPV 294
|
250
....*....|....*
gi 28574259 371 GMSQFAELLVSMRRI 385
Cdd:cd18591 295 VIPILINAVVSTRRL 309
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
451-647 |
6.81e-37 |
|
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: 139.28 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNI 517
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLPMDKQryrTVLKRCALE-------RDLEllHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:cd03254 98 RLGRPNATD---EEVIEAAKEagahdfiMKLP--NGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 591 HVgRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSG 647
Cdd:cd03254 173 ET-EKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
442-653 |
6.88e-37 |
|
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: 139.29 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 442 RWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWL 508
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirEVTLDSlrraigvvpQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 509 FNASVRDNILFGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:cd03253 87 FNDTIGYNIRYGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 587 AVDTHVGRHLFdECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:cd03253 167 ALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1032-1272 |
1.58e-36 |
|
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: 146.82 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1032 NSPAEKQPPkSWPK-EGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL----------FR 1100
Cdd:COG4618 314 AVPAEPERM-PLPRpKGRLSVENLTVVP-PGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptagsVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1101 LsynDGAIlIDSLDTNDIGLHdlrskISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKA--LEDVHlkEEISELPSGLQS 1178
Cdd:COG4618 391 L---DGAD-LSQWDREELGRH-----IGYLPQDVELFDGTIAENIARFGDADPEKVVAAakLAGVH--EMILRLPDGYDT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1179 IISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVM 1257
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVL 539
|
250
....*....|....*
gi 28574259 1258 DAGHVVEFGSPYELL 1272
Cdd:COG4618 540 RDGRVQAFGPRDEVL 554
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
451-653 |
1.67e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 138.44 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------SYASQEPWLFNASVRDNI 517
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqiGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH 595
Cdd:cd03249 98 RYGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 596 L---FDECMRGFlgkqLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:cd03249 178 VqeaLDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1049-1273 |
3.17e-36 |
|
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: 137.08 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHDLRS 1125
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT--SGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPV--LFSGT---------MRYNLDPFEQypDDKLWKALEDVHLKE----EISELpSGlqsiiseggtnfsvG 1190
Cdd:COG1122 76 KVGLVFQNPDdqLFAPTveedvafgpENLGLPREEI--RERVEEALELVGLEHladrPPHEL-SG--------------G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1191 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1268
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTP 218
|
....*
gi 28574259 1269 YELLT 1273
Cdd:COG1122 219 REVFS 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1049-1262 |
1.59e-35 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 133.11 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGLHDLRSKI 1127
Cdd:cd03246 1 LEVENVSFRY-PGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1262
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
448-634 |
3.47e-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: 134.14 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 448 HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVR 514
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFGLPMDKQRYRTVLKRCALERDL--ELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 592
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAHAHSFisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 28574259 593 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 634
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
430-646 |
2.08e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SY 501
Cdd:COG1121 3 MMPAIELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQE---PWLFNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLHGDGTIVGErgasLSGGQRARICLAR 570
Cdd:COG1121 80 VPQRaevDWDFPITVRDVVLMGRygrrglfrRPSRADREAVDE--ALER-VGLEDLADRPIGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 571 AVYRRADVYLLDDPLSAVDtHVGRHLFDECMRGF--LGKqLVILVTHQLQFLED-ADLIVIMDKGHVsACGTYEEMLKS 646
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVD-AATEEALYELLRELrrEGK-TILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEEVLTP 228
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
109-385 |
3.00e-34 |
|
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: 133.49 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 109 ATVPLLLAGLISeFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIYRKALRLSRTSLGGT 188
Cdd:cd18559 14 FSGPSNLWLLLW-FDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 189 TTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIGMASFYGISILVLYLPLQTYLSRVTSKLRLQTALRT 268
Cdd:cd18559 93 PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 269 DQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLLGFVLGG--GELT 346
Cdd:cd18559 173 DPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLV 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 28574259 347 AERAFCVTAFYNILRRTVsKFFPSGMSQFAELLVSMRRI 385
Cdd:cd18559 253 ALKVFYSLALTTYLNWPL-NMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1049-1260 |
3.32e-34 |
|
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: 130.67 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPD-TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIdsldtndiglhdlRSK 1126
Cdd:cd03250 1 ISVEDASFTWDSGeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENR 1206
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1207 ILVMDEATANVDPQT-DALIQATIRNKFKDC-TVLTIAHRLNTIMDSDKVLVMDAG 1260
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
452-586 |
5.52e-34 |
|
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: 127.76 E-value: 5.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------SYASQEPWLFNA-SVRDNI 517
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 518 LFGLPMDKQRYRTVLKRC--ALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAeeALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
412-617 |
1.11e-33 |
|
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: 137.49 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 412 HLLKEVEKRSYPVGIGKEP--------DTLVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL 483
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPaagavglgKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 484 GELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLE-LLHGDG 548
Cdd:TIGR02868 383 GLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRaLPDGLD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 549 TIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKqLVILVTHQL 617
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR-TVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
434-639 |
2.32e-33 |
|
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: 128.77 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 500
Cdd:cd03244 3 IEFKNVSLRYRPNL-PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLFNASVRDNI-LFGLPMDKQRYRtVLKRCAL-ERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADV 578
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLkEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 579 YLLDDPLSAVDTH-------VGRHLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGT 639
Cdd:cd03244 161 LVLDEATASVDPEtdaliqkTIREAFKDCT--------VLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
451-629 |
4.86e-33 |
|
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: 127.59 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SYASQE----PWLfnaSVRDNIL 518
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvtgpgpdrGYVFQQdallPWL---TVLDNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 519 FGLpmdkqRYRTVLKRCALERDLELLHgdgtIVGERGAS------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:cd03293 96 LGL-----ELQGVPKAEARERAEELLE----LVGLSGFEnayphqLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 28574259 593 GRHLFDECMRGFLGKQL-VILVTHQLQ---FLedADLIVIM 629
Cdd:cd03293 167 REQLQEELLDIWRETGKtVLLVTHDIDeavFL--ADRVVVL 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
434-646 |
6.65e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 6.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 501
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQEPWLF-NASVRDNI-----LFGLPMD--KQRYRTVLKRCALERDLellhgdgtivGERGASLSGGQRARICLARAVY 573
Cdd:COG1131 78 VPQEPALYpDLTVRENLrffarLYGLPRKeaRERIDELLELFGLTDAA----------DRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 574 RRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:COG1131 148 HDPELLILDEPTSGLDP-EARRELWELLRELAAEGKtVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1049-1266 |
6.77e-33 |
|
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: 125.89 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGlHDLRSKI 1127
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGTMRYNLdpfeqypddklwkaledvhlkeeiselpsglqsiisegGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFG 1266
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-1274 |
1.06e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 138.62 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 406 KAEEEQHLLKEVEKRSYPVGIGKEPDTL-----VEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQ 480
Cdd:PTZ00265 350 KSLEATNSLYEIINRKPLVENNDDGKKLkdikkIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 481 AILGELPPESGSVQVS--------------GKYSYASQEPWLFNASVRDNILFGL--------------------PMDKQ 526
Cdd:PTZ00265 430 LIERLYDPTEGDIIINdshnlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsQENKN 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 527 RYRTVLKRCALERDL--------ELLHGDG-------------------------------TIVGERGASLSGGQRARIC 567
Cdd:PTZ00265 510 KRNSCRAKCAGDLNDmsnttdsnELIEMRKnyqtikdsevvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRIS 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 568 LARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQ--LVILVTHQLQFLEDADLIVIM---DKGHVSAC----- 637
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNEnrITIIIAHRLSTIRYANTIFVLsnrERGSTVDVdiige 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 638 ---------------------------------------GTYEEMLKSGQDFAQLLVE----STQNSGGGDEIITSPNls 674
Cdd:PTZ00265 669 dptkdnkennnknnkddnnnnnnnnnnkinnagsyiieqGTHDALMKNKNGIYYTMINnqkvSSKKSSNNDNDKDSDM-- 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 675 rQSSALSTK--------SSNGSSSSLESMVEKEKPKPSAVSSQESRSGGQIGL--SMYKKYFGAGCGVLVFVVLI----- 739
Cdd:PTZ00265 747 -KSSAYKDSergydpdeMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFlrNLFKRKPKAPNNLRIVYREIfsykk 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 740 -MLCIGTQILASGGDY--FLSYWVK---------NTASSSTLDIYYFTAINVGLVICALLRTllFFNITMHSSTE--LHN 805
Cdd:PTZ00265 826 dVTIIALSILVAGGLYpvFALLYAKyvstlfdfaNLEANSNKYSLYILVIAIAMFISETLKN--YYNNVIGEKVEktMKR 903
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 806 TMFQGLSRTALYFFH--TNPSGRILNRFANDLgqvdEVMPAVMLDCIQIFLTLTGIICVLCVTNpWYLINTFAMMLAFYY 883
Cdd:PTZ00265 904 RLFENILYQEISFFDqdKHAPGLLSAHINRDV----HLLKTGLVNNIVIFTHFIVLFLVSMVMS-FYFCPIVAAVLTGTY 978
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 884 W---RDFYLKT----SRDVKRLEAVARSPMYSHFS-------------ATLVGLPTIRAMGAQQ---TLIGQYDNYQD-- 938
Cdd:PTZ00265 979 FifmRVFAIRArltaNKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIYGLEDyfcNLIEKAIDYSNkg 1058
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 939 -----LHSSGYYTFVSTSR----AFGYYLDLFCVAYviSVILHNFFNPPLHNAGQIGLAITQALGMTGmvqwgmrqsaEL 1009
Cdd:PTZ00265 1059 qkrktLVNSMLWGFSQSAQlfinSFAYWFGSFLIRR--GTILVDDFMKSLFTFLFTGSYAGKLMSLKG----------DS 1126
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1010 ENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKSWPKEGKLVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGA 1089
Cdd:PTZ00265 1127 ENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVP-IYKDLTFSCDSKKTTAIVGETGS 1205
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1090 GKSSLINALFR-------------------------------------------------------LSYNDGAILIDSLD 1114
Cdd:PTZ00265 1206 GKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVD 1285
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1115 TNDIGLHDLRSKISIIPQEPVLFsgtmryNLDPFEQYPDDKLWKALEDVH-------LKEEISELPSGLQSIISEGGTNF 1187
Cdd:PTZ00265 1286 ICDYNLKDLRNLFSIVSQEPMLF------NMSIYENIKFGKEDATREDVKrackfaaIDEFIESLPNKYDTNVGPYGKSL 1359
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQAT---IRNKfKDCTVLTIAHRLNTIMDSDKVLVMD----AG 1260
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDK-ADKTIITIAHRIASIKRSDKIVVFNnpdrTG 1438
|
1130
....*....|....*
gi 28574259 1261 HVVEF-GSPYELLTA 1274
Cdd:PTZ00265 1439 SFVQAhGTHEELLSV 1453
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
446-653 |
2.23e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.18 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 446 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YSYA---------SQEPWLFNAS 512
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadYSEAalrqaisvvSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGLP-MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH 591
Cdd:PRK11160 430 LRDNLLLAAPnASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 592 VGRHLFDECMRGFLGKQLvILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:PRK11160 510 TERQILELLAEHAQNKTV-LMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
434-638 |
2.95e-32 |
|
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: 125.32 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 502
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCALErdLELLHGDGTIvGERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVREL--LELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 582 DDPLSAVDTHVGRHLFDEcMRGFLGKQ--LVILVTH-QLQFLEDADLIVIMDKGHVSACG 638
Cdd:cd03259 155 DEPLSALDAKLREELREE-LKELQRELgiTTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1052-1266 |
4.20e-32 |
|
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: 125.31 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDL---RSKI 1127
Cdd:cd03257 5 KNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlKPTSGSIIFDGKDLLKLSRRLRkirRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPvlFSgtmryNLDP------------FEQYPDDKLWKALEDVHLKEEISELPSG-LQSIISEggtnFSVGQRQL 1194
Cdd:cd03257 85 QMVFQDP--MS-----SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1195 VCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFG 1266
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
430-632 |
4.92e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 4.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------YS 500
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQE----PWLfnaSVRDNILFGLPMdkqryRTVLKRCALERDLELLHgdgtIVGERGA------SLSGGQRARICLAR 570
Cdd:COG1116 84 VVFQEpallPWL---TVLDNVALGLEL-----RGVPKAERRERARELLE----LVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 571 AVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ---FLedADLIVIMDKG 632
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLR--LWQETgktVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
434-642 |
2.87e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.41 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYAS-------- 503
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPprerrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 --QEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCalERDLELLHGDGtiVGERGAS-LSGGQRARICLARAVYRRADVY 579
Cdd:COG1118 80 vfQHYALFpHMTVAENIAFGLRVRPPSKAEIRARV--EELLELVQLEG--LADRYPSqLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 580 LLDDPLSAVDTHVG-------RHLFDECmrgflgKQLVILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 642
Cdd:COG1118 156 LLDEPFGALDAKVRkelrrwlRRLHDEL------GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDE 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
451-646 |
4.00e-31 |
|
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: 130.25 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV------------QVSGKY-SYASQEPWLFNASVRDNI 517
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRHiGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 -LFGLPmDKQRyrtVLKRCAL----ERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThV 592
Cdd:COG4618 427 aRFGDA-DPEK---VVAAAKLagvhEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-E 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 593 GRHLFDECMRGFlgKQ---LVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:COG4618 502 GEAALAAAIRAL--KArgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1068-1215 |
6.24e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 119.29 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSG-TMRYNL 1145
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1146 -------DPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADR-------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
434-646 |
1.40e-30 |
|
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: 121.07 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGqEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---------------- 497
Cdd:cd03261 1 IELRGLTKSFG-GRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 KYSYASQEPWLFNA-SVRDNILFGLPMDKQRYRTVLKRCALERdLELlhgdgtiVGERG------ASLSGGQRARICLAR 570
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLSEEEIREIVLEK-LEA-------VGLRGaedlypAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 571 AVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDP-IASGVIDDLIRS-LKKELgltSIMVTHDLDTaFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1050-1261 |
3.09e-30 |
|
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: 119.49 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1050 VTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL-FRLSYNDGAILIDSLDTNDIGLHDLRSKIS 1128
Cdd:cd03225 1 ELKNLSFSY-PDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEP------------VLFsGTMRYNLDPFEQypDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1196
Cdd:cd03225 79 LVFQNPddqffgptveeeVAF-GLENLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1197 LARAILRENRILVMDEATANVDPQTDALIQATIRnKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGH 1261
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1049-1281 |
4.44e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.15 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKI 1127
Cdd:COG1120 2 LEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVL-FSGT------M-RYN-LDPFEQYPDD---KLWKALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQ 1191
Cdd:COG1120 78 AYVPQEPPApFGLTvrelvaLgRYPhLGLFGRPSAEdreAVEEALERTgleHLADrPVDEL-SG--------------GE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDP--QTDALiqATIR--NKFKDCTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFG 1266
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLahQLEVL--ELLRrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
250
....*....|....*.
gi 28574259 1267 SPYELLTASK-AKVFH 1281
Cdd:COG1120 221 PPEEVLTPELlEEVYG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1049-1277 |
4.97e-30 |
|
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: 126.17 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND----GAILIDSLDTNDIGLHDLR 1124
Cdd:COG1123 5 LEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrisGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEPvlfsgtmRYNLDP---FEQYPDDKLWKALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLAR 1199
Cdd:COG1123 83 RRIGMVFQDP-------MTQLNPvtvGDQIAEALENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1200 AILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 28574259 1277 A 1277
Cdd:COG1123 236 A 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
434-645 |
5.54e-30 |
|
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: 119.36 E-value: 5.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW------ 507
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK-DITKKNLRelrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 ----------LFNASVRDNILFG-----LPMD--KQRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLAR 570
Cdd:COG1122 78 glvfqnpddqLFAPTVEEDVAFGpenlgLPREeiRERVEEALELVGLE---HLAD-------RPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 571 AVYRRADVYLLDDPLSAVDtHVGRHLFDECMRGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 645
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLD-PRGRRELLELLKRLNKEGKtVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
434-642 |
1.18e-29 |
|
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: 118.60 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 502
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLF-NASVRDNILFGLPMDKQRYRT--VLKRCALERDLELLHGDGtiVGER-GASLSGGQRARICLARAVYRRADV 578
Cdd:cd03296 80 FQHYALFrHMTVFDNVAFGLRVKPRSERPpeAEIRAKVHELLKLVQLDW--LADRyPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 579 YLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 642
Cdd:cd03296 158 LLLDEPFGALDAKVRKEL-----RRWL-RRLhdelhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1052-1261 |
3.26e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 114.65 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1130
Cdd:cd00267 3 ENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLlKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQepvlfsgtmrynldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRILVM 1210
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1211 DEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGH 1261
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
435-634 |
3.54e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.07 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------Y----SY 501
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppeWrrqvAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQEPWLFNASVRDNILFGLPMDKQRYrtvlKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKF----DRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 582 DDPLSAVDTHvGRHLFDECMRGFLGKQ--LVILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:COG4619 155 DEPTSALDPE-NTRRVEELLREYLAEEgrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1060-1275 |
3.76e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.44 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1060 PDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFS 1138
Cdd:PRK10789 324 PQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 GTMRYNL---DPFEQYPDDKLWKALEDVHlkEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:PRK10789 403 DTVANNIalgRPDATQQEIEHVARLASVH--DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1216 NVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTAS 1275
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
451-654 |
4.14e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.22 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLFNASVRDNI 517
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGL---PMDKQRYRTVlKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgR 594
Cdd:TIGR00958 576 AYGLtdtPDEEIMAAAK-AANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-E 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 595 HLFDECMRgfLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 654
Cdd:TIGR00958 654 QLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
430-642 |
4.88e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.20 E-value: 4.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY---------- 499
Cdd:COG3842 2 AMPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglppekrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 ------SYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDGtiVGERGAS-LSGGQRARICLARA 571
Cdd:COG3842 79 vgmvfqDYA-----LFpHLTVAENVAFGLRMRGVPKAEIRAR--VAELLELVGLEG--LADRYPHqLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 572 VYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEE 642
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRR--LQRELgitFIYVTHD---QEEAlalaDRIAVMNDGRIEQVGTPEE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
430-646 |
7.52e-29 |
|
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: 116.23 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS----- 503
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ----------QEPWLFNA-SVRDNILFGLpmdkqRYRTVLKRcALERDL--ELLHgdgtIVGERGA------SLSGGQRA 564
Cdd:COG1127 79 elrrrigmlfQGGALFDSlTVFENVAFPL-----REHTDLSE-AEIRELvlEKLE----LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTY 640
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRE-LRDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....*.
gi 28574259 641 EEMLKS 646
Cdd:COG1127 227 EELLAS 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
435-633 |
1.69e-28 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 114.49 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS----------- 503
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 --QEP--WLFNASVRDNILFGL-------PMDKQRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLARAV 572
Cdd:cd03225 80 vfQNPddQFFGPTVEEEVAFGLenlglpeEEIEERVEEALELVGLE---GLRD-------RSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 573 YRRADVYLLDDPLSAVDTHVGRHLFDecmrgFLgKQL------VILVTHQLQFLED-ADLIVIMDKGH 633
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLE-----LL-KKLkaegktIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
452-654 |
2.06e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.38 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWLFNASVRDNIL 518
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASlrrniavvfQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 519 FGLP--MDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHL 596
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 597 ---FDECMRGflgkQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 654
Cdd:PRK13657 511 kaaLDELMKG----RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
433-644 |
2.20e-28 |
|
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: 115.53 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YS-------- 500
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlasLSrrelarri 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 -YASQEPWL-FNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLHGDGTIVGErgasLSGGQRARICLAR 570
Cdd:COG1120 78 aYVPQEPPApFGLTVRELVALGRyphlglfgRPSAEDREAVEE--ALER-TGLEHLADRPVDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 571 AVYRRADVYLLDDPLSAVDTHvgrHLFD--ECMRGFLGKQ--LVILVTHQL----QFledADLIVIMDKGHVSACGTYEE 642
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLA---HQLEvlELLRRLARERgrTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEE 224
|
..
gi 28574259 643 ML 644
Cdd:COG1120 225 VL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1049-1272 |
2.72e-28 |
|
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: 114.95 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdLRSKI 1127
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDVRKEPRE-ARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSG-TMRYNLDPF-EQYPDDKlwkalEDVHLK-EEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRE 1204
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFaELYGLFD-----EELKKRiEELIEL-LGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1205 NRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHrlntIMD-----SDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSH----IMQevealCDRVVILHKGKVVAQGSLDELR 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
451-642 |
3.23e-28 |
|
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: 114.57 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS------------YASQEPWLF-NASVRDNI 517
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPDERGLYdRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 -----LFGLPMDKQRYRT--VLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:COG4555 96 ryfaeLYGLFDEELKKRIeeLIELLGLEEFLD----------RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 591 HVGRhlfdeCMRGFLgKQL------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEE 642
Cdd:COG4555 166 MARR-----LLREIL-RALkkegktVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
435-638 |
4.46e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.40 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------SYASQE- 505
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 --PWLFNASVRDNILFGL--------PMDKQRYRTVLKrcALERdLELLH-GDGTIvgergASLSGGQRARICLARAVYR 574
Cdd:cd03235 78 siDRDFPISVRDVVLMGLyghkglfrRLSKADKAKVDE--ALER-VGLSElADRQI-----GELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 575 RADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL------VILVTHQLQFLEDADLIVIMDKGHVSACG 638
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYE------LLRELrregmtILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1052-1276 |
4.99e-28 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 113.83 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRlsYNDGAILIDSLD---TNDIGLHDLRS 1125
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER--PTSGSVLVDGTDltlLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSG-TMRYNLdpfeQYPdDKLWKaLEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAIL 1202
Cdd:cd03258 83 RIGMIFQHFNLLSSrTVFENV----ALP-LEIAG-VPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1203 RENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1049-1277 |
6.01e-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: 114.13 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKI 1127
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWsGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPvlfsgtmRYNLDPF---------------EQYPDDKLWKALEDVHLKEEI-----SELpSGlqsiiseggtnf 1187
Cdd:COG1124 82 QMVFQDP-------YASLHPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFldrypHQL-SG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 svGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFKD------CTVLTIAHRLNTI--MdSDKVLVMDA 1259
Cdd:COG1124 142 --GQRQRVAIARALILEPELLLLDEPTSAL----DVSVQAEILNLLKDlreergLTYLFVSHDLAVVahL-CDRVAVMQN 214
|
250 260 270
....*....|....*....|....*....|
gi 28574259 1260 GHVVEFG----------SPY--ELLTASKA 1277
Cdd:COG1124 215 GRIVEELtvadllagpkHPYtrELLAASLA 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
434-634 |
6.03e-28 |
|
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: 111.34 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqEPWLFNASV 513
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK------DIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFgLPMDKQRYR--TVLkrcalerdlELLHgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTh 591
Cdd:cd03230 72 KRRIGY-LPEEPSLYEnlTVR---------ENLK------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28574259 592 VGRHLFDECMRGFLGKQ-LVILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:cd03230 129 ESRREFWELLRELKKEGkTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
435-633 |
7.29e-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: 110.80 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGqeqHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwlfnasvr 514
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 dnilfglPMDKQRYRTVLKRCALErdlellhgdgtivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGR 594
Cdd:cd00267 62 -------DIAKLPLEELRRRIGYV-----------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 28574259 595 HLFDECMRGFLGKQL-VILVTHQLQFLEDA-DLIVIMDKGH 633
Cdd:cd00267 117 ERLLELLRELAEEGRtVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
429-644 |
7.97e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.20 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 429 EPDTL-VEIKALRarWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS----------- 496
Cdd:PRK10789 310 GRGELdVNIRQFT--YPQTDHP-ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqlds 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 497 --GKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERD--LELLHGDGTIVGERGASLSGGQRARICLARAV 572
Cdd:PRK10789 387 wrSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDdiLRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 573 YRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
435-634 |
1.07e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.77 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkysyASQEPWLFNAsVR 514
Cdd:cd03246 2 EVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPNE-LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNIlfGlpmdkqryrtvlkrcALERDLELLhgDGTIvgeRGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGR 594
Cdd:cd03246 76 DHV--G---------------YLPQDDELF--SGSI---AENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 28574259 595 HLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 634
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1052-1266 |
1.52e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.60 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISII 1130
Cdd:cd03214 3 ENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQepvlfsgtmrynldpfeqypddklwkALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQRQLVCLARAILRENR 1206
Cdd:cd03214 79 PQ--------------------------ALELLglaHLADrPFNEL-SG--------------GERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1207 ILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFG 1266
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
433-630 |
1.91e-27 |
|
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: 111.03 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------------S 500
Cdd:COG4133 2 MLEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLFNA-SVRDNILF-----GLPMDKQRYRTVLKRCALERdlellHGDgtivgERGASLSGGQRARICLARAVYR 574
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAG-----LAD-----LPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 575 RADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQ-LVILVTHQLQFLEDADLIVIMD 630
Cdd:COG4133 149 PAPLWLLDEPFTALDAA-GVALLAELIAAHLARGgAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-364 |
2.20e-27 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 113.12 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 93 LIMSGITIAALELgTRATVPLLLAGLISEFSEHGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSA 172
Cdd:pfam00664 1 LILAILLAILSGA-ISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 173 IYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLYEQIG-MASFYGISILVLYLPLQT 251
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 252 YLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFeitLGRIAI 331
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGI---TQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 28574259 332 FVSLLGFVLGG-----GELTAERAFCVTAFYNILRRTV 364
Cdd:pfam00664 237 LSYALALWFGAylvisGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1051-1271 |
4.85e-27 |
|
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: 110.73 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1051 TKDLSLRYEPDtnspCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYN------DGAILIDSLDTNDIGLHD-- 1122
Cdd:cd03260 3 LRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapdEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1123 LRSKISIIPQEPVLFSGTMRYNLDpfeqYP------------DDKLWKALEDVHLKEEISELPSGLQsiiseggtnFSVG 1190
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVKDRLHALG---------LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1191 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH------RLntimdSDKVLVMDAGHVVE 1264
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVE 220
|
....*..
gi 28574259 1265 FGSPYEL 1271
Cdd:cd03260 221 FGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
434-643 |
5.23e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.01 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-------------- 499
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrniamv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 --SYAsqepwLF-NASVRDNILFGLPMDK-------QRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLA 569
Cdd:COG3839 81 fqSYA-----LYpHMTVYENIAFPLKLRKvpkaeidRRVREAAELLGLE---DLLD-------RKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 570 RAVYRRADVYLLDDPLSAVDthvgRHLFDEcMRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYE 641
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLD----AKLRVE-MRAEI-KRLhrrlgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
..
gi 28574259 642 EM 643
Cdd:COG3839 220 EL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
434-646 |
2.12e-26 |
|
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: 108.96 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 502
Cdd:cd03299 1 LKVENLSKDWK----EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLF-NASVRDNILFGLPMdKQRYRTVLKRCALE--RDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVY 579
Cdd:cd03299 77 PQNYALFpHMTVYKNIAYGLKK-RKVDKKEIERKVLEiaEMLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 580 LLDDPLSAVDTHVGRHLFDEcMRgFLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEEMLKS 646
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREE-LK-KIRKEFgvtVLHVTHD---FEEAwalaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
431-651 |
3.53e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 114.62 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKY-------- 499
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 -----SYASQEPW--LFNASVRDNILFGLpmdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLAR 570
Cdd:COG1123 81 rgrriGMVFQDPMtqLNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 571 AVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRE--LQRERgttVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
....*
gi 28574259 647 GQDFA 651
Cdd:COG1123 234 PQALA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1049-1274 |
6.18e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.84 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRY-EPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDL 1123
Cdd:COG1123 261 LEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLlRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RSKISIIPQEPV--LF-----SGTMRYNLDPFEQYPDDKLWK----ALEDVHLKEE-ISELPSGlqsiiseggtnFSVGQ 1191
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGLLSRAERRErvaeLLERVGLPPDlADRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPqtdaLIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|
gi 28574259 1265 FGSPYELLTA 1274
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
451-629 |
7.57e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA-----SQEPWLFNASVRDNILFGL--PM 523
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAyvpqrSEVPDSLPLTVRDLVAMGRwaRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 524 DKQRYRTVLKRCALERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD----E 599
Cdd:NF040873 87 GLWRRLTRDDRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAllaeE 165
|
170 180 190
....*....|....*....|....*....|
gi 28574259 600 CMRGflgkQLVILVTHQLQFLEDADLIVIM 629
Cdd:NF040873 166 HARG----ATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
446-638 |
1.07e-25 |
|
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: 105.09 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 446 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQEPWLFNASV 513
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNIlfglpmdkqryrtvlkrcalerdlellhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVG 593
Cdd:cd03247 92 RNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28574259 594 RHLFdECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACG 638
Cdd:cd03247 135 RQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
434-632 |
1.22e-25 |
|
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: 106.50 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS----- 503
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGapdEGEVLLDGKDIYDLdvdvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ----------QEPWLFNASVRDNILFGLpmdkqRYRTVLKRCAL-ERDLELLHGDG--TIVGER--GASLSGGQRARICL 568
Cdd:cd03260 78 elrrrvgmvfQKPNPFPGSIYDNVAYGL-----RLHGIKLKEELdERVEEALRKAAlwDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 569 ARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKG 632
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMqQAARVADRTAFLLNG 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1049-1284 |
1.66e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDSLDtndigLHDLRS 1125
Cdd:COG1121 7 IELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAilgLLPPT--SGTVRLFGKP-----PRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEP------------VLFSGtmRYNLDPFEQYPD----DKLWKALEDVHLKE----EISELpSGlqsiiseggt 1185
Cdd:COG1121 76 RIGYVPQRAevdwdfpitvrdVVLMG--RYGRRGLFRRPSradrEAVDEALERVGLEDladrPIGEL-SG---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1186 nfsvGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKfKDCTVLTIAHRLNTIMD-SDKVLVMDaGHV 1262
Cdd:COG1121 143 ----GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelRR-EGKTILVVTHDLGAVREyFDRVLLLN-RGL 216
|
250 260
....*....|....*....|...
gi 28574259 1263 VEFGSPYELLTASK-AKVFHGMV 1284
Cdd:COG1121 217 VAHGPPEEVLTPENlSRAYGGPV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
431-636 |
1.73e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 106.28 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQE-- 505
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 -----------------PWLfnaSVRDNILfgLPMdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARI 566
Cdd:COG1136 82 rlrrrhigfvfqffnllPEL---TALENVA--LPL---LLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 567 CLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDECMRGFlgKQLVILVTHQLQFLEDADLIVIMDKGHVSA 636
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEvleLLRELNREL--GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
434-634 |
1.79e-25 |
|
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: 105.57 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYS 500
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLFNASVRDNI-LFGLPMDKQRYrTVLKrcalerdlellhgdgtiVGERGASLSGGQRARICLARAVYRRADVY 579
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIY-GALR-----------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 580 LLDDPLSAVDTHVGrHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHV 634
Cdd:cd03369 148 VLDEATASIDYATD-ALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
435-638 |
2.34e-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: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwlfnasvr 514
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 dnilfglPMDKQRYRTVLKRCA-----LERdLELLHgdgtiVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAV 588
Cdd:cd03214 62 -------DLASLSPKELARKIAyvpqaLEL-LGLAH-----LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 589 DTHVGRHLFDECMRgfLGKQL---VILVTHQL----QFledADLIVIMDKGHVSACG 638
Cdd:cd03214 129 DIAHQIELLELLRR--LARERgktVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
434-642 |
2.35e-25 |
|
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: 106.17 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 498
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpvntv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 -YSYAsqepwLF-NASVRDNILFGLPMdKQRYRTVLKRcALERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRA 576
Cdd:cd03300 78 fQNYA-----LFpHLTVFENIAFGLRL-KKLPKAEIKE-RVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 577 DVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT----YEE 642
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKR--LQKELgitFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTpeeiYEE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1049-1272 |
3.46e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.53 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDiGLHDLRSKI 1127
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVLGEDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSG-TMRYNLDPF-------EQYPDDKLWKALEDVHLKEEISELPSglqsiiseggtNFSVGQRQLVCLAR 1199
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFFarlyglpRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1200 AILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLtiahrLNT-IMD-----SDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVL-----LSThYLEeaerlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
434-633 |
4.24e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 103.42 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 498
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 YSYASQEPWLF-NASVRDNILFGlpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRAD 577
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 578 VYLLDDPLSAVDTHVGRHLFDEC--MRGFLGKQlVILVTHQLQFLED-ADLIVIMDKGH 633
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLksLQAQLGIT-VVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
434-634 |
5.37e-25 |
|
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: 104.26 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 498
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdiamv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 -YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRA 576
Cdd:cd03301 78 fQNYA-----LYpHMTVYDNIAFGLKLRKVPKDEIDER--VREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 577 DVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHV 634
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKR--LQQRLgttTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1049-1262 |
1.83e-24 |
|
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: 101.32 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGlHDLRSKI 1127
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsGEIKVLGKDIKKEP-EEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSgtmryNLDPFEqypddklwkaledvHLKeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03230 76 GYLPEEPSLYE-----NLTVRE--------------NLK--------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHV 1262
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
434-634 |
2.96e-24 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 102.18 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWG-QEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQEPWLF- 509
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdiSKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 ---------------NASVRDNILfgLPMdkqRYRTVLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLARAV 572
Cdd:cd03255 81 rrhigfvfqsfnllpDLTALENVE--LPL---LLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 573 YRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQ--LVILVTHQLQFLEDADLIVIMDKGHV 634
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
433-657 |
3.52e-24 |
|
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: 102.96 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------- 498
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 ------YSYASQEPWLfnaSVRDNI-----LFGLPMDKQRYRTVLKRCALERDLellhgdgtiVGERGASLSGGQRARIC 567
Cdd:COG1124 81 vqmvfqDPYASLHPRH---TVDRILaeplrIHGLPDREERIAELLEQVGLPPSF---------LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 568 LARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFLED-ADLIVIMDKGHVSACGT 639
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILN------LLKDLreergltYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 28574259 640 YEEMLKSGQ-DFAQLLVES 657
Cdd:COG1124 223 VADLLAGPKhPYTRELLAA 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1045-1277 |
9.49e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.79 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1045 KEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLH 1121
Cdd:PRK13635 2 KEEIIRVEHISFRY-PDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPE--AGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQEP-VLFSGTMRYNLDPF----EQYPDDKLWK----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1192
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFVGATVQDDVAFglenIGVPREEMVErvdqALRQVGMEDFLNREPHRL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYE 1270
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*..
gi 28574259 1271 LLTASKA 1277
Cdd:PRK13635 227 IFKSGHM 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
434-634 |
1.00e-23 |
|
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: 100.68 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW------ 507
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 ---------LF-NASVRDNILFGLpmdkqryRTVLKRC---ALERDLELLhgdgTIVG------ERGASLSGGQRARICL 568
Cdd:cd03262 78 vgmvfqqfnLFpHLTVLENITLAP-------IKVKGMSkaeAEERALELL----EKVGladkadAYPAQLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 569 ARAVYRRADVYLLDDPLSAVDTH-VGRHLfdECMrgflgKQL------VILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPElVGEVL--DVM-----KDLaeegmtMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
419-657 |
1.12e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.91 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 419 KRSYPVGIGKEPDTLVEIKALRARWGQEQHDLV--LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 496
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 497 GK----YSYAS------------QEPWL-FNA--SVRDNILFGL----PMDK----QRYRTVLKRCALERDLEllhgdgt 549
Cdd:COG1123 326 GKdltkLSRRSlrelrrrvqmvfQDPYSsLNPrmTVGDIIAEPLrlhgLLSRaerrERVAELLERVGLPPDLA------- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 550 ivGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQFLED-ADL 625
Cdd:COG1123 399 --DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD--LQRELgltYLFISHDLAVVRYiADR 474
|
250 260 270
....*....|....*....|....*....|...
gi 28574259 626 IVIMDKGHVSACGTYEEMLKSGQ-DFAQLLVES 657
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEVFANPQhPYTRALLAA 507
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
452-653 |
1.85e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYA---------SQEPWLFNASVRDNIL 518
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrDYTLAslrnqvalvSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 519 FGlpmDKQRY-RTVLKR-----CALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PRK11176 439 YA---RTEQYsREQIEEaarmaYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 593 GRHL---FDEcmrgfLGKQLVILV-THQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:PRK11176 516 ERAIqaaLDE-----LQKNRTSLViAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
914-1257 |
3.99e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.42 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 914 LVGLPTIRAMGAQQTLIGQ-------YDNY-------QDLHSSGYYTFVSTSRAFGYYldlFCVAYVISVILHNFFNPPL 979
Cdd:PTZ00265 243 LVGIRTVVSYCGEKTILKKfnlseklYSKYilkanfmESLHIGMINGFILASYAFGFW---YGTRIIISDLSNQQPNNDF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 980 HNAGQIGLAITQALGMTgMVQWGMRQSAELENAMTSVERVLEYKDLDPEGDFNSPAEKQPPKSwpkegKLVTKDLSLRYe 1059
Cdd:PTZ00265 320 HGGSVISILLGVLISMF-MLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-----KIQFKNVRFHY- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1060 pDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsYN--DGAILI-DSLDTNDIGLHDLRSKISIIPQEPV 1135
Cdd:PTZ00265 393 -DTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL-YDptEGDIIInDSHNLKDINLKWWRSKIGVVSQDPL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1136 LFSGTMR-------------------YNLDPFEQYPDD------------------------------KLWKALED---- 1162
Cdd:PTZ00265 471 LFSNSIKnnikyslyslkdlealsnyYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneliemrKNYQTIKDsevv 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1163 -----VHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT 1237
Cdd:PTZ00265 551 dvskkVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
410 420
....*....|....*....|..
gi 28574259 1238 VLT--IAHRLNTIMDSDKVLVM 1257
Cdd:PTZ00265 631 RITiiIAHRLSTIRYANTIFVL 652
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
732-955 |
4.65e-23 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 100.41 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 732 VLVFVVLIMLCIGTQILASggdYFLSYW-----VKNTASSSTLDIY--YFTAINVGLVICALLRTLLFFNITMHSSTELH 804
Cdd:pfam00664 1 LILAILLAILSGAISPAFP---LVLGRIldvllPDGDPETQALNVYslALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 805 NTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYW 884
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 885 RDFYLKTSRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFG 955
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSF 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
433-634 |
4.82e-23 |
|
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: 99.12 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------- 498
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 ---------YSYASQEPWLfnaSVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLA 569
Cdd:cd03257 81 rkeiqmvfqDPMSSLNPRM---TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGR---HLFDEcmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAqilDLLKK-----LQEELgltLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
462-634 |
7.78e-23 |
|
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: 98.14 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 462 GQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NASVRDNILFGLPM 523
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 524 DKQRYRTVLkrcaLERDLELLHGDGtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLfdecmRG 603
Cdd:cd03297 103 KRNREDRIS----VDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL-----LP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 28574259 604 FLGKQL------VILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:cd03297 173 ELKQIKknlnipVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
433-649 |
1.39e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.14 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW----- 507
Cdd:COG1126 1 MIEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 ----------LF-NASVRDNILFGLpmdkqryRTVLKRC---ALERDLELLhgdgTIVG--ERG----ASLSGGQRARIC 567
Cdd:COG1126 78 kvgmvfqqfnLFpHLTVLENVTLAP-------IKVKKMSkaeAEERAMELL----ERVGlaDKAdaypAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 568 LARAVYRRADVYLLDDPLSAVDTH-VG------RHLFDECMRgflgkqlVILVTHQLQFLED-ADLIVIMDKGHVSACGT 639
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElVGevldvmRDLAKEGMT-------MVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
250
....*....|
gi 28574259 640 YEEMLKSGQD 649
Cdd:COG1126 220 PEEFFENPQH 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
432-653 |
1.40e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------K 498
Cdd:PRK13635 4 EIIRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 YSYASQEP--WLFNASVRDNILFGL-----PMDK--QRYRTVLKRCALErdlELLHgdgtivgERGASLSGGQRARICLA 569
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLenigvPREEmvERVDQALRQVGME---DFLN-------REPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 570 RAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGfLGKQL---VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDP-RGRREVLETVRQ-LKEQKgitVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
....*..
gi 28574259 647 GQDFAQL 653
Cdd:PRK13635 231 GHMLQEI 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1052-1266 |
1.49e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.22 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDtndigLHDLRSKISII 1130
Cdd:cd03235 3 EDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsGSIRVFGKP-----LEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQE-------PVL---FSGTMRYNLDPFEQYPDDKLWK----ALEDVHLKE----EISELpSGlqsiiseggtnfsvGQR 1192
Cdd:cd03235 74 PQRrsidrdfPISvrdVVLMGLYGHKGLFRRLSKADKAkvdeALERVGLSEladrQIGEL-SG--------------GQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDS-DKVLVMDaGHVVEFG 1266
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN-RTVVASG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
450-644 |
1.88e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNV-----------NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW----------- 507
Cdd:COG3840 2 LRLDDLtyrygdfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-DLTALPPAerpvsmlfqen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 -LFNA-SVRDNILFGL-------PMDKQRYRTVLKRCALErDLEllhgdgtivGERGASLSGGQRARICLARAVYRRADV 578
Cdd:COG3840 81 nLFPHlTVAQNIGLGLrpglkltAEQRAQVEQALERVGLA-GLL---------DRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 579 YLLDDPLSAVD---THVGRHLFDEcmrgfLGKQL---VILVTHQlqfLEDA----DLIVIMDKGHVSACGTYEEML 644
Cdd:COG3840 151 LLLDEPFSALDpalRQEMLDLVDE-----LCRERgltVLMVTHD---PEDAariaDRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1273 |
2.32e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLsyNDGAILIDSLDTNDIGLHDLRSKIS 1128
Cdd:PRK13632 11 ENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKP--QSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEP------------VLFsGTMRYNLDPfeqypdDKLWKALEDVHLKeeiselpSGLQSIISEGGTNFSVGQRQLVC 1196
Cdd:PRK13632 87 IIFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIIDDLAKK-------VGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1197 LARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
982-1244 |
2.88e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 982 AGQIGL-AITQALGMTGMVQ----WGMRQSAELENAMTSVERVLEYKDLDPEGDfnSPAEKQPPKSWPKEGKLVTKDLSL 1056
Cdd:COG4178 293 AGEITLgGLMQAASAFGQVQgalsWFVDNYQSLAEWRATVDRLAGFEEALEAAD--ALPEAASRIETSEDGALALEDLTL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1057 R---YEPdtnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndiglhdlrsKISIIPQ 1132
Cdd:COG4178 371 RtpdGRP------LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIARPAGA-----------RVLFLPQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1133 EPVLFSGTMR----YNLDPfEQYPDDKLWKALEDVHLkeeiselpSGLQSIISEG---GTNFSVGQRQLVCLARAILREN 1205
Cdd:COG4178 434 RPYLPLGTLReallYPATA-EAFSDAELREALEAVGL--------GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKP 504
|
250 260 270
....*....|....*....|....*....|....*....
gi 28574259 1206 RILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHR 1244
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
451-646 |
4.37e-22 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 96.99 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------------KYSYASQEPWLF-NASVRDN 516
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 I-----LFGLPmdKQRYRtvlkrcalERDLELLH----GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:cd03295 96 IalvpkLLKWP--KEKIR--------ERADELLAlvglDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 588 VDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:cd03295 166 LDPITRDQLQEEFKR--LQQELgktIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1049-1262 |
5.18e-22 |
|
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: 96.02 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDL---- 1123
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RSKISIIPQEpvlfsgtmrYNLDPF---------------EQYPDDKLW--KALEDVHLKEEISELPSGLqsiiseggtn 1186
Cdd:cd03255 81 RRHIGFVFQS---------FNLLPDltalenvelplllagVPKKERRERaeELLERVGLGDRLNHYPSEL---------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1187 fSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHV 1262
Cdd:cd03255 142 -SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
429-642 |
6.10e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.64 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 429 EPDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------- 498
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 ------YSYAsqepwLF-NASVRDNILFGLPMDK-------QRYRTVLKRCALERdlellhgdgtIVGERGASLSGGQRA 564
Cdd:PRK09452 87 hvntvfQSYA-----LFpHMTVFENVAFGLRMQKtpaaeitPRVMEALRMVQLEE----------FAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT- 639
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKA--LQRKLgitFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTp 229
|
....*.
gi 28574259 640 ---YEE 642
Cdd:PRK09452 230 reiYEE 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
435-615 |
6.18e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARW-GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS--------QE 505
Cdd:COG4525 5 TVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgadrgvvfQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 ----PWLfnaSVRDNILFGLpmdkqRYRTVLKRCALERDLELLHgdgtIVGERGA------SLSGGQRARICLARAVYRR 575
Cdd:COG4525 85 dallPWL---NVLDNVAFGL-----RLRGVPKAERRARAEELLA----LVGLADFarrriwQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28574259 576 ADVYLLDDPLSAVDThvgrhLFDECMRGFL-------GKQlVILVTH 615
Cdd:COG4525 153 PRFLLMDEPFGALDA-----LTREQMQELLldvwqrtGKG-VFLITH 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1052-1273 |
6.33e-22 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 96.03 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDT---NDIGLHDLRSKI 1127
Cdd:cd03261 4 RGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSGT---------MRYNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLA 1198
Cdd:cd03261 80 GMLFQSGALFDSLtvfenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1049-1266 |
9.59e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 94.89 E-value: 9.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHdlRS 1125
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLlrlIAGLERPD--SGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSgtmryNLDPFE--QYP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1192
Cdd:cd03259 73 NIGMVFQDYALFP-----HLTVAEniAFGlklrgvpkaeiRARVRELLELVGLEGLLNRYPHEL-----------SGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
434-642 |
1.17e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-----------YSYA 502
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLF-NASVRDNILFGLPMDKQRYR---TVLKR---CALERdLELLHgdgtiVGER-GASLSGGQRARICLARAVYR 574
Cdd:PRK10851 80 FQHYALFrHMTVFDNIAFGLTVLPRRERpnaAAIKAkvtQLLEM-VQLAH-----LADRyPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 575 RADVYLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTH-QLQFLEDADLIVIMDKGHVSACGTYEE 642
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKEL-----RRWL-RQLheelkftSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
454-630 |
1.20e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 454 NVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKYSYAS-----------QEPWLF-NASVRDNIL 518
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALpaeqrrigilfQDDLLFpHLSVGENLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 519 FGLPMD---KQRYRTVLKrcALErDLELLHgdgtiVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThvgr 594
Cdd:COG4136 99 FALPPTigrAQRRARVEQ--ALE-EAGLAG-----FADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA---- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 28574259 595 HLFDEcMRGFLGKQL------VILVTHQLQFLEDADLIVIMD 630
Cdd:COG4136 167 ALRAQ-FREFVFEQIrqrgipALLVTHDEEDAPAAGRVLDLG 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
430-645 |
1.45e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPW 507
Cdd:COG0488 312 GKKVLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 LF--NASVRDNILFGLPMDKQRY-RTVLKRCalerdleLLHGD--GTIVGergaSLSGGQRARICLARAVYRRADVYLLD 582
Cdd:COG0488 389 ELdpDKTVLDELRDGAPGGTEQEvRGYLGRF-------LFSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 583 DP---LSaVDThvgRHLFDECMRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGHVSAC-GTYEEMLK 645
Cdd:COG0488 458 EPtnhLD-IET---LEALEEALDDFPGT--VLLVSHDRYFLDRvATRILEFEDGGVREYpGGYDDYLE 519
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
429-618 |
1.70e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 429 EPDTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS 503
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ---------------QEPWLFNASVRDNILFGLPM----DK----QRYRTVLKRCAL-----ERdlelLHgdgtivgERG 555
Cdd:COG1117 84 dvdvvelrrrvgmvfQKPNPFPKSIYDNVAYGLRLhgikSKseldEIVEESLRKAALwdevkDR----LK-------KSA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 556 ASLSGGQRARICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDEcmrgfLGKQL-VILVTHQLQ 618
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILE-----LKKDYtIVIVTHNMQ 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
433-652 |
1.74e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS--------- 503
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ------QEPWLF-NASVRDNILFGlPMdkqRYRTVLKRCALERDLELLHGDGtiVGERG----ASLSGGQRARICLARAV 572
Cdd:PRK09493 78 eagmvfQQFYLFpHLTALENVMFG-PL---RVRGASKEEAEKQARELLAKVG--LAERAhhypSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 573 YRRADVYLLDDPLSAVDTHVgRHLFDECMRGFL--GKQLVIlVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKSG-- 647
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPEL-RHEVLKVMQDLAeeGMTMVI-VTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPps 229
|
....*...
gi 28574259 648 ---QDFAQ 652
Cdd:PRK09493 230 qrlQEFLQ 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
435-634 |
1.94e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.94 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------K 498
Cdd:cd03256 2 EVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 YSYASQEPWLFN-ASVRDNILFGL---------------PMDKQRYRTVLKRCALerdLELLHgdgtivgERGASLSGGQ 562
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGL---LDKAY-------QRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 563 RARICLARAVYRRADVYLLDDPLSAVD----THVGRHLFDECMRgflgKQL-VILVTHQLQF-LEDADLIVIMDKGHV 634
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDpassRQVMDLLKRINRE----EGItVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
451-644 |
2.61e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPWL---------------FNASVRD 515
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGL---PMDKQRYRTVLKRcALER-DLELLhgdgtivGERG-ASLSGGQRARICLARA-------VYRRADVYLLDD 583
Cdd:COG4559 95 VVALGRaphGSSAAQDRQIVRE-ALALvGLAHL-------AGRSyQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 584 PLSAVDTHVGRHLFdECMRGFLGKQL-VILVTHQL----QFledADLIVIMDKGHVSACGTYEEML 644
Cdd:COG4559 167 PTSALDLAHQHAVL-RLARQLARRGGgVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
438-644 |
3.19e-21 |
|
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: 97.09 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 438 ALRARWGQEQHDLVLNnVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY-----------------S 500
Cdd:COG4148 2 MLEVDFRLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLF-NASVRDNILFGLPMDKQRYRTVlkrcALERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRRADVY 579
Cdd:COG4148 81 YVFQEARLFpHLSVRGNLLYGRKRAPRAERRI----SFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 580 LLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLER--LRDELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1067-1261 |
3.59e-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: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSYndGAILID--SLDTNDIGLHDLRSKISIIPQEPVLFSgtm 1141
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLlrcIAGLEEPDS--GSILIDgeDLTDLEDELPPLRRRIGMVFQDFALFP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 rynldpfeqypddklwkaledvHL--KEEISELPSGlqsiiseggtnfsvGQRQLVCLARAILRENRILVMDEATANVDP 1219
Cdd:cd03229 90 ----------------------HLtvLENIALGLSG--------------GQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28574259 1220 QTDALIQATIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGH 1261
Cdd:cd03229 134 ITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
451-653 |
4.58e-21 |
|
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: 99.12 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYAS---------QEPWLFNASVRDNI 517
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirDVTQASlraaigivpQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLP-MDKQRYRTVLKRCALERDLELL-HGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH 595
Cdd:COG5265 453 AYGRPdASEEEVEAAARAAQIHDFIESLpDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 596 LFDECMRgfLGKQ---LVIlvTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:COG5265 533 IQAALRE--VARGrttLVI--AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
450-653 |
4.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.09 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFN 510
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklkplrkkvgivfqfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFGlPMD--------KQRYRTVLKRCALERDLEllhgdgtivgERGA-SLSGGQRARICLARAVYRRADVYLL 581
Cdd:PRK13634 101 ETVEKDICFG-PMNfgvseedaKQKAREMIELVGLPEELL----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 582 DDPLSAVDTHvGRHlfdECMRGF--LGKQ---LVILVTHQlqfLED----ADLIVIMDKGHVSACGTYEEMLKSGQDFAQ 652
Cdd:PRK13634 170 DEPTAGLDPK-GRK---EMMEMFykLHKEkglTTVLVTHS---MEDaaryADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
.
gi 28574259 653 L 653
Cdd:PRK13634 243 I 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
435-644 |
7.61e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 92.50 E-value: 7.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YS 500
Cdd:cd03224 2 EVENLNAGYGKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLF-NASVRDNILFGLpmdKQRYRTVLKRcALERDLELLhgdgTIVGER----GASLSGGQRARICLARAVYRR 575
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGA---YARRRAKRKA-RLERVYELF----PRLKERrkqlAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 576 ADVYLLDDP---LS-AVDTHVGRHLFDECMRGflgkQLVILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEML 644
Cdd:cd03224 151 PKLLLLDEPsegLApKIVEEIFEAIRELRDEG----VTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
431-626 |
9.78e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS-- 503
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPrt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 -------------QEPWLFNASVRDNILFGLPMDKQRYRTVLKRcALERDL----------ELLHgdgtivgERGASLSG 560
Cdd:PRK14239 80 dtvdlrkeigmvfQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLkgasiwdevkDRLH-------DSALGLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 561 GQRARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQ----------FLEDADLI 626
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQqasrisdrtgFFLDGDLI 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
451-646 |
1.18e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 92.50 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ-----VSGKYSYAS---------QEPWLF-NASVRD 515
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPHEIarlgigrtfQIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKRCALERDL-----ELLHgdgtIVG------ERGASLSGGQRARICLARAVYRRADVYLLDDP 584
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeELLE----RVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 585 ---LSAVDTHVGRHLFDEcMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:cd03219 171 aagLNPEETEELAELIRE-LRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
434-645 |
1.82e-20 |
|
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: 91.41 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY------------SY 501
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkaarqslGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQEPWLFNA-SVRDNILF-----GLPmDKQRYRTVLKrcaLERDLELLHgdgtiVGERGAS-LSGGQRARICLARAVYR 574
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLP-KSEIKEEVEL---LLRVLGLTD-----KANKRARtLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 575 RADVYLLDDPLSAVDtHVGRHLFDECMRGFLGKQLVILVTHqlqFLEDADL----IVIMDKGHVSACGTYEEmLK 645
Cdd:cd03263 151 GPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQE-LK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1049-1264 |
2.33e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.26 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDT---NDIGLHDLR 1124
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDIsslSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 -SKISIIPQepvlfsgtmRYNLDPF-----------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtn 1186
Cdd:COG1136 85 rRHIGFVFQ---------FFNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1187 fSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVE 1264
Cdd:COG1136 146 -SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1052-1274 |
4.80e-20 |
|
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: 92.81 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYNDGAILIDSLDTNDIGLHDLRS-- 1125
Cdd:COG0444 5 RNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKELRKir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 --KISIIPQEPvlfsgtmrYN-LDP--------------FEQYPDDKLWK----ALEDVHL---KEEISELPSglqsiis 1181
Cdd:COG0444 85 grEIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEAREraieLLERVGLpdpERRLDRYPH------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1182 eggtNFSVGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFKD------CTVLTIAHRLNTI--MdSDK 1253
Cdd:COG0444 150 ----ELSGGMRQRVMIARALALEPKLLIADEPTTAL----DVTIQAQILNLLKDlqrelgLAILFITHDLGVVaeI-ADR 220
|
250 260
....*....|....*....|.
gi 28574259 1254 VLVMDAGHVVEFGSPYELLTA 1274
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFEN 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
430-642 |
6.22e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGqeqhDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPW- 507
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-DITGLPPHr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 --------------LF-NASVRDNI---------------LFGLPMDKQRYRTVLKRC--ALERdLELLHgdgtIVGERG 555
Cdd:COG0411 76 iarlgiartfqnprLFpELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAeeLLER-VGLAD----RADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 556 ASLSGGQRARICLARAVYRRADVYLLDDP---LSAVDTH-VGRHLFDecMRGFLGKqLVILVTHQLQFLED-ADLIVIMD 630
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPaagLNPEETEeLAELIRR--LRDERGI-TILLIEHDMDLVMGlADRIVVLD 227
|
250
....*....|..
gi 28574259 631 KGHVSACGTYEE 642
Cdd:COG0411 228 FGRVIAEGTPAE 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1052-1279 |
6.40e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.83 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRlsYNDGAILIDSLDTNDI---GLHDLRS 1125
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER--PTSGSVLVDGVDLTALserELRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSG-TMRYNLD-PFEQypdDKLWKA---------LEDVHLKEEISELPSGLqsiiseggtnfSVGQRQL 1194
Cdd:COG1135 83 KIGMIFQHFNLLSSrTVAENVAlPLEI---AGVPKAeirkrvaelLELVGLSDKADAYPSQL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1195 VCLARAILRENRILVMDEATANVDPQTD----ALIQaTIRNKFKdCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPY 1269
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
250
....*....|
gi 28574259 1270 ELLTASKAKV 1279
Cdd:COG1135 227 DVFANPQSEL 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
451-627 |
9.13e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------YSYASQEPWLFNASVRDNI 517
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLPMDKQRyrtvLKRCALERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLF 597
Cdd:PRK10247 102 IFPWQIRNQQ----PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|.
gi 28574259 598 DECMRGFLGKQLVIL-VTHQLQFLEDADLIV 627
Cdd:PRK10247 178 EIIHRYVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
743-1022 |
1.14e-19 |
|
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: 91.12 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 743 IGTQILASG-GDYFLSYWVKNTASSSTLDIYYFTAinvGLVICALLRTLLFFN-------ITMHSSTELHNTMFQGLSRT 814
Cdd:cd18559 8 VLCNHVFSGpSNLWLLLWFDDPVNGPQEHGQVYLS---VLGALAILQGITVFQysmavsiGGIFASRAVHLDLYHKALRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 815 ALYFFHTNPSGRILNRFANDLGQVDEVMPAV-MLDCIQIFLTLTGIICVLCVTnPWYLINTFAMMLAFYYWRdFYLKTSR 893
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQViKMWMGPLQNVIGLYLLILLAG-PMAAVGIPLGLLYVPVNR-VYAASSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 894 DVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDlHSSGYYTFVSTSRAFGYYldLFCVAYVIsVILHN 973
Cdd:cd18559 163 QLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVR--LWCVGPCI-VLFAS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 974 FFNPPL--HNAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEY 1022
Cdd:cd18559 239 FFAYVSrhSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1048-1273 |
1.64e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.71 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsyND--------GAILIDSLDTND-- 1117
Cdd:COG1117 11 KIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRM--NDlipgarveGEILLDGEDIYDpd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1118 IGLHDLRSKISIIPQEPVLFSGT--------MRYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNFSV 1189
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALWDEVKD-------RLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1190 GQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRlntiMD-----SDKVLVMDAGHVVE 1264
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN----MQqaarvSDYTAFFYLGELVE 233
|
....*....
gi 28574259 1265 FGSPYELLT 1273
Cdd:COG1117 234 FGPTEQIFT 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
432-644 |
1.74e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYASQEPWL--- 508
Cdd:PRK13548 1 AMLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR-PLADWSPAElar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 509 ------------FNASVRDNILFGL---PMDKQRYRTVLKRcALERdLELLHgdgtIVGERGASLSGGQRARICLARA-- 571
Cdd:PRK13548 77 rravlpqhsslsFPFTVEEVVAMGRaphGLSRAEDDALVAA-ALAQ-VDLAH----LAGRDYPQLSGGEQQRVQLARVla 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 572 -VYRRAD---VYLLDDPLSAVDT----HVGRHLFDECMRGFLGkqlVILVTHQL----QFledADLIVIMDKGHVSACGT 639
Cdd:PRK13548 151 qLWEPDGpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLA---VIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
....*
gi 28574259 640 YEEML 644
Cdd:PRK13548 225 PAEVL 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1067-1263 |
2.09e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 86.71 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHD-LRSKISIIPQepvlfsgtmryn 1144
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSgLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 ldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDA 1223
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 28574259 1224 LIqATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:cd03216 121 LF-KVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1271 |
2.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTnsPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLHDLRSKISII 1130
Cdd:PRK13648 11 KNVSFQYQSDA--SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQEPV-LFSG-TMRY--------NLDPFEQYpDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARA 1200
Cdd:PRK13648 89 FQNPDnQFVGsIVKYdvafglenHAVPYDEM-HRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1271
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
414-645 |
2.30e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 414 LKEVEKRsYPVGiGKEPDTLVEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV 493
Cdd:COG1134 7 VENVSKS-YRLY-HEPSRSLKELLLRRRRTRREEF-WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 494 QVSGKYSyasqepWL------FN--ASVRDNILFG---LPMDKQRYRTVLKRCA----LER--DLELlhgdgtivgergA 556
Cdd:COG1134 84 EVNGRVS------ALlelgagFHpeLTGRENIYLNgrlLGLSRKEIDEKFDEIVefaeLGDfiDQPV------------K 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 557 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGK-QLVILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLAR-IRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRL 224
|
250
....*....|.
gi 28574259 635 SACGTYEEMLK 645
Cdd:COG1134 225 VMDGDPEEVIA 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
456-654 |
2.65e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.49 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 456 NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS-----------QEPWLFN-ASVRDNILFGL-- 521
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsmlfQENNLFShLTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 522 -----PMDKQRYRTVLKRCALERDLELLHGDgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgRH- 595
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL-RQe 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 596 ---LFDE-CMRgflgKQLVIL-VTHQlqfLEDADLI----VIMDKGHVSACGTYEEMLKSGQDFAQLL 654
Cdd:PRK10771 168 mltLVSQvCQE----RQLTLLmVSHS---LEDAARIaprsLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
431-646 |
3.54e-19 |
|
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: 88.60 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESG-SVQVSGK----------- 498
Cdd:COG1119 1 DPLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 -----YSYASQEPWLFNASVRDNILFGL-----------PMDKQRYRTVLKRcalerdLELLHgdgtIVGERGASLSGGQ 562
Cdd:COG1119 78 kriglVSPALQLRFPRDETVLDVVLSGFfdsiglyreptDEQRERARELLEL------LGLAH----LADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 563 RARICLARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQL--VILVTHQlqfLEDA----DLIVIMDKGHVSA 636
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAptLVLVTHH---VEEIppgiTHVLLLKDGRVVA 223
|
250
....*....|
gi 28574259 637 CGTYEEMLKS 646
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
451-634 |
3.67e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkYSYASQEPW------------------LFNAS 512
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRReipylrrrigvvfqdfrlLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILF-----GLPMDKQRYRTvlkRCALERdLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:COG2884 96 VYENVALplrvtGKSRKEIRRRV---REVLDL-VGLSDKAKALPHE----LSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 588 VDTHVGR---HLFDECMRgfLGKQlVILVTHQLQFLEDADLIVI-MDKGHV 634
Cdd:COG2884 168 LDPETSWeimELLEEINR--RGTT-VLIATHDLELVDRMPKRVLeLEDGRL 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
452-649 |
3.69e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 88.85 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NASV 513
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFGLPMdkqryRTVLKRCALERDLELLHgdgtIVGERGAS------LSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:cd03294 120 LENVAFGLEV-----QGVPRAEREERAAEALE----LVGLEGWEhkypdeLSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 588 VDTHVGRHLFDECMRgfLGKQL---VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQD 649
Cdd:cd03294 191 LDPLIRREMQDELLR--LQAELqktIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
431-653 |
4.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------- 497
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 KYSYASQEP--WLFNASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRR 575
Cdd:PRK13650 82 KIGMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKER--VNEALELV-GMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 576 ADVYLLDDPLSAVDTHvGRHLFDECMRGFLGK-QL-VILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:PRK13650 159 PKIIILDEATSMLDPE-GRLELIKTIKGIRDDyQMtVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
433-618 |
5.24e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YS 500
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergvvFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLfnaSVRDNILFGLpmdkqRYRTVLKRCALERDLELLhgdgTIVGERGA------SLSGGQRARICLARAVYR 574
Cdd:PRK11248 78 NEGLLPWR---NVQDNVAFGL-----QLAGVEKMQRLEIAHQML----KKVGLEGAekryiwQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 575 RADVYLLDDPLSAVDTHVgrhlfDECMRGFL-------GKQlVILVTHQLQ 618
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFT-----REQMQTLLlklwqetGKQ-VLLITHDIE 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
461-638 |
8.91e-19 |
|
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: 86.39 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 461 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------KYSYASQEPWLF-NASVRDNILFGL------- 521
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFaHLTVEQNVGLGLspglklt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 522 PMDKQRYRTVLKRCALERDLELLHGdgtivgergaSLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM 601
Cdd:cd03298 103 AEDRQAIEVALARVGLAGLEKRLPG----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 28574259 602 RGFLGKQL-VILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:cd03298 173 DLHAETKMtVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1067-1272 |
9.27e-19 |
|
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: 86.72 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-YNDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSG-TMRY 1143
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLD-PFEQYPDDKLWKALEDVH-----LKEEISELpsglqsiiseGGTnFSVGQRQLVCLARAILRENRILVMDEATANV 1217
Cdd:cd03224 95 NLLlGAYARRRAKRKARLERVYelfprLKERRKQL----------AGT-LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1218 DPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1272
Cdd:cd03224 164 APKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1051-1271 |
1.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1051 TKDLSLRYEPD--TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIG-LHDLR 1124
Cdd:PRK13633 7 CKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPS--EGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SKISIIPQEP------------VLFsGTMRYNLDPFE--QYPDDklwkALEDVHLKEEISELPSGLqsiiseggtnfSVG 1190
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPPEEirERVDE----SLKKVGMYEYRRHAPHLL-----------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1191 QRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSP 1268
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
...
gi 28574259 1269 YEL 1271
Cdd:PRK13633 229 KEI 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
434-636 |
1.18e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 84.40 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYASqepwlfnas 512
Cdd:cd03216 1 LELRGITKRFGGVK---ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFAS--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 vrdnilfglPMDKQRyrtvlkrcalerdlellHGDGTIvgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:cd03216 69 ---------PRDARR-----------------AGIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28574259 593 GRHLFdECMRGFLGKQL-VILVTHQLQ-FLEDADLIVIMDKGHVSA 636
Cdd:cd03216 118 VERLF-KVIRRLRAQGVaVIFISHRLDeVFEIADRVTVLRDGRVVG 162
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
451-647 |
1.29e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYAS-------------QEPWL-FNASVRDN 516
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraasrrvasvpQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 ILFGLPMDKQRY--RTVLKRCALERDLEllHGDGTIVGERG-ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH-- 591
Cdd:PRK09536 98 VEMGRTPHRSRFdtWTETDRAAVERAME--RTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhq 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 592 -----VGRHLFDEcmrgflGKQlVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLKSG 647
Cdd:PRK09536 176 vrtleLVRRLVDD------GKT-AVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1052-1264 |
1.80e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDI---GLHDLRSKI 1127
Cdd:COG2884 5 ENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQ-----------EPVLFSgtMRYnldpfeQYPDDKLWK-----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQ 1191
Cdd:COG2884 82 GVVFQdfrllpdrtvyENVALP--LRV------TGKSRKEIRrrvreVLDLVGLSDKAKALPHEL-----------SGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQT-----DALIQAtirNKfKDCTVLtIA-HRLNtIMDS--DKVLVMDAGHVV 1263
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsweimELLEEI---NR-RGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLV 216
|
.
gi 28574259 1264 E 1264
Cdd:COG2884 217 R 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-638 |
2.20e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.66 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 420 RSYPvgIGKEPDTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY 499
Cdd:cd03220 8 KSYP--TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 SyasqepWLF--------NASVRDNILFG---LPMDKQRYRTVLKRCA----LERDLELlhgdgtivgeRGASLSGGQRA 564
Cdd:cd03220 86 S------SLLglgggfnpELTGRENIYLNgrlLGLSRKEIDEKIDEIIefseLGDFIDL----------PVKTYSSGMKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDTHvgrhlFDE-CMRGFLGKQL----VILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAA-----FQEkCQRRLRELLKqgktVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1068-1270 |
2.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILIDSLDTND--IGLHDLRSKISIIPQEP--VLFSGT 1140
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlNGL--LKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1141 MR-------YNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQsiiseggtnFSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:PRK13637 101 IEkdiafgpINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFE---------LSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1214 TANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1270
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1052-1271 |
2.25e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALfrLSYNDGAILIDSLDTNDIGLHDLRSKIS 1128
Cdd:PRK13650 8 KNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGL--LEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEP-VLFSGTMrynldpfeqYPDDKLW----KALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAI 1201
Cdd:PRK13650 85 MVFQNPdNQFVGAT---------VEDDVAFglenKGIPHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1202 LRENRILVMDEATANVDPQTD-ALIQA--TIRNKFkDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1271
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1052-1243 |
3.24e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.77 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDigLHD-----LRS 1125
Cdd:cd03292 4 INVTKTYPNGTAA---LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSD--LRGraipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFsgtmrYNLDPFEQ--------YPDDKLWK-----ALEDVHLKEEISELPSGLqsiiseggtnfSVGQR 1192
Cdd:cd03292 79 KIGVVFQDFRLL-----PDRNVYENvafalevtGVPPREIRkrvpaALELVGLSHKHRALPAEL-----------SGGEQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTDALIqATIRNKFKD--CTVLTIAH 1243
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATH 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1052-1271 |
4.28e-18 |
|
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: 85.31 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIG---LHDLRSKI 1127
Cdd:cd03256 4 ENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTsGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEP-----------VLFS-----GTMRYNLDPFeqYPDDKL--WKALEDVHLKEEISELPSGLqsiiseggtnfSV 1189
Cdd:cd03256 81 GMIFQQFnlierlsvlenVLSGrlgrrSTWRSLFGLF--PKEEKQraLAALERVGLLDKAYQRADQL-----------SG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1190 GQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
....*
gi 28574259 1267 SPYEL 1271
Cdd:cd03256 228 PPAEL 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1068-1274 |
7.33e-18 |
|
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: 88.59 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL-----IDSLDTNDigLHDLRSKISIIPQEP-------- 1134
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRfdgqdLDGLSRRA--LRPLRRRMQVVFQDPfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1135 -----------VLFSGtmrynLDPFEQypDDKLWKALEDVHLKEEIselpsgLQSIISEggtnFSVGQRQLVCLARAILR 1203
Cdd:COG4172 380 tvgqiiaeglrVHGPG-----LSAAER--RARVAEALEEVGLDPAA------RHRYPHE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1204 ENRILVMDEATAnvdpqtdAL---IQATIRNKFKDC------TVLTIAHRLNTI--MdSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG4172 443 EPKLLVLDEPTS-------ALdvsVQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 28574259 1273 TA 1274
Cdd:COG4172 515 DA 516
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
451-644 |
7.47e-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: 84.17 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------KYSYASQEPWLFNA-SV 513
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFGLPMDKQRyrtvlKRCALERDLELLHgdgtIVG--ERG----ASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:cd03258 100 FENVALPLEIAGVP-----KAEIEERVLELLE----LVGleDKAdaypAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 588 VD---TH-VGRHLFDecmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEML 644
Cdd:cd03258 171 LDpetTQsILALLRD------INRELgltIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1044-1264 |
8.86e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.76 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1044 PKEGKLVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDsldtnDIGL 1120
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagLEKPT--SGEVLVD-----GKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1121 HDLRSKISIIPQEPVLFsgtmrynldpfeqyPddklWK--------------------------ALEDVHLKEEISELPS 1174
Cdd:COG1116 76 TGPGPDRGVVFQEPALL--------------P----WLtvldnvalglelrgvpkaerrerareLLELVGLAGFEDAYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1175 GLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ---ATIRNKFKdCTVLTIAH------RL 1245
Cdd:COG1116 138 QL-----------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQdelLRLWQETG-KTVLFVTHdvdeavFL 205
|
250 260
....*....|....*....|.
gi 28574259 1246 ntimdSDKVLVMDA--GHVVE 1264
Cdd:COG1116 206 -----ADRVVVLSArpGRIVE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
448-584 |
1.06e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 448 HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEPWLF-NASVRDNILFGlpmD 524
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDdDLTVLDTVLDG---D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 525 KQRYRTVLKRCALERDLELLHGDGTIVGE-------RGA--------------------------SLSGGQRARICLARA 571
Cdd:COG0488 87 AELRALEAELEELEAKLAEPDEDLERLAElqeefeaLGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARA 166
|
170
....*....|...
gi 28574259 572 VYRRADVYLLDDP 584
Cdd:COG0488 167 LLSEPDLLLLDEP 179
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
431-645 |
1.21e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.31 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------ 498
Cdd:PRK11432 4 KNFVVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 ----YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDGtiVGERGA-SLSGGQRARICLARAV 572
Cdd:PRK11432 81 cmvfQSYA-----LFpHMSLGENVGYGLKMLGVPKEERKQR--VKEALELVDLAG--FEDRYVdQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 573 YRRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQLVI---LVTH-QLQFLEDADLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRE--LQQQFNItslYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
432-648 |
1.37e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARW-GQEqhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVsGKYSYASQEPW--- 507
Cdd:PRK11264 2 SAIEVKNLVKKFhGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 -------------------LF-NASVRDNILFGLPMDKQRYRTVlkrcALERDLELLHGDGtIVGERGA---SLSGGQRA 564
Cdd:PRK11264 77 kglirqlrqhvgfvfqnfnLFpHRTVLENIIEGPVIVKGEPKEE----ATARARELLAKVG-LAGKETSyprRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDTH-VG------RHLFDEcmrgflgKQLVILVTHQLQFLED-ADLIVIMDKGHVSA 636
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPElVGevlntiRQLAQE-------KRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
250
....*....|..
gi 28574259 637 CGTYEEMLKSGQ 648
Cdd:PRK11264 225 QGPAKALFADPQ 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
451-646 |
1.38e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 83.36 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KY----------SYASQEPWLF-NASVRD 515
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditKLpmhkrarlgiGYLPQEASIFrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD------ 589
Cdd:cd03218 95 NILAVLEIRGLSKKEREEK--LEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavqd 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 590 -THVGRHLFDecmrgflgKQLVILVT-HQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:cd03218 172 iQKIIKILKD--------RGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1044-1271 |
1.89e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1044 PKEGKLVTKDLSLRYePDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLSYNDGA-ILIDSLDTNDIG 1119
Cdd:PRK13640 1 MKDNIVEFKHVSFTY-PDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSkITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1120 LHDLRSKISIIPQEP------------VLFSGTMRynldpfeQYPDDKLWK----ALEDVHLKEEISELPSglqsiiseg 1183
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnqfvgatvgddVAFGLENR-------AVPRPEMIKivrdVLADVGMLDYIDSEPA--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1184 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDSDKVLVMDAGH 1261
Cdd:PRK13640 143 --NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
250
....*....|
gi 28574259 1262 VVEFGSPYEL 1271
Cdd:PRK13640 221 LLAQGSPVEI 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
434-633 |
2.00e-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: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQepwlfna 511
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 svrdnilfglpmdkqryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH 591
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 28574259 592 vGRHLFDECMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGH 633
Cdd:cd03221 105 -SIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
434-632 |
2.01e-17 |
|
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: 82.26 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQE-------- 505
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalrrigal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 ---PWLF-NASVRDNILFglpmdKQRYRTVLKRcALERDLELLhGDGTIVGERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:cd03268 78 ieaPGFYpNLTARENLRL-----LARLLGIRKK-RIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 582 DDPLSAVDThVGRHLfdecMRGFL------GKQlVILVTHQLQFLED-ADLIVIMDKG 632
Cdd:cd03268 151 DEPTNGLDP-DGIKE----LRELIlslrdqGIT-VLISSHLLSEIQKvADRIGIINKG 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
434-643 |
2.06e-17 |
|
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: 82.42 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 501
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQEPWLFNA-SVRDNI-----LFGLPMDKQRyrtvlkrcalERDLELLH--GDGTIVGERGASLSGGQRARICLARAVY 573
Cdd:cd03265 78 VFQDLSVDDElTGWENLyiharLYGVPGAERR----------ERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 574 RRADVYLLDDPLSAVDTHVGRHLFD--ECMRGFLGKQlVILVTHqlqFLEDADL----IVIMDKGHVSACGTYEEM 643
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEyiEKLKEEFGMT-ILLTTH---YMEEAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1049-1271 |
2.42e-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: 82.55 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDiGLHDLRSKI 1127
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSGTAYINGYSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSG-TMRYNLdpfeqypddKLW---KALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAI 1201
Cdd:cd03263 78 GYCPQFDALFDElTVREHL---------RFYarlKGLPKSEIKEEVELLLRvlGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1202 LRENRILVMDEATANVDPQTD----ALIQATIRNKfkdCTVLTIAHrlntiMD-----SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRraiwDLILEVRKGR---SIILTTHS-----MDeaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1049-1264 |
2.53e-17 |
|
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: 82.13 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndigLHDLRSKI 1127
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFS-GTMRYN--LDPFEQYPDDKLWKA-----LEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLAR 1199
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAREraeelLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1200 AILRENRILVMDEATANVDPQTDALIQATI-----RNKFkdcTVLTIAHRLN-TIMDSDKVLVMDA--GHVVE 1264
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
434-638 |
3.06e-17 |
|
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: 81.94 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------YSYASQ 504
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 505 EPWLF-NASVRDNILF-----GLPMD--KQRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRA 576
Cdd:cd03269 78 ERGLYpKMKVIDQLVYlaqlkGLKKEeaRRRIDEWLERLELSEYAN----------KRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 577 DVYLLDDPLSAVDThVGRHLFDECMRGFLGK-QLVILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:cd03269 148 ELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
449-616 |
3.43e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 449 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyASQEPWLF---------NA-----SVR 514
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAeachylghrNAmkpalTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFglpmdkqrYRTVL--KRCALERDLELLhGDGTIVGERGASLSGGQRARICLAR--AVYRRadVYLLDDPLSAVDT 590
Cdd:PRK13539 92 ENLEF--------WAAFLggEELDIAAALEAV-GLAPLAHLPFGYLSAGQKRRVALARllVSNRP--IWILDEPTAALDA 160
|
170 180
....*....|....*....|....*..
gi 28574259 591 HvGRHLFDECMRGFLGKQ-LVILVTHQ 616
Cdd:PRK13539 161 A-AVALFAELIRAHLAQGgIVIAATHI 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1049-1283 |
5.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPcVLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRlsYNDGAILIDSLDTNDIGLHDLRS 1125
Cdd:PRK13642 5 LEVENLVFKYEKESDVN-QLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEP-VLFSGTMRYNLDPF----EQYPDDKLWKALEDVHLKEEISELPsglqsiiSEGGTNFSVGQRQLVCLARA 1200
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIrNKFKD---CTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYELLTASKA 1277
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVI-HEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
....*.
gi 28574259 1278 KVFHGM 1283
Cdd:PRK13642 234 MVEIGL 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1083-1260 |
5.71e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.22 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1083 IVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSK----ISIIPQEPVLFSGTMRYNLdPFEQYPDDKLW 1157
Cdd:cd03290 32 IVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENI-TFGSPFNKQRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1158 KALEDV-HLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDALIQATIRNKFKD 1235
Cdd:cd03290 111 KAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQD 190
|
170 180
....*....|....*....|....*..
gi 28574259 1236 --CTVLTIAHRLNTIMDSDKVLVMDAG 1260
Cdd:cd03290 191 dkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
447-634 |
6.22e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 447 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQ----AILGELPPES------GSVQVSGKYS-----------YASQE 505
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRLArdirksrantgYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 PWLFNA-SVRDNILFGLPMDKQRYRTVLK---RCALERDLELLH--GDGTIVGERGASLSGGQRARICLARAVYRRADVY 579
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALGSTPFWRTCFSwftREQKQRALQALTrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 580 LLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVT-HQLQF-LEDADLIVIMDKGHV 634
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1289 |
7.30e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.88 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSLDTNDIGLH 1121
Cdd:PRK14247 3 KIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQEPVLFSgtmryNLDPFEQYP---------------DDKLWKALEDVHLKEEISE---LPSGlqsiiseg 1183
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIP-----NLSIFENVAlglklnrlvkskkelQERVRWALEKAQLWDEVKDrldAPAG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1184 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAH------RLntimdSDKVLVM 1257
Cdd:PRK14247 146 --KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFL 218
|
250 260 270
....*....|....*....|....*....|..
gi 28574259 1258 DAGHVVEFGSPYELLTASKAKVFHGMVmqTGK 1289
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNPRHELTEKYV--TGR 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
430-662 |
7.68e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ-----VSGKYSYASQ 504
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 505 E----PWLFNA----SVRDNIL-----FGLPMDKQRYR--TVLKRCALERDLEllhgdgTIVGErgasLSGGQRARICLA 569
Cdd:PRK13537 81 RvgvvPQFDNLdpdfTVRENLLvfgryFGLSAAAARALvpPLLEFAKLENKAD------AKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGKQLVILVThqLQFLEDA----DLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLT--THFMEEAerlcDRLCVIEEGRKIAEGAPHALIE 227
|
250 260 270
....*....|....*....|....*....|...
gi 28574259 646 S----------GQDFAQL------LVESTQNSG 662
Cdd:PRK13537 228 SeigcdvieiyGPDPVALrdelapLAERTEISG 260
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1049-1278 |
7.99e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.05 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLsyNDGAILIDSLDTNDIGLHDlRS 1125
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKP--DSGKILLDGQDITKLPMHK-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISII--PQEPVLFSG-TMRYNLDPF--EQYPDDKLWKALedvhLKEEISELpsGLQSIISEGGTNFSVGQRQLVCLARA 1200
Cdd:cd03218 74 RLGIGylPQEASIFRKlTVEENILAVleIRGLSKKEREEK----LEELLEEF--HITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAK 1278
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1049-1230 |
8.59e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 80.22 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGlHDLRSKI 1127
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgLLPPSAGEVLWNGEPIRDAR-EDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFSG-TMRYNLDpF------EQYPDDKLWKALEDVHLkEEISELPSGlqsiiseggtNFSVGQRQLVCLARA 1200
Cdd:COG4133 78 AYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARL 145
|
170 180 190
....*....|....*....|....*....|
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIR 1230
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
431-618 |
1.01e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS-- 503
Cdd:PRK14243 8 ETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 -------------QEPWLFNASVRDNILFGL-------PMDKQRYRTvLKRCALERDLEllhgdgTIVGERGASLSGGQR 563
Cdd:PRK14243 85 dpvevrrrigmvfQKPNPFPKSIYDNIAYGAringykgDMDELVERS-LRQAALWDEVK------DKLKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 564 ARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTHQLQ 618
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1068-1307 |
1.10e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLsyNDGAILIDSLDTNDIG-LHDLRSKISIIPQEPV-------- 1135
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRP--QKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtqfvgrtv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1136 ---LFSGTMRYNLDPFEqypddklWKALEDVHLKEeiselpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDE 1212
Cdd:PRK13644 96 eedLAFGPENLCLPPIE-------IRKRVDRALAE------IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1213 ATANVDPQT-DALIQATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPyelltaskAKVFHGMVMQTGKAS 1291
Cdd:PRK13644 163 VTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP--------ENVLSDVSLQTLGLT 234
|
250
....*....|....*.
gi 28574259 1292 FDHLLKVAENTKQNHI 1307
Cdd:PRK13644 235 PPSLIELAENLKMHGV 250
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1067-1272 |
1.76e-16 |
|
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: 80.46 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLIN--ALFrLSYNDGAILIDSLD-TNdigLHDLRSKISIIPQEPVLFSgtmry 1143
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLEtiAGF-IKPDSGKILLNGKDiTN---LPPEKRDISYVPQNYALFP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLDPFE--QYPDDKLWKALEDVHLK-EEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1220
Cdd:cd03299 85 HMTVYKniAYGLKKRKVDKKEIERKvLEIAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1221 T-DALIQ--ATIRNKFkDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:cd03299 164 TkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
452-645 |
2.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---------------KYSYASQEP--WLFNASVR 514
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFGlPMD--------KQRYRTVLKRCALERDlellhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK13637 103 KDIAFG-PINlglseeeiENRVKRAMNIVGLDYE--------DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 587 AVDTHvGRhlfDECMrgFLGKQL-------VILVTHQlqfLED----ADLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK13637 174 GLDPK-GR---DEIL--NKIKELhkeynmtIILVSHS---MEDvaklADRIIVMNKGKCELQGTPREVFK 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
433-643 |
2.68e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWgQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------------- 498
Cdd:PRK11607 19 LLEIRNLTKSF-DGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpinm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 --YSYAsqepwLF-NASVRDNILFGLPMDKQRYRTVLKRcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRR 575
Cdd:PRK11607 96 mfQSYA-----LFpHMTVEQNIAFGLKQDKLPKAEIASR--VNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 576 ADVYLLDDPLSAVDTHVGRHLFDECMrGFLGKQLV--ILVTH-QLQFLEDADLIVIMDKGHVSACGTYEEM 643
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVV-DILERVGVtcVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
449-616 |
3.12e-16 |
|
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: 78.55 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 449 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS------------YASQEPWLFNA-SVRD 515
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrdephenilYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKrcALERdLELLHGDGTIVgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGRH 595
Cdd:TIGR01189 93 NLHFWAAIHGGAQRTIED--ALAA-VGLTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVA 164
|
170 180
....*....|....*....|..
gi 28574259 596 LFDECMRGFLGKQ-LVILVTHQ 616
Cdd:TIGR01189 165 LLAGLLRAHLARGgIVLLTTHQ 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
453-638 |
3.68e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 453 NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG-----------------ELPPESGSVQVSGKySYASQePWLfnaSVRD 515
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGMVFQ-SYALY-PHL---SVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKRC-ALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGR 594
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVnQVAEVLQLAH----LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 28574259 595 HLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACG 638
Cdd:PRK11000 171 QMRIEISR--LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1052-1276 |
4.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTnsPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILID----SLDTNDIGLH 1121
Cdd:PRK13641 6 ENVDYIYSPGT--PMEKKGLdniSFELEEGSFVALVGHTGSGKSTLMqhfNALLKPS--SGTITIAgyhiTPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQ--EPVLFSGTM-------RYNLDPFEQYPDDKLWKALEDVHLKEEiselpsglqsIISEGGTNFSVGQR 1192
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVlkdvefgPKNFGFSEDEAKEKALKWLKKVGLSED----------LISKSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTdaliQATIRNKFKDC-----TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
250
....*....|
gi 28574259 1267 SPYELLTASK 1276
Cdd:PRK13641 228 SPKEIFSDKE 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
434-638 |
4.32e-16 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 78.39 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGqeqHDLVLNNVNMSLRRGqLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------KYSY 501
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 502 ASQEPWLF-NASVRDNIlfglpmdkqRYRTVLKRC-------ALERDLELLHgDGTIVGERGASLSGGQRARICLARAVY 573
Cdd:cd03264 77 LPQEFGVYpNFTVREFL---------DYIAWLKGIpskevkaRVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 574 RRADVYLLDDPLSAVDT---HVGRHLFDEcmrgfLGK-QLVILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:cd03264 147 GDPSILIVDEPTAGLDPeerIRFRNLLSE-----LGEdRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1052-1287 |
4.37e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILIDSLDT---NDIGLHDLRS 1125
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLERPT--SGRVLVDGQDLtalSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSG-TMRYNLD-PFE--QYPDDKLWKA----LEDVHLKEEISELPSglqsiiseggtNFSVGQRQLVCL 1197
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVAlPLElaGTPKAEIKARvtelLELVGLSDKADRYPA-----------QLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1198 ARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRlntiMD-----SDKVLVMDAGHVVEFGSPYE 1270
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDAGRLVEQGTVSE 227
|
250
....*....|....*..
gi 28574259 1271 LLTASKAKVFHGMVMQT 1287
Cdd:PRK11153 228 VFSHPKHPLTREFIQST 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1067-1264 |
4.92e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLF------- 1137
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSgVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 ----------SGTMRynldpfeqypddklWKALE------------DVHLKEEISELpsglqsiiseggtnfSVGQRQLV 1195
Cdd:COG1129 99 niflgreprrGGLID--------------WRAMRrrarellarlglDIDPDTPVGDL---------------SVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1196 CLARAILRENRILVMDEATANVDPQ-TDALIqATIRnKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEReVERLF-RIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
450-638 |
6.03e-16 |
|
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: 78.47 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGK----------YSYASQ-EPWLFNASVRD 515
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpdqfqkcVAYVRQdDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKRCALERDLELLH-GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH--- 591
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRVEDVLLRDlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFtal 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 592 -VGRHLFDECMRGflgkQLVILVTHQ-----LQFLedaDLIVIMDKGHVSACG 638
Cdd:cd03234 181 nLVSTLSQLARRN----RIVILTIHQprsdlFRLF---DRILLLSSGEIVYSG 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1049-1278 |
6.15e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.05 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-------------SYNDGAILIDSLDT 1115
Cdd:PRK14239 6 LQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpevtitgsiVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1116 NDiglhdLRSKISIIPQEPVLFSGT--------MRYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsIISEGGTNF 1187
Cdd:PRK14239 82 VD-----LRKEIGMVFQQPNPFPMSiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
250
....*....|..
gi 28574259 1267 SPYELLTASKAK 1278
Cdd:PRK14239 230 DTKQMFMNPKHK 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1066-1244 |
7.72e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1066 CVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGailidsldtnDIGLHDlRSKISIIPQEPVLFSGTMRyn 1144
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG----------RIGMPE-GEDLLFLPQRPYLPLGTLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 ldpfEQ--YPddklWkaledvhlkeeiselpsglqsiisegGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1222
Cdd:cd03223 82 ----EQliYP----W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 28574259 1223 ALIQATIRNKFkdCTVLTIAHR 1244
Cdd:cd03223 128 DRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1067-1262 |
8.18e-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: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILID--SLDTNDIGLHDLRSKISIIPQepvlfsgtmRY 1143
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIIIDglKLTDDKKNINELRQKVGMVFQ---------QF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLDPF------------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILREN 1205
Cdd:cd03262 86 NLFPHltvlenitlapikvkgmsKAEAEERALELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1206 RILVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHV 1262
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
276-644 |
8.48e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.46 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 276 NEIISGIQVIKMYTWERPFGKLIGQMRRSEMSSIRQMNLLRGILLSFEITLGRIAIFVSLL---GF----VLGGGELTAe 348
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCGLLmlfGFsasgTIEVGVLYA- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 349 rafcvtaFYNILRRTVSKF--FPSGMSQFAELLVSMRRITNFMMREeanvidmserRDEKAEEEQhllkevekrsyPVGI 426
Cdd:PRK10790 287 -------FISYLGRLNEPLieLTTQQSMLQQAVVAGERVFELMDGP----------RQQYGNDDR-----------PLQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 427 GKepdtlVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK----YSYA 502
Cdd:PRK10790 339 GR-----IDIDNVSFAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplssLSHS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 S---------QEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALErdlELLHG--DG--TIVGERGASLSGGQRARICLA 569
Cdd:PRK10790 412 VlrqgvamvqQDPVVLADTFLANVTLGRDISEEQVWQALETVQLA---ELARSlpDGlyTPLGEQGNNLSVGQKQLLALA 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGRHLfDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1049-1271 |
1.26e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.41 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLD-TNDIGlhDLRSK 1126
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHDvVREPR--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSG-TMRYNLDPFEQ---YPDDKLwkaledvhlKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARA 1200
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENLYIHARlygVPGAER---------RERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHrlntIMD-----SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTH----YMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
434-646 |
1.49e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYAS-------- 503
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvATTPSrelakrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ---QEPwLFNA--SVRDNILFG---------LPMDKQRYRTVLKRCALErDLELLHGDgtivgergaSLSGGQRARICLA 569
Cdd:COG4604 79 ilrQEN-HINSrlTVRELVAFGrfpyskgrlTAEDREIIDEAIAYLDLE-DLADRYLD---------ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgfLGKQlVILVTHQLQFLED-ADLIVIMDKGHVSACGTYE 641
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKhsvqmmkLLRRLADE-----LGKT-VVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
....*
gi 28574259 642 EMLKS 646
Cdd:COG4604 222 EIITP 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
451-643 |
1.53e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---------------YSYASQEPWLFNASVRD 515
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFG---LPMD----KQRYRTVLKRCALE--RDLELLHgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK13652 99 DIAFGpinLGLDeetvAHRVSSALHMLGLEelRDRVPHH------------LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 587 AVDTHVGRHLFDeCMRGFLGK--QLVILVTHQLQFL-EDADLIVIMDKGHVSACGTYEEM 643
Cdd:PRK13652 167 GLDPQGVKELID-FLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
451-644 |
1.79e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQE--------PWLFNA----SVRDN 516
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQlarrlallPQHHLTpegiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 ILFG----LPM-------DKQRyrtvlkrcaLERDLELLHGDgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPL 585
Cdd:PRK11231 97 VAYGrspwLSLwgrlsaeDNAR---------VNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 586 SAVDTHvgrHLFdECMRgfLGKQL------VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:PRK11231 167 TYLDIN---HQV-ELMR--LMRELntqgktVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
452-634 |
1.84e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.33 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQ--EPWLFNAS 512
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGlPM------DKQRYRTV--LKRCALERDLellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYLLDDP 584
Cdd:PRK13641 103 VLKDVEFG-PKnfgfseDEAKEKALkwLKKVGLSEDL---------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 585 LSAVDTHvGRHlfdECMRGFLGKQ----LVILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:PRK13641 173 AAGLDPE-GRK---EMMQLFKDYQkaghTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
451-642 |
2.43e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLF-NASVRD 515
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpCARLTpakahqlgiylvpQEPLLFpNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLP---MDKQRYRTVLKRCALERDLELLHGdgtivgergaSLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PRK15439 106 NILFGLPkrqASMQKMKQLLAALGCQLDLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 593 GRHLFDEcMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEE 642
Cdd:PRK15439 176 TERLFSR-IRELLAQGVgIVFISHKLpEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1052-1273 |
2.65e-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: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLRSKISII 1130
Cdd:cd03295 4 ENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTsGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQEPVLFSG-TMRYN--LDP-FEQYP----DDKLWKALEDVHLKEE--ISELPSGLqsiiseggtnfSVGQRQLVCLARA 1200
Cdd:cd03295 81 IQQIGLFPHmTVEENiaLVPkLLKWPkekiRERADELLALVGLDPAefADRYPHEL-----------SGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLN-TIMDSDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
451-650 |
3.10e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------Y-------SYASQEPWLF-NASVRD 515
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmHkrarlgiGYLPQEASIFrKLTVED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NIL-----FGLPMDKQRYRTVlkrcALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD- 589
Cdd:COG1137 98 NILavlelRKLSKKEREERLE----ELLEEFGITH----LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 590 ------THVGRHLFDecmRGfLGkqlvILVT-HQ----LQfledadlIV----IMDKGHVSACGTYEEMLKS-------- 646
Cdd:COG1137 170 iavadiQKIIRHLKE---RG-IG----VLITdHNvretLG-------ICdrayIISEGKVLAEGTPEEILNNplvrkvyl 234
|
....
gi 28574259 647 GQDF 650
Cdd:COG1137 235 GEDF 238
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
424-644 |
3.69e-15 |
|
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: 76.87 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 424 VGIGKEpdtlVEIKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------ 497
Cdd:cd03288 14 VGLGGE----IKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 -------KYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLA 569
Cdd:cd03288 89 plhtlrsRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGlDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFlGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAF-ADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
433-634 |
3.97e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARW--GQEQHDlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQaILGEL-PPESGSVQVSGKySYASQEPWLF 509
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVE-VLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQ-DVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 NASVRDNilFGLPMdkQRYRT------------------VLKRCALERDLELLH--GDGTIVGERGASLSGGQRARICLA 569
Cdd:PRK10535 81 AQLRREH--FGFIF--QRYHLlshltaaqnvevpavyagLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGrhlfDECMRgfLGKQL------VILVTHQLQFLEDADLIVIMDKGHV 634
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSG----EEVMA--ILHQLrdrghtVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
451-616 |
4.45e-15 |
|
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: 75.22 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------KYSYASQEPWLFNA-------SVRDNI 517
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYLGHApgikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLPmdkqryrtvlkrcalerdlelLHGDGTI------VGERG------ASLSGGQRARICLARAVYRRADVYLLDDPL 585
Cdd:cd03231 95 RFWHA---------------------DHSDEQVeealarVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|..
gi 28574259 586 SAVDTHvGRHLFDECMRGFLGK-QLVILVTHQ 616
Cdd:cd03231 154 TALDKA-GVARFAEAMAGHCARgGMVVLTTHQ 184
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
452-590 |
5.18e-15 |
|
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: 75.52 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----------------KYSYASQE-PWLFNASVR 514
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDfRLLPDRNVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 515 DNILFGLPMDKQRYRTVLKRC--ALERdLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVpaALEL-VGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
436-634 |
5.85e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 436 IKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVqVSGKYSYAS---------QE- 505
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEaredtrlmfQDa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 ---PWlfnASVRDNILFGLPMD-KQRYRTVLKRCAL-ERdlellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYL 580
Cdd:PRK11247 91 rllPW---KKVIDNVGLGLKGQwRDAALQALAAVGLaDR-----------ANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 581 LDDPLSAVD--THVG-RHLFDECMR--GFlgkqLVILVTHQL-QFLEDADLIVIMDKGHV 634
Cdd:PRK11247 157 LDEPLGALDalTRIEmQDLIESLWQqhGF----TVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
451-638 |
6.27e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.51 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE--SGSVQVSGKysyaSQEPWLFNASV----RDNILFGlpmd 524
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGR----PLDKRSFRKIIgyvpQDDILHP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 525 kqrYRTVlkRCALERDLELlhgdgtivgeRGasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFdECMRGf 604
Cdd:cd03213 96 ---TLTV--RETLMFAAKL----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-SLLRR- 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 28574259 605 LGKQ--LVILVTHQL--QFLEDADLIVIMDKGHVSACG 638
Cdd:cd03213 157 LADTgrTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1070-1271 |
6.48e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.46 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1070 GLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDLRSKISIIPQEPvlFSgtmryNL 1145
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLeEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YA-----SL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 DP--------------FEQYP----DDKLWKALEDVHLKEE-ISELPSglqsiisEggtnFSVGQRQLVCLARAILRENR 1206
Cdd:COG4608 109 NPrmtvgdiiaeplriHGLASkaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1207 ILVMDEATAnvdpqtdAL---IQATIRNKFKD------CTVLTIAHRLNT---ImdSDKVLVMDAGHVVEFGSPYEL 1271
Cdd:COG4608 178 LIVCDEPVS-------ALdvsIQAQVLNLLEDlqdelgLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1053-1266 |
6.60e-15 |
|
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: 75.10 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1053 DLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLhDLRSKISIIP 1131
Cdd:cd03266 6 ALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDGFDVVKEPA-EARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1132 QEPVLFSG-TMRYNLDPFEQY---PDDKLWKALEDVHLKEEISELpsglqsiISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:cd03266 85 DSTGLYDRlTARENLEYFAGLyglKGDELTARLEELADRLGMEEL-------LDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 1208 LVMDEATANVD-PQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03266 158 LLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
452-645 |
7.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFNAS 512
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpvrkkvgvvfqfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGlPMDKQRYRTVLKRCALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 593 GRHLFDECMRGFLGKQLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
430-644 |
8.40e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK---YS------ 500
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidYSrkglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 --------YASQEPWLFNASVRDNILFG-----LPMD--KQRYRTVLKRCALERdlelLHGDGTivgergASLSGGQRAR 565
Cdd:PRK13636 80 lresvgmvFQDPDNQLFSASVYQDVSFGavnlkLPEDevRKRVDNALKRTGIEH----LKDKPT------HCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 566 ICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDECMRGfLGKQLVIlVTHQLQFLE-DADLIVIMDKGHVSACGTYE 641
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKE-LGLTIII-ATHDIDIVPlYCDNVFVMKEGRVILQGNPK 227
|
...
gi 28574259 642 EML 644
Cdd:PRK13636 228 EVF 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1066-1266 |
8.84e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 74.12 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1066 CVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FRLSYND-GAILIDSLdtnDIGLHDLRSKISIIPQEPVLFSgtmr 1142
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVsGEVLINGR---PLDKRSFRKIIGYVPQDDILHP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 yNLDPFEQypddkLWKALEdvhlkeeiselpsgLQSIiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1222
Cdd:cd03213 96 -TLTVRET-----LMFAAK--------------LRGL--------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28574259 1223 ALIQATIRNKFKD-CTVLTIAHRLNTIMDS--DKVLVMDAGHVVEFG 1266
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1047-1271 |
9.26e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.42 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINA---LFRLSynDGAILIDSLDTNDIGLHDl 1123
Cdd:COG3839 2 ASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLEDPT--SGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RsKISIIPQEPVLF-SGTMRYNLdpfeQYP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQ 1191
Cdd:COG3839 75 R-NIAMVFQSYALYpHMTVYENI----AFPlklrkvpkaeiDRRVREAAELLGLEDLLDRKPKQL-----------SGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQtdalIQATIRNKFKDctvltIAHRLNTIM-----D-------SDKVLVMDA 1259
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIKR-----LHRRLGTTTiyvthDqveamtlADRIAVMND 209
|
250
....*....|..
gi 28574259 1260 GHVVEFGSPYEL 1271
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
499-649 |
9.36e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 YSYASQEPWLFNASVRDNILFGLP-MDKQRYRTVLKRCALERDLELLHGD-GTIVGERGASLSGGQRARICLARAVYRRA 576
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 577 DVYLLDDPLSAVDTHvGRHLFDECMRGFLGK--QLVILVTHQLQFLEDADLIVIMDK-----GHVSACGTYEEMLkSGQD 649
Cdd:PTZ00265 1378 KILLLDEATSSLDSN-SEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELL-SVQD 1455
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
436-634 |
9.56e-15 |
|
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: 75.06 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 436 IKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASV- 513
Cdd:cd03267 20 IGSLKSLFKRKYREVEaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 ---RDNILFGLP-------------MDKQRYRTVLKRCALERDLE-LLHgdgTIVgergASLSGGQRARICLARAVYRRA 576
Cdd:cd03267 100 fgqKTQLWWDLPvidsfyllaaiydLPPARFKKRLDELSELLDLEeLLD---TPV----RQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 577 DVYLLDDPLSAVDTHVGRHLfdecmRGFLgKQL-------VILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENI-----RNFL-KEYnrergttVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1052-1273 |
1.06e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYepDTNSpcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILID--------SLDTNDIGLHDL 1123
Cdd:PRK14258 11 NNLSFYY--DTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RSKISIIPQEPVLFSGTM----RYNLDPFEQYP----DDKLWKALEDVHLKEEIselpsglQSIISEGGTNFSVGQRQLV 1195
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVydnvAYGVKIVGWRPkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1196 CLARAILRENRILVMDEATANVDPQTDALIQATIRNKF--KDCTVLTIAHRLNTIMD-SDKVLVMDA-----GHVVEFGS 1267
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
....*.
gi 28574259 1268 PYELLT 1273
Cdd:PRK14258 240 TKKIFN 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
444-634 |
1.11e-14 |
|
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: 75.61 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 444 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV--------QVSGKYSYASQE---------P 506
Cdd:TIGR02769 19 GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyQLDRKQRRAFRRdvqlvfqdsP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 WLFNA--SVRDNIlfGLPMdkqRYRTVLKRCA-LERDLELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYL 580
Cdd:TIGR02769 99 SAVNPrmTVRQII--GEPL---RHLTSLDESEqKARIAELLDMvglRSEDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 581 LDDPLSAVDTHVGRHLFD--ECMRGFLGKQLViLVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILEllRKLQQAFGTAYL-FITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1067-1268 |
1.16e-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: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSYndGAILIDSLDTNDIGLHDlRSKISIIP--QEPVLFSG-T 1140
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgfLRPTS--GSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1141 MRYNLD---------------PFEQYPD--DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILR 1203
Cdd:cd03219 92 VLENVMvaaqartgsglllarARREEREarERAEELLERVGLADLADRPAGEL-----------SYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1204 ENRILVMDEATANVDPQ-TDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1268
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTP 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1049-1272 |
1.27e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcvlKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNDGAILIDSLDTNDIGLHDlRsK 1126
Cdd:COG3840 2 LRLDDLTYRYGDFP------LRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNGQDLTALPPAE-R-P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSG-TMRYN----------LDPFEQypdDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLV 1195
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNiglglrpglkLTAEQR---AQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1196 CLARAILRENRILVMDEATANVDP----QTDALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1270
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
..
gi 28574259 1271 LL 1272
Cdd:COG3840 217 LL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
353-589 |
1.41e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 353 VTAFyNILRRTVSkFFPSGMSQFAELLVSMRRITNFMmreeaNVIDMSERRDEKAEeeqhllkevekrsypvGIGKEPDT 432
Cdd:COG4178 305 ASAF-GQVQGALS-WFVDNYQSLAEWRATVDRLAGFE-----EALEAADALPEAAS----------------RIETSEDG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQEPWLFN 510
Cdd:COG4178 362 ALALEDLTLRTPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFGLP---MDKQRYRTVLKRCALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:COG4178 440 GTLREALLYPATaeaFSDAELREALEAVGLGHLAERLD----EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
..
gi 28574259 588 VD 589
Cdd:COG4178 516 LD 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
427-649 |
1.43e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 427 GKEPDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--------- 497
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNR---CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 -------KYSYASQEPWLF-NASVRDNILFGLPMDKQRYRTVLKRCALERdLEllhgdgtIVGERGAS------LSGGQR 563
Cdd:PRK11831 78 rlytvrkRMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMK-LE-------AVGLRGAAklmpseLSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 564 ARICLARAVYRRADVYLLDDPLSAVD---THVGRHLFDEcMRGFLGKQLVIlVTHQL-QFLEDADLIVIMDKGHVSACGT 639
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDpitMGVLVKLISE-LNSALGVTCVV-VSHDVpEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|
gi 28574259 640 YEEmLKSGQD 649
Cdd:PRK11831 228 AQA-LQANPD 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
452-644 |
1.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS----------------YASQEPWLFNASVRD 515
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvgivFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFG---LPMDKQRYRTVLKRCALERDLELLHGDGTivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PRK13644 98 DLAFGpenLCLPPIEIRKRVDRALAEIGLEKYRHRSP------KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 593 GRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1272 |
1.83e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDS--LDTNDIGLHDL 1123
Cdd:PRK13636 6 LKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLfqnLNGILKPS--SGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RSKISIIPQEP--VLFSGTMRYNLD--PFE-QYPDDKLWKALEDVHLKEEISELPSGLQSIISeggtnfsVGQRQLVCLA 1198
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLS-------FGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFGSPYELL 1272
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1048-1280 |
1.94e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSK 1126
Cdd:PRK11231 2 TLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPISMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKLWKAL--EDVHL------KEEISELPSGLQsiiseggTNFSVGQRQLVCLA 1198
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLsaEDNARvnqameQTRINHLADRRL-------TDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIR---NKFKdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRelnTQGK--TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
....*..
gi 28574259 1275 SKAK-VF 1280
Cdd:PRK11231 229 GLLRtVF 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
392-638 |
2.35e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 392 EEANVIDMSERRDEKAEEEQHLLKEVEKRSYPvgiGKEPDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPV 471
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGISEAKASIP---GSMSTVAIDLAGVSKSYGDK---AVVNGLSFTVASGECFGLLGPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 472 GSGKSSLIQAILGELPPESGSVQVSG------------KYSYASQEPWL-FNASVRDNIL-FG--LPMDKQRYRTV---- 531
Cdd:PRK13536 77 GAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLdLEFTVRENLLvFGryFGMSTREIEAVipsl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 532 LKRCALERDLELlhgdgtivgeRGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHvGRHLFDECMRGFLGK-QLV 610
Cdd:PRK13536 157 LEFARLESKADA----------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARgKTI 225
|
250 260 270
....*....|....*....|....*....|..
gi 28574259 611 ILVTHqlqFLEDA----DLIVIMDKGHVSACG 638
Cdd:PRK13536 226 LLTTH---FMEEAerlcDRLCVLEAGRKIAEG 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1036-1273 |
3.15e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1036 EKQPPKSWPKEGKLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSYND------ 1105
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYCVFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVthfNGLIKSKYGTiqvgdi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1106 --GAILIDSLDTNDIG------LHDLRSKISIIPQEP--VLFSGTMR-------YNLDPFEQYPDDKLWKALEDVHLKEE 1168
Cdd:PRK13631 89 yiGDKKNNHELITNPYskkiknFKELRRRVSMVFQFPeyQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1169 ISEL-PSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA-LIQATIRNKFKDCTVLTIAHRLN 1246
Cdd:PRK13631 169 YLERsPFGL-----------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTME 237
|
250 260
....*....|....*....|....*...
gi 28574259 1247 TIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK13631 238 HVLEvADEVIVMDKGKILKTGTPYEIFT 265
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
430-636 |
4.41e-14 |
|
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: 73.24 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIqAILGEL-PPESGSVQVSGkysyasQEpw 507
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELtILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAGLdRPTSGTVRLAG------QD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 LFN------ASVR--------------------DNI-----LFGLPMDKQRYRTVLKRCALErdlELLHgdgtivgERGA 556
Cdd:COG4181 76 LFAldedarARLRarhvgfvfqsfqllptltalENVmlpleLAGRRDARARARALLERVGLG---HRLD-------HYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 557 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH----LFDecMRGFLGKQLViLVTHQLQFLEDADLIVIMDKG 632
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFE--LNRERGTTLV-LVTHDPALAARCDRVLRLRAG 222
|
....
gi 28574259 633 HVSA 636
Cdd:COG4181 223 RLVE 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1067-1270 |
5.07e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 73.53 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSynDGAILIDSLDTNDIGLHDL-RSKISIIPQEPVLFSG--- 1139
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItgfYRPT--SGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPEltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 ----------TMRYNLDPFEQYPD----------DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLAR 1199
Cdd:COG0411 97 lenvlvaahaRLGRGLLAALLRLPrarreerearERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1200 AILRENRILVMDEATANVDPQ-TDALIQaTIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1270
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEeTEELAE-LIRrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1049-1277 |
6.68e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL-INALFRLSYNDGAILI--DSLDTNDIGLHDLRS 1125
Cdd:PRK13638 2 LATSDLWFRYQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPvlfsgtmryNLDPFEQYPDDKLWKALEDVHLKE-EISELPSGLQSIISEGGTN------FSVGQRQLVCLA 1198
Cdd:PRK13638 78 QVATVFQDP---------EQQIFYTDIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI-AHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE 228
|
.
gi 28574259 1277 A 1277
Cdd:PRK13638 229 A 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1067-1271 |
7.45e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--------------FRLSY-----------NDG-----------AILI 1110
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHVALcekcgyverpsKVGepcpvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1111 DSLDTNDIGLHDLRSKISIIPQEPVLFSG--TMRYN-LDPFEQ--YP-DDKLWKA---LEDVHLKEEISELPSGLqsiis 1181
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAvdlIEMVQLSHRITHIARDL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1182 eggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMD 1258
Cdd:TIGR03269 170 ------SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250
....*....|...
gi 28574259 1259 AGHVVEFGSPYEL 1271
Cdd:TIGR03269 244 NGEIKEEGTPDEV 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
431-634 |
8.13e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 70.92 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARwgqeqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASqepwlfn 510
Cdd:cd03215 2 EPVLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 aSVRDNILFGL---PMDKQRYRTVLKRcALERDLELlhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:cd03215 68 -SPRDAIRAGIayvPEDRKREGLVLDL-SVAENIAL-----------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 588 VDthVG-----RHLFDECMRGFLGkqlVILVTHQLQ-FLEDADLIVIMDKGHV 634
Cdd:cd03215 135 VD--VGakaeiYRLIRELADAGKA---VLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
452-679 |
8.99e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQE-PWLFNASVRDNIL 518
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvaYVPQSEEvDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 519 FGL-----------PMDKQRYRTVLKRCALerdLELLHGDgtiVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:PRK15056 103 MGRyghmgwlrrakKRDRQIVTAALARVDM---VEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 588 VDTHVG-------RHLFDEcmrgflGKQLVIlVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSG---QDFAQLLVES 657
Cdd:PRK15056 173 VDVKTEariisllRELRDE------GKTMLV-STHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEnleLAFSGVLRHV 245
|
250 260
....*....|....*....|....*
gi 28574259 658 TQnSGGGDEIITS---PNLSRQSSA 679
Cdd:PRK15056 246 AL-NGSEESIITDderPFISHRPAA 269
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1052-1274 |
9.00e-14 |
|
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: 72.81 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEpDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL---SYNDGAILIDsldtNDIG---LHDLRS 1125
Cdd:COG1119 7 RNVTVRRG-GKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlppTYGNDVRLFG----ERRGgedVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISII---------PQEPVL------FSGTmrynLDPFEQYPD---DKLWKALEDVHLKEEISELPSGLqsiiseggtnf 1187
Cdd:COG1119 79 RIGLVspalqlrfpRDETVLdvvlsgFFDS----IGLYREPTDeqrERARELLELLGLAHLADRPFGTL----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMDS-DKVLVMDAGHVVE 1264
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
250
....*....|
gi 28574259 1265 FGSPYELLTA 1274
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1069-1271 |
9.99e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1069 KGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILI---DSLDTNDIGLHDLRSKISIIPQEPvLFSGTMRYN 1144
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLvKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 L-----DPFEQY-PDdklwkaLEDVHLKEEISE--LPSGL-QSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:PRK15079 117 IgeiiaEPLRTYhPK------LSRQEVKDRVKAmmLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1216 NVDPQtdalIQATIRNKFKDC------TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:PRK15079 191 ALDVS----IQAQVVNLLQQLqremglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-644 |
1.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPE---SGSVQVSGKYSYAS----- 503
Cdd:PRK14247 4 IEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQDIFKMdviel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 --------QEP-WLFNASVRDNILFGLPMDK---------QRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQRAR 565
Cdd:PRK14247 81 rrrvqmvfQIPnPIPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEVK------DRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 566 ICLARAVYRRADVYLLDDP---LSAVDTHVGRHLFDEcmrgfLGKQL-VILVTH-QLQFLEDADLIVIMDKGHVSACGTY 640
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPtanLDPENTAKIESLFLE-----LKKDMtIVLVTHfPQQAARISDYVAFLYKGQIVEWGPT 229
|
....
gi 28574259 641 EEML 644
Cdd:PRK14247 230 REVF 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-675 |
1.28e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAiLGELPPESGSVQVSGKYSYASQ---------------------EPWLF 509
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnlnrlrrqvsmvhpKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 NASVRDNILFGLPMDKQRYRTVLK---RCALeRDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGWRPKLEIDdivESAL-KDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 587 AVDTHVGRHLFDECMRGFLGKQL-VILVTHQLQfledadlivimdkgHVSACGTYEEMLKSGQDFAQLLVEstqnSGGGD 665
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELtMVIVSHNLH--------------QVSRLSDFTAFFKGNENRIGQLVE----FGLTK 241
|
250
....*....|
gi 28574259 666 EIITSPNLSR 675
Cdd:PRK14258 242 KIFNSPHDSR 251
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
451-643 |
1.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG---KYSYAS------------QEP--WLFNASV 513
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepiKYDKKSllevrktvgivfQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFG-----LPMD--KQRYRTVLKRCALErdlellhgdgtivG-ERGAS--LSGGQRARICLARAVYRRADVYLLDD 583
Cdd:PRK13639 97 EEDVAFGplnlgLSKEevEKRVKEALKAVGME-------------GfENKPPhhLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 584 PLSAVD----THVGRHLFDECMRGFlgkqLVILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEM 643
Cdd:PRK13639 164 PTSGLDpmgaSQIMKLLYDLNKEGI----TIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1072-1279 |
1.31e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1072 SFTIQPMEKVGIVGRTGAGKSSLIN--ALFrLSYNDGAILIDSLDTNDIGlhDLRSKISIIPQEPVLFSG-TMRYN---- 1144
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTTP--PSRRPVSMLFQENNLFSHlTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 LDP---FEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDP-- 1219
Cdd:PRK10771 96 LNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1220 --QTDALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT--ASKAKV 1279
Cdd:PRK10771 165 rqEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSgkASASAL 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
446-646 |
1.34e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 446 EQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS------------QEP--WLFN 510
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItISKENlkeirkkigiifQNPdnQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFGLP---MDKQRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:PRK13632 99 ATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGME------DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 588 VDTHvGRHLFDECMRGF--LGKQLVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:PRK13632 173 LDPK-GKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
444-634 |
1.56e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 444 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYASQE-------------P 506
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaKLNRAQRKafrrdiqmvfqdsI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 WLFNA--SVRDNIlfGLPMdkqRYRTVLKRCA-LERDLELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYL 580
Cdd:PRK10419 100 SAVNPrkTVREII--REPL---RHLLSLDKAErLARASEMLRAvdlDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 581 LDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHV 634
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKK--LQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1068-1263 |
1.74e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILID--------SLDTNDIGlhdlrskISIIPQEPVLF- 1137
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDsGEILIDgkpvrirsPRDAIALG-------IGMVHQHFMLVp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 ------------SGTMRYNLDPfeqypdDKLWKALE--------DVHLKEEISELpsglqsiiseggtnfSVGQRQLVCL 1197
Cdd:COG3845 94 nltvaenivlglEPTKGGRLDR------KAARARIRelseryglDVDPDAKVEDL---------------SVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1198 ARAILRENRILVMDEATANVDPQ-TDALIqATIRnKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQeADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
451-632 |
2.13e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVsgkysyaSQEPWLFNASVRDNILFGLPMDKQRY 528
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV-------PDNQFGREASLIDAIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 529 rtVLKRCALerdlellhGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH----VGRHLFDECMRgf 604
Cdd:COG2401 118 --LLNAVGL--------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrVARNLQKLARR-- 185
|
170 180 190
....*....|....*....|....*....|
gi 28574259 605 LGKQLVIlVTHQLQFLED--ADLIVIMDKG 632
Cdd:COG2401 186 AGITLVV-ATHHYDVIDDlqPDLLIFVGYG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
452-653 |
2.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.12 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-------KYSYASQ------------EPWLFNAS 512
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPvrkrigmvfqfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFG-----LPMD--KQRYRTVLKRCALERDlellhgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPL 585
Cdd:PRK13646 103 VEREIIFGpknfkMNLDevKNYAHRLLMDLGFSRD---------VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 586 SAVDTHvGRHlfdECMRGFLGKQL-----VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQL 653
Cdd:PRK13646 174 AGLDPQ-SKR---QVMRLLKSLQTdenktIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1277 |
2.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILID--SLDTNDIGLHDL 1123
Cdd:PRK13639 2 LETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPT--SGEVLIKgePIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1124 RSKISIIPQEpvlfsgtmrynldpfeqyPDDKLW--KALEDVHL--------KEEISE-LPSGLQSIISEGGTN-----F 1187
Cdd:PRK13639 77 RKTVGIVFQN------------------PDDQLFapTVEEDVAFgplnlglsKEEVEKrVKEALKAVGMEGFENkpphhL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKfKDCTVLTIAHRLNTI-MDSDKVLVMDAGHVVE 1264
Cdd:PRK13639 139 SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNK-EGITIIISTHDVDLVpVYADKVYVMSDGKIIK 217
|
250
....*....|...
gi 28574259 1265 FGSPYELLTASKA 1277
Cdd:PRK13639 218 EGTPKEVFSDIET 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
451-629 |
3.10e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLF-NASVRD 515
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpVRFRSprdaqaagiaiihQELNLVpNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLP------MDK----QRYRTVLKRCALERDLEllhgdgTIVGErgasLSGGQRARICLARAVYRRADVYLLDDP- 584
Cdd:COG1129 99 NIFLGREprrgglIDWramrRRARELLARLGLDIDPD------TPVGD----LSVAQQQLVEIARALSRDARVLILDEPt 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 585 --LSAVDThvgRHLFDeCMRgflgkQL------VILVTHQL-QFLEDADLIVIM 629
Cdd:COG1129 169 asLTEREV---ERLFR-IIR-----RLkaqgvaIIYISHRLdEVFEIADRVTVL 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
161-602 |
3.98e-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: 74.01 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 161 LAMKMRVAVSSAIYRKalrlsrtSLGGTTTGQVVNL----------LSNDLNRFDRCLIHFHFLWLGP-LELLIASYFLY 229
Cdd:TIGR00954 162 LKLRFRVRLTRYLYSK-------YLSGFTFYKVSNLdsriqnpdqlLTQDVEKFCDSVVELYSNLTKPiLDVILYSFKLL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 230 EQIG------MASFYGISILVLylplqTYLSRVTSKLRLQTAlRTDQRVRMMN-EIISGIQVIKMY--------TWERPF 294
Cdd:TIGR00954 235 TALGsvgpagLFAYLFATGVVL-----TKLRPPIGKLTVEEQ-ALEGEYRYVHsRLIMNSEEIAFYqgnkvekeTVMSSF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 295 GKLIGQMRRSEMSSIrQMNLLRGILLSFEIT-LGRIAIFVSLLgFVLGGGELTAERAFCVTAFYNILRRTVSkfFPSGMS 373
Cdd:TIGR00954 309 YRLVEHLNLIIKFRF-SYGFLDNIVAKYTWSaVGLVAVSIPIF-DKTHPAFLEMSEEELMQEFYNNGRLLLK--AADALG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 374 QFAELLVSMRRITNFMMR--EEANVIDMSERRDEK--AEEEQHLLKEVEKRSYPV-GIGKEPDTLVEIKALRARWGQEQH 448
Cdd:TIGR00954 385 RLMLAGRDMTRLAGFTARvdTLLQVLDDVKSGNFKrpRVEEIESGREGGRNSNLVpGRGIVEYQDNGIKFENIPLVTPNG 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 449 DLVLNNVNMSLRRGQLVAVIGPVGSGKSSLiQAILGELPPESG---SVQVSGKYSYASQEPWLFNASVRDNILFglPMDK 525
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSL-FRILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 526 -QRYRTVLKRCALERDLELLHGDGTIVGERGAS--------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHL 596
Cdd:TIGR00954 542 eDMKRRGLSDKDLEQILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
....*.
gi 28574259 597 FDECMR 602
Cdd:TIGR00954 622 YRLCRE 627
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
433-638 |
4.11e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQ-HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGkySYASQEP----- 506
Cdd:cd03266 1 MITADALTKRFRDVKkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 ---WLFNA-------SVRDNI-----LFGLPMD--KQRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLA 569
Cdd:cd03266 79 rlgFVSDStglydrlTARENLeyfagLYGLKGDelTARLEELADRLGMEELLD----------RRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1052-1263 |
4.44e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDT-NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL---FRLSynDGAILIDSLDTNDIGLHDlRSK- 1126
Cdd:COG1101 5 KNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIagsLPPD--SGSILIDGKDVTKLPEYK-RAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLfsGT---M--------------RYNLDPfeqypddKLWKALEDvHLKEEISELPSGLQSIISEGGTNFSV 1189
Cdd:COG1101 82 IGRVFQDPMM--GTapsMtieenlalayrrgkRRGLRR-------GLTKKRRE-LFRELLATLGLGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1190 GQRQLVCLARAILRENRILVMDEATANVDPQTDALI-QATirNKF---KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlELT--EKIveeNNLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
434-652 |
4.74e-13 |
|
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: 71.04 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-------------KYS 500
Cdd:cd03289 3 MTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswnsvplqkwrkAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 501 YASQEPWLFNASVRDNI-LFGLPMDKQRYR--------TVLKRCALERDLELLHGdgtivgerGASLSGGQRARICLARA 571
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLdPYGKWSDEEIWKvaeevglkSVIEQFPGQLDFVLVDG--------GCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 572 VYRRADVYLLDDPLSAVD-------THVGRHLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDpityqviRKTLKQAFADCT--------VILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
....*...
gi 28574259 645 KSGQDFAQ 652
Cdd:cd03289 225 NEKSHFKQ 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
451-634 |
6.09e-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: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------YSYAS------QEPWL---FNASVR 514
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeYKRAKyigrvfQDPMMgtaPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNIL--------FGLPM-----DKQRYRTVLKRcaLERDLE--LlhgdGTIVGergaSLSGGQRARICLARAVYRRADVY 579
Cdd:COG1101 101 ENLAlayrrgkrRGLRRgltkkRRELFRELLAT--LGLGLEnrL----DTKVG----LLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 580 LLDDPLSAVDTHVGRHLFDecmrgfLGKQLV-------ILVTHQLQF-LEDADLIVIMDKGHV 634
Cdd:COG1101 171 LLDEHTAALDPKTAALVLE------LTEKIVeennlttLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-615 |
8.85e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI--LGELPPES---GSVQVSGKYSYAS----- 503
Cdd:PRK14267 5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRLFGRNIYSPdvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ----------QEPWLF-NASVRDNILFGLPMDK---------QRYRTVLKRCALERDLEllhgdgTIVGERGASLSGGQR 563
Cdd:PRK14267 82 evrrevgmvfQYPNPFpHLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVK------DRLNDYPSNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 564 ARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLVILVTH 615
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTH 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
431-641 |
9.53e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--------- 499
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 500 --------------------SYASQEP--WLFNASVRDNILFG---LPMDKQRYRTVLKRCalerdLELLHGDGTIVGER 554
Cdd:PRK13631 99 litnpyskkiknfkelrrrvSMVFQFPeyQLFKDTIEKDIMFGpvaLGVKKSEAKKLAKFY-----LNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 555 GASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKGH 633
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGK 253
|
....*....
gi 28574259 634 VSACGT-YE 641
Cdd:PRK13631 254 ILKTGTpYE 262
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
403-670 |
1.30e-12 |
|
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: 73.12 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 403 RDEKA-EEEQHLLKEVEKRSYPVGIGkepDTLVEIKALRARWGQEQHDLV----------LNNVNMSLRRGQLVAVIGPV 471
Cdd:TIGR01257 889 REERAlEKTEPLTEEMEDPEHPEGIN---DSFFERELPGLVPGVCVKNLVkifepsgrpaVDRLNITFYENQITAFLGHN 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 472 GSGKSSLIQAILGELPPESGSVQVSGK------------YSYASQEPWLF-NASVRDNILFGLPMDKQRYRTV-LKRCAL 537
Cdd:TIGR01257 966 GAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFhHLTVAEHILFYAQLKGRSWEEAqLEMEAM 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 538 ERDLELLHGDgtivGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQlVILVTHQl 617
Cdd:TIGR01257 1046 LEDTGLHHKR----NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT-IIMSTHH- 1119
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 618 qfLEDADL----IVIMDKGHVSACGTyEEMLKS--GQDFAQLLV---ESTQNSGGGDEIITS 670
Cdd:TIGR01257 1120 --MDEADLlgdrIAIISQGRLYCSGT-PLFLKNcfGTGFYLTLVrkmKNIQSQRGGCEGTCS 1178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
452-656 |
1.48e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVsGKYS---------------------YASQEPWLFN 510
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlkkikevkrlrkeiglvFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFG---LPMDKQR-YRTV---LKRCALERDLellhgdgtiVGERGASLSGGQRARICLARAVYRRADVYLLDD 583
Cdd:PRK13645 106 ETIEKDIAFGpvnLGENKQEaYKKVpelLKLVQLPEDY---------VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 584 PLSAVDTHVGR---HLFDECMRGFlgKQLVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLLVE 656
Cdd:PRK13645 177 PTGGLDPKGEEdfiNLFERLNKEY--KKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
454-628 |
1.53e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 454 NVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK------YSYASQEPWLFNA-------SVRDNILFG 520
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLGHQpgiktelTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 521 LPMdKQRYRTVLKRCALERdlellhgdgtiVGERG------ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH--- 591
Cdd:PRK13538 99 QRL-HGPGDDEALWEALAQ-----------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgva 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 28574259 592 -VGRHLFDECMRGflGkqLVILVTHQLQFLEDADLIVI 628
Cdd:PRK13538 167 rLEALLAQHAEQG--G--MVILTTHQDLPVASDKVRKL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1052-1274 |
1.55e-12 |
|
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: 71.64 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-----SYNDGAILIDSLDTNDIGLHDLR-- 1124
Cdd:COG4172 10 EDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSGSILFDGQDLLGLSERELRri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 --SKISIIPQEPvlfsgtMRyNLDPF----EQ----------YPDDKLWK----ALEDVHLKEE---ISELP---SGlqs 1178
Cdd:COG4172 90 rgNRIAMIFQEP------MT-SLNPLhtigKQiaevlrlhrgLSGAAARAraleLLERVGIPDPerrLDAYPhqlSG--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1179 iiseggtnfsvGQRQLVCLARAILRENRILVMDEatanvdPQT--DALIQATIRNKFKDCT------VLTIAHRLNTIMD 1250
Cdd:COG4172 160 -----------GQRQRVMIAMALANEPDLLIADE------PTTalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRR 222
|
250 260
....*....|....*....|....*
gi 28574259 1251 -SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1049-1266 |
1.61e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 68.05 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIGLHDlrS 1125
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTlrmIAGLEEPT--SGRIYIGGRDVTDLPPKD--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFS-----GTMRYNLDpFEQYPDDKLWKALEDV----HLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1196
Cdd:cd03301 73 DIAMVFQNYALYPhmtvyDNIAFGLK-LRKVPKDEIDERVREVaellQIEHLLDRKPKQL-----------SGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1197 LARAILRENRILVMDEATANVdpqtDALIQATIRNKFK------DCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlqqrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1067-1271 |
1.85e-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: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILidsldtndiglHDLRskISIIPQEPVLFSGTMRYNL 1145
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIK-----------HSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 DPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALI 1225
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1226 qatirnkFKDC--------TVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1271
Cdd:cd03291 199 -------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
447-642 |
2.04e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 447 QHDLvlnNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF 509
Cdd:PRK11144 12 DLCL---TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppekrRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 -NASVRDNILFGL-PMDKQRYRTVLKRCALERDLELLhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSA 587
Cdd:PRK11144 89 pHYKVRGNLRYGMaKSMVAQFDKIVALLGIEPLLDRY----------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 588 VDTHVGRHLFDECMRgfLGKQL---VILVTHQLQ-FLEDADLIVIMDKGHVSACGTYEE 642
Cdd:PRK11144 159 LDLPRKRELLPYLER--LAREInipILYVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-385 |
2.11e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 69.50 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 93 LIMSGITIAALELGtratVPLLLAGLISEFSEHGNGHSYNaqIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSA 172
Cdd:cd07346 4 ALLLLLLATALGLA----LPLLTKLLIDDVIPAGDLSLLL--WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 173 IYRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHFHFLWLGPLELLIASYFLyeqigMAS------FYGISILVLY 246
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVI-----LFYlnwkltLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 247 LPLQTYLSRVTSKLRLQTALRTDQRVRMMNEIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRQMNLLrGILLSF 322
Cdd:cd07346 153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALF-SPLIGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 323 EITLGRIAIFVsLLGFVLGGGELTAERAFCVTAFYNILRRTVsKFFPSGMSQFAELLVSMRRI 385
Cdd:cd07346 232 LTALGTALVLL-YGGYLVLQGSLTIGELVAFLAYLGMLFGPI-QRLANLYNQLQQALASLERI 292
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
444-653 |
2.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.58 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 444 GQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW---------------- 507
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 LFNASVRDNILFG---LPMDKQRYRTVLKRCaLERdlellhgdgtiVG----ERGAS--LSGGQRARICLARAVYRRADV 578
Cdd:PRK13633 98 IVATIVEEDVAFGpenLGIPPEEIRERVDES-LKK-----------VGmyeyRRHAPhlLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 579 YLLDDPLSAVDTHVGRHLFDECMRgfLGKQ---LVILVTHQLQFLEDADLIVIMDKGHVSACGT-------YEEMLKSGQ 648
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKE--LNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeifkeVEMMKKIGL 243
|
....*
gi 28574259 649 DFAQL 653
Cdd:PRK13633 244 DVPQV 248
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1067-1278 |
3.31e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSGTMRY- 1143
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRLSVYd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLDPFEQYPDDKLWKALED--VHLKEE--ISELPSGLqsiisegGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1219
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDraNELMEEfhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1220 QTDALIQATIRNkFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAK 1278
Cdd:PRK10895 171 ISVIDIKRIIEH-LRDsgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1067-1274 |
3.35e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDslDTNDIGL-----HDLrsKISIIPQEPVLFSG- 1139
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIG--GNPCARLtpakaHQL--GIYLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 TMRYNLD---PFEQYPDDKLwkaledvhlKEEISELPSGLQSIISEGGTNfsVGQRQLVCLARAILRENRILVMDEATAN 1216
Cdd:PRK15439 102 SVKENILfglPKRQASMQKM---------KQLLAALGCQLDLDSSAGSLE--VADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1217 VDP-QTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK15439 171 LTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1049-1267 |
3.51e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYE-PDTNSPCVlKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL-------IDSLDTNDIGL 1120
Cdd:PRK09473 13 LDVKDLRVTFStPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatfngREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1121 HDLRS-KISIIPQEPVLfsgtmryNLDPFEQYPDdklwKALEDVHLKEEISELPSGLQSI-------ISEGGT------- 1185
Cdd:PRK09473 92 NKLRAeQISMIFQDPMT-------SLNPYMRVGE----QLMEVLMLHKGMSKAEAFEESVrmldavkMPEARKrmkmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1186 NFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQaTIRNKFKD---CTVLTIAHRLNTIMDS-DKVLVMDAGH 1261
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM-TLLNELKRefnTAIIMITHDLGVVAGIcDKVLVMYAGR 239
|
....*.
gi 28574259 1262 VVEFGS 1267
Cdd:PRK09473 240 TMEYGN 245
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
451-668 |
3.92e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--YSYASQEpwL-------------FN----A 511
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdlTALSERE--LraarrkigmifqhFNllssR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 SVRDNILF-----GLPMDKQRyrtvlkrcalERDLELLHgdgtIVG--ERGAS----LSGGQRARICLARAVYRRADVYL 580
Cdd:COG1135 98 TVAENVALpleiaGVPKAEIR----------KRVAELLE----LVGlsDKADAypsqLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 581 LDDPLSAVDTHVGR---HLFDEcmrgfLGKQL---VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEM-LKSGQDFAQ 652
Cdd:COG1135 164 CDEATSALDPETTRsilDLLKD-----INRELgltIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVfANPQSELTR 238
|
250
....*....|....*.
gi 28574259 653 LLVESTQNSGGGDEII 668
Cdd:COG1135 239 RFLPTVLNDELPEELL 254
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
431-638 |
4.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPW--- 507
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 ------------LFNASVRDNILFGlPMD--------KQRYRTVLKRCALE--RDLELLHgdgtivgergasLSGGQRAR 565
Cdd:PRK13647 80 kvglvfqdpddqVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWdfRDKPPYH------------LSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 566 ICLARAVYRRADVYLLDDPLSAVDTHVGRHLFdECMRGF--LGKQlVILVTHQLQF-LEDADLIVIMDKGHVSACG 638
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLhnQGKT-VIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
434-642 |
5.85e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKysyasqepwLFNASV 513
Cdd:COG4152 2 LELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---------PLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNIlfG-LP-----------------------MDKQRYRTVLKRcALERdLELlhgdgtivGERGA----SLSGGQRAR 565
Cdd:COG4152 70 RRRI--GyLPeerglypkmkvgeqlvylarlkgLSKAEAKRRADE-WLER-LGL--------GDRANkkveELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 566 ICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRgflgkQL------VILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDP-VNVELLKDVIR-----ELaakgttVIFSSHQMELVEElCDRIVIINKGRKVLSG 211
|
....
gi 28574259 639 TYEE 642
Cdd:COG4152 212 SVDE 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1273 |
6.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSynDGAILIDSLDTNDIGLHDLRSKIS 1128
Cdd:PRK13647 8 EDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLPQ--RGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEP--VLFSGT---------MRYNLDPFEQypDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCL 1197
Cdd:PRK13647 83 LVFQDPddQVFSSTvwddvafgpVNMGLDKDEV--ERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1198 ARAILRENRILVMDEATANVDPQTDALIQaTIRNKF--KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPyELLT 1273
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLT 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
432-641 |
7.17e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEPWLF 509
Cdd:PRK09544 3 SLVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 NAsvrdnilfgLPMDKQRY---RTVLKRCALERDLELLHGdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK09544 80 TT---------LPLTVNRFlrlRPGTKKEDILPALKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 587 AVDTHVGRHLFD--ECMRGFLGKQlVILVTHQLQFLEDADLIVIMDKGHVSACGTYE 641
Cdd:PRK09544 150 GVDVNGQVALYDliDQLRRELDCA-VLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1067-1264 |
7.31e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL------IDSLDTND---------------IGLHDLRS 1125
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgepLAKLNRAQrkafrrdiqmvfqdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPvlfsgtMRY--NLDPFEQypDDKLWKALEDVHLKEEI-SELPSGLqsiiseggtnfSVGQRQLVCLARAIL 1202
Cdd:PRK10419 107 TVREIIREP------LRHllSLDKAER--LARASEMLRAVDLDDSVlDKRPPQL-----------SGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1203 RENRILVMDEATANVDP--QTDALIQ-ATIRNKFkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLvlQAGVIRLlKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
434-639 |
9.47e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------- 498
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdiamv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 -YSYAsqepwLF-NASVRDNILFGLP---MDKQRYRTVLKRCAleRDLELlhgdGTIVGERGASLSGGQRARICLARAVY 573
Cdd:PRK11650 82 fQNYA-----LYpHMSVRENMAYGLKirgMPKAEIEERVAEAA--RILEL----EPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 574 RRADVYLLDDPLSAVDTHVGRHLFDECMRgfLGKQL---VILVTH-QLQFLEDADLIVIMDKGHVSACGT 639
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQR--LHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1051-1273 |
9.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1051 TKDLSLRYEPDTNspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalFR-----LSYNDGAILIDSLDTNDIGLHDLRS 1125
Cdd:PRK13652 6 TRDLCYSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTL----FRhfngiLKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEP--VLFSGTMRY-------NLDPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1196
Cdd:PRK13652 79 FVGLVFQNPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1197 LARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1052-1271 |
1.13e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.82 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FrLSYNDGAILIDSLDTNDIGLHDlRsKISI 1129
Cdd:COG3842 9 ENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF-ETPDSGRILLDGRDVTGLPPEK-R-NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1130 IPQEPVLFSgtmryNLDPFE--QYP-----------DDKLWKALEDVHLKE----EISELpSGlqsiiseggtnfsvGQR 1192
Cdd:COG3842 82 VFQDYALFP-----HLTVAEnvAFGlrmrgvpkaeiRARVAELLELVGLEGladrYPHQL-SG--------------GQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1193 QLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfkdctvltIAHRLN--TIM---D-------SDKVLVMDAG 1260
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR---------LQRELGitFIYvthDqeealalADRIAVMNDG 212
|
250
....*....|.
gi 28574259 1261 HVVEFGSPYEL 1271
Cdd:COG3842 213 RIEQVGTPEEI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1067-1271 |
1.19e-11 |
|
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: 66.11 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdlRSKISIIPQEPVLFSgtmryNL 1145
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTsGEILLDGKDITNLPPH--KRPVNTVFQNYALFP-----HL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 DPFEQ--YP-----------DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDE 1212
Cdd:cd03300 88 TVFENiaFGlrlkklpkaeiKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1213 ATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1067-1274 |
1.27e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVL-FSGT---- 1140
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1141 --M-RYNLDPFEQYPDDKLWKALEDV---HLKE-EISELpSGlqsiiseggtnfsvGQRQLVCLARAILR------ENRI 1207
Cdd:PRK13548 97 vaMgRAPHGLSRAEDDALVAAALAQVdlaHLAGrDYPQL-SG--------------GEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLN-TIMDSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
431-623 |
1.31e-11 |
|
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: 68.81 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGqeqHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQ---- 504
Cdd:TIGR03719 320 DKVIEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQsrda 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 505 -EPwlfNASVRDNILFGLPMDKQRYRTVLKRCALERdlelLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDD 583
Cdd:TIGR03719 397 lDP---NKTVWEEISGGLDIIKLGKREIPSRAYVGR----FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 28574259 584 PLSAVDTHVGRHLfDECMRGFLGKQLVI---------LVTHQLQFLEDA 623
Cdd:TIGR03719 470 PTNDLDVETLRAL-EEALLNFAGCAVVIshdrwfldrIATHILAFEGDS 517
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1067-1274 |
1.31e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.14 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQ----EPVLfsgTMR 1142
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQfdnlDPDF---TVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1222
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1223 ALIQATIRNKF-KDCTVLTIAH------RLntimdSDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK13537 175 HLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1062-1257 |
1.37e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1062 TNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGT 1140
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1141 MRYNLD-PFE---QYPD-DKLWKALEDVHLKEEIselpsgLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:PRK10247 97 VYDNLIfPWQirnQQPDpAIFLDDLERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28574259 1216 NVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVM 1257
Cdd:PRK10247 167 ALDESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1067-1277 |
1.46e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDsldtnDIGLHDL--------RSKISIIPQEPvlfS 1138
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFD-----GQPLHNLnrrqllpvRHRIQVVFQDP---N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 GTMRYNLDPFE--------QYP-------DDKLWKALEDVHLKeeiselPSGLQSIISEggtnFSVGQRQLVCLARAILR 1203
Cdd:PRK15134 373 SSLNPRLNVLQiieeglrvHQPtlsaaqrEQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1204 ENRILVMDEATANVDPQTDALIQATIRNkfkdctvLTIAHRLNTIMDS----------DKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKS-------LQQKHQLAYLFIShdlhvvralcHQVIVLRQGEVVEQGDCERVFA 515
|
....
gi 28574259 1274 ASKA 1277
Cdd:PRK15134 516 APQQ 519
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1067-1230 |
1.69e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.69 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNdiglhdlrsKISIIPQEPVLFSG------ 1139
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWNGTPLA---------EQRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 ---TMRYNLD---PFEQYPDDKLWKALEDVHLKEeISELPSGlqsiiseggtNFSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*..
gi 28574259 1214 TANVDPQTDALIQATIR 1230
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1049-1264 |
1.69e-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: 65.53 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLinalfrLSyndgaiLIDSLDTNDIG--------L 1120
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTL------LG------LLAGLDRPTSGtvrlagqdL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1121 HDL---------RSKISIIPQ-EPVLFSGTMRYNL----------DPFEQYPDdklwkALEDVHLKEEISELPSGLqsii 1180
Cdd:COG4181 77 FALdedararlrARHVGFVFQsFQLLPTLTALENVmlplelagrrDARARARA-----LLERVGLGHRLDHYPAQL---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1181 seggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMDSDKVLVMD 1258
Cdd:COG4181 148 -------SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLR 220
|
....*.
gi 28574259 1259 AGHVVE 1264
Cdd:COG4181 221 AGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
431-653 |
1.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG------------- 497
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 498 KYSYASQEP--WLFNASVRDNILFGLPMDKQRYRTVLKRCalerDLELLHGDGTIVGERG-ASLSGGQRARICLARAVYR 574
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREpARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 575 RADVYLLDDPLSAVDThVGRHLFDECMRGFLGK-QLVIL-VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQ 652
Cdd:PRK13642 158 RPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
.
gi 28574259 653 L 653
Cdd:PRK13642 237 I 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1049-1266 |
1.86e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 64.99 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILID--SLDTNDiglhdlRS 1125
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDsGEVLFDgkPLDIAA------RN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 KISIIPQEPVLFSGT-----MRY-----NLDPFEQYPDDKLWkaLEDVHL----KEEISELpsglqsiiseggtnfSVGQ 1191
Cdd:cd03269 71 RIGYLPEERGLYPKMkvidqLVYlaqlkGLKKEEARRRIDEW--LERLELseyaNKRVEEL---------------SKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
439-648 |
2.00e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 439 LRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEP------------ 506
Cdd:PRK10619 11 LHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 ----------------WLFnASVRDNIL------FGLPMDKQRYRTVlkrcaleRDLELLHGDGTIVGERGASLSGGQRA 564
Cdd:PRK10619 88 rllrtrltmvfqhfnlWSH-MTVLENVMeapiqvLGLSKQEARERAV-------KYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 565 RICLARAVYRRADVYLLDDPLSAVDThvgrHLFDECMRGFL-----GKQLVIlVTHQLQFLEDADLIVI-MDKGHVSACG 638
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQqlaeeGKTMVV-VTHEMGFARHVSSHVIfLHQGKIEEEG 234
|
250
....*....|
gi 28574259 639 TYEEMLKSGQ 648
Cdd:PRK10619 235 APEQLFGNPQ 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
431-657 |
2.00e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKAL------RARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS------GK 498
Cdd:PRK15112 2 ETLLEVRNLsktfryRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 499 YSYAS-------QEP-----------WLFNASVRDNILFGLPMDKQRYRTVLKRCALERDlellHgdgtiVGERGASLSG 560
Cdd:PRK15112 82 YSYRSqrirmifQDPstslnprqrisQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD----H-----ASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 561 GQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDeCMRGFLGKQLV--ILVTHQLQFLED-ADLIVIMDKGHVSAC 637
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN-LMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 28574259 638 GTYEEMLKSGQ-DFAQLLVES 657
Cdd:PRK15112 232 GSTADVLASPLhELTKRLIAG 252
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
770-971 |
2.02e-11 |
|
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: 66.42 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 770 DIYYFTAINVGLVICALLRTLLFFnITMHSSTELHNTMFQGLsRTALY---------FFHTNPSGRILNRFANDLGQVDE 840
Cdd:cd07346 34 DLSLLLWIALLLLLLALLRALLSY-LRRYLAARLGQRVVFDL-RRDLFrhlqrlslsFFDRNRTGDLMSRLTSDVDAVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 841 VMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMM----LAFYYWRDFYLKTSRDVKrlEAVARspMYSHFSATLVG 916
Cdd:cd07346 112 LVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLplyvLILRYFRRRIRKASREVR--ESLAE--LSAFLQESLSG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 917 LPTIRAMGAQQTLIGQYDNYQDLHSSGYYTFVSTSRAFGYYLDLFCVAYVISVIL 971
Cdd:cd07346 188 IRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
447-616 |
2.15e-11 |
|
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: 63.71 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 447 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ--VSGKYSYASQEPWLFNASVRDNILFglPMD 524
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGmpEGEDLLFLPQRPYLPLGTLREQLIY--PWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 525 KQryrtvlkrcalerdlellhgdgtivgergasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECmrgf 604
Cdd:cd03223 90 DV-------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---- 134
|
170
....*....|....*
gi 28574259 605 lgKQL---VILVTHQ 616
Cdd:cd03223 135 --KELgitVISVGHR 147
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1067-1260 |
3.55e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.38 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRlSY--NDGAILIDSLDT-------NDIGLHDLRSK--------ISI 1129
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYlpDSGSILVRHDGGwvdlaqaSPREILALRRRtigyvsqfLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1130 IPQ--------EPVLFSGTMRynldpfeqypDDKLWKA---LEDVHLKEEISELPSglqsiiseggTNFSVGQRQLVCLA 1198
Cdd:COG4778 105 IPRvsaldvvaEPLLERGVDR----------EEARARArelLARLNLPERLWDLPP----------ATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTiMD--SDKVLVMDAG 1260
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEaKARGTAIIGIFHDEEV-REavADRVVDVTPF 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
461-631 |
4.51e-11 |
|
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: 62.39 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 461 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVqvsgkysyasqepwlfnasvrdnilfglpmdkqryrtVLKRCALERD 540
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------IYIDGEDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 541 LELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL------VILVT 614
Cdd:smart00382 44 EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKseknltVILTT 123
|
170
....*....|....*..
gi 28574259 615 HQLQFLEDADLIVIMDK 631
Cdd:smart00382 124 NDEKDLGPALLRRRFDR 140
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-649 |
4.89e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA------------------- 511
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 -SVRDNILFGLP----MDKQRYRTVLKRCAleRDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK14246 105 lSIYDNIAYPLKshgiKEKREIKKIVEECL--RKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 587 AVDThVGRHLFDECMRGFLGKQLVILVTHQ-LQFLEDADLIVIMDKGHVSACGTYEEMLKSGQD 649
Cdd:PRK14246 183 MIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1051-1272 |
5.21e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1051 TKDLSLRY-EPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSYNDGAILI--DSLDTNDIGLhDLR 1124
Cdd:TIGR03269 282 VRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLskiIAGVLEPTSGEVNVRVgdEWVDMTKPGP-DGR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 SK----ISIIPQEPVLFsgTMRYNLDPFE-----QYPDD----KLWKALEDVHLKEEISElpsglqSIISEGGTNFSVGQ 1191
Cdd:TIGR03269 361 GRakryIGILHQEYDLY--PHRTVLDNLTeaiglELPDElarmKAVITLKMVGFDEEKAE------EILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDC--TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1268
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
....
gi 28574259 1269 YELL 1272
Cdd:TIGR03269 513 EEIV 516
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
451-646 |
5.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.73 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAiLGELPPE------SGSVQVSGK--YSYAS------------QEPWLFN 510
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKvsgyrySGDVLLGGRsiFNYRDvlefrrrvgmlfQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 511 ASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTI--VGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAV 588
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 589 DTHVGRHLfDECMRGFLGKQLVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:PRK14271 195 DPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
452-635 |
6.17e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYASQEPW--LFNASVRDNILF-------GL 521
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYrkLFSAVFTDFHLFdqllgpeGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 522 PMDKQRYRTVLKRCALERDLELlhGDGTIVGERgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDEC- 600
Cdd:PRK10522 419 PANPALVEKWLERLKMAHKLEL--EDGRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLl 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 28574259 601 --MRGfLGKQlVILVTHQLQFLEDADLIVIMDKGHVS 635
Cdd:PRK10522 494 plLQE-MGKT-IFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
452-656 |
6.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQ-------------------EPWLFNAS 512
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirkkvglvfqfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGlPMDKQRYRTVLKRCALERdLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 592
Cdd:PRK13649 103 VLKDVAFG-PQNFGVSQEEAEALAREK-LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 593 GRHlfdECMRGFlgKQL------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYE------EMLKSGQ-------DFAQ 652
Cdd:PRK13649 180 GRK---ELMTLF--KKLhqsgmtIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKdifqdvDFLEEKQlgvpkitKFAQ 254
|
....
gi 28574259 653 LLVE 656
Cdd:PRK13649 255 RLAD 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1051-1270 |
6.50e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1051 TKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSldtndiglhDLRskISI 1129
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIPK---------GLR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1130 IPQEPVLFSGT---------------MRYNLDPFEQYPDDKLWKALEDVHLKEEISEL-----PSGLQSIISEGG----- 1184
Cdd:COG0488 66 LPQEPPLDDDLtvldtvldgdaelraLEAELEELEAKLAEPDEDLERLAELQEEFEALggweaEARAEEILSGLGfpeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1185 -----TNFSVGQRQLVCLARAILRENRILVMDEATANVDpqtdalIQATIR-----NKFKdCTVLTIAH-R--LNTImdS 1251
Cdd:COG0488 146 ldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEWleeflKNYP-GTVLVVSHdRyfLDRV--A 216
|
250
....*....|....*....
gi 28574259 1252 DKVLVMDAGHVVEFGSPYE 1270
Cdd:COG0488 217 TRILELDRGKLTLYPGNYS 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1067-1274 |
6.80e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVL---FSGTM- 1141
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 --------RYNLDPFEQYPDDKLWKALEDVhlkeeiselpsGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:PRK09536 98 vemgrtphRSRFDTWTETDRAAVERAMERT-----------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1214 TANVD----PQTDALIQATIRNkfkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK09536 167 TASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1071-1263 |
7.13e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 63.28 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIQPMEKVGIVGRTGAGKSSLIN--ALFRLSyNDGAILIDSLDTNdiGLHDLRSKISIIPQEPVLFSG-TMRYN--- 1144
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNliAGFETP-QSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNvgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 -------LDPFEQypdDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANV 1217
Cdd:cd03298 94 glspglkLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 28574259 1218 DPQTDALIQA---TIRNKFKDcTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:cd03298 160 DPALRAEMLDlvlDLHAETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1063-1276 |
7.29e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1063 NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS--YN-----DGAILIDSLDTNDIGLHDLRSKISIIPQEPV 1135
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiYDskikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1136 LFS-----GTMRYNLDPFEQYPDDKLWKALEDVHLKEEI-SELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILV 1209
Cdd:PRK14246 101 PFPhlsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1210 MDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
451-648 |
7.51e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YSYASQEPWLFNA-SVRD 515
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFGLPMDKQRYRTVLKRCALE--RDLELLHGDGTIvgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD---- 589
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANElmEEFHIEHLRDSM----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisv 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 590 ---THVGRHLFDECmrgfLGkqlVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQ 648
Cdd:PRK10895 174 idiKRIIEHLRDSG----LG---VLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
433-657 |
7.73e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQHdlvLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS-----YASQEP- 506
Cdd:PRK11701 6 LLSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGqlrdlYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 --------WLFnasVRDNILFGLPMD--------------KQRYRTVLKRCALE--RDLELlhgDGTIVGERGASLSGGQ 562
Cdd:PRK11701 83 rrrllrteWGF---VHQHPRDGLRMQvsaggnigerlmavGARHYGDIRATAGDwlERVEI---DAARIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 563 RARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDeCMRGfLGKQL---VILVTHQL---QFLedADLIVIMDKGHVSA 636
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD-LLRG-LVRELglaVVIVTHDLavaRLL--AHRLLVMKQGRVVE 232
|
250 260
....*....|....*....|..
gi 28574259 637 CGTYEEMLKSGQD-FAQLLVES 657
Cdd:PRK11701 233 SGLTDQVLDDPQHpYTQLLVSS 254
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1067-1272 |
8.00e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIdsLDTNDIGLHDL-RSKISIIPQEPVL-FSGTMRY 1143
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKITV--LGVPVPARARLaRARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLDPFEQYPDDKLWKALEDVHLKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDA 1223
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1224 LIQATIRNKF-KDCTVLTIAHrlntIMDS-----DKVLVMDAGHVVEFGSPYELL 1272
Cdd:PRK13536 210 LIWERLRSLLaRGKTILLTTH----FMEEaerlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1067-1273 |
8.90e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAILIDSLDTNDIglhdlRSKISIIPQEP-VLFSgtmR 1142
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEEIT--SGDLIVDGLKVNDP-----KVDERLIRQEAgMVFQ---Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNLdpFEQYpddklwKALEDVHL---------KEEISELPS------GLQSIISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:PRK09493 86 FYL--FPHL------TALENVMFgplrvrgasKEEAEKQARellakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1037-1270 |
9.03e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1037 KQPPKSwpkeGKLV--TKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL-FRLSYNDGAIlidsl 1113
Cdd:COG0488 306 PPPERL----GKKVleLEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPDSGTV----- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1114 dtnDIGlHDLrsKISIIPQEpvlfsgtmRYNLDpfeqyPDDKLWKALEDVHLKEEISEL----------PSGLQSIISeg 1183
Cdd:COG0488 373 ---KLG-ETV--KIGYFDQH--------QEELD-----PDKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPVG-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1184 gtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT-DALIQATirNKFKDcTVLTIAH-R--LNTImdSDKVLVMDA 1259
Cdd:COG0488 432 --VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlEALEEAL--DDFPG-TVLLVSHdRyfLDRV--ATRILEFED 504
|
250
....*....|.
gi 28574259 1260 GHVVEFGSPYE 1270
Cdd:COG0488 505 GGVREYPGGYD 515
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1271 |
9.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.27 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPdtNSPC---VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILIDSL----DTNDIGLH 1121
Cdd:PRK13634 6 QKVEHRYQY--KTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlNGL--LQPTSGTVTIGERvitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 DLRSKISIIPQ--EPVLFSGTMR-------YNLDPFEQYPDDKLWKALEDVHLKEEISEL-PSGLqsiiseggtnfSVGQ 1191
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLARsPFEL-----------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQTdaliQATIRNKF------KDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
....*..
gi 28574259 1265 FGSPYEL 1271
Cdd:PRK13634 227 QGTPREI 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1068-1271 |
9.68e-11 |
|
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: 63.51 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDlrSKISIIPQEPVLFSG-TMRYNL 1145
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDsGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1146 -----------DPFEQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEAT 1214
Cdd:cd03296 96 afglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1215 ANVDPQTDALIQATIRNKFKDCTVLTI--AHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1068-1272 |
1.28e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDT---NDIGLHDLRSK--------ISIIPQEPV 1135
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIakiSDAELREVRRKkiamvfqsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1136 LFSGTMRYNLD--PFEQYPDDKLwKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKAL-DALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1214 TANVDP-----QTDALIQATIRNKFkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1272
Cdd:PRK10070 192 FSALDPlirteMQDELVKLQAKHQR---TIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
403-587 |
1.30e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 403 RDEKAEEEQHLLKEVEKRsypvgigkepDTLVEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 482
Cdd:PRK13409 320 RPEPIEFEERPPRDESER----------ETLVEYPDLTKKLG----DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 483 LGELPPESGSVQVSGKYSYASQ--EPwLFNASVRDNilfgLPMDKQRYRT------VLKRCALERDLELLHGDgtivger 554
Cdd:PRK13409 386 AGVLKPDEGEVDPELKISYKPQyiKP-DYDGTVEDL----LRSITDDLGSsyykseIIKPLQLERLLDKNVKD------- 453
|
170 180 190
....*....|....*....|....*....|...
gi 28574259 555 gasLSGGQRARICLARAVYRRADVYLLDDPlSA 587
Cdd:PRK13409 454 ---LSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1067-1276 |
1.31e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND------GAILID---SLDTNDIGLHDLRSKISIIPQEpvlf 1137
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDtarSLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 sgtmrYNLDPFEQypddklwkALEDV---------HLKEEISELPSGLQSIISEGGTN------FSVGQRQLVCLARAIL 1202
Cdd:PRK11264 94 -----FNLFPHRT--------VLENIiegpvivkgEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1203 RENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1052-1261 |
1.32e-10 |
|
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: 60.54 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSldtndiglhdlRSKISII 1130
Cdd:cd03221 4 ENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1131 PQepvlFSGtmrynldpfeqypddklwkaledvhlkeeiselpsglqsiiseggtnfsvGQRQLVCLARAILRENRILVM 1210
Cdd:cd03221 69 EQ----LSG--------------------------------------------------GEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1211 DEATANVDPQT-DALIQATirNKFKdCTVLTIAH-R--LNTImdSDKVLVMDAGH 1261
Cdd:cd03221 95 DEPTNHLDLESiEALEEAL--KEYP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1067-1263 |
1.43e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 62.74 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlsynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFS--GTMRYN 1144
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 LDPFEQYPDDKLWKALEDVHLKEEISELPSGLQ--SIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1222
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28574259 1223 ALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:cd03267 190 ENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
411-589 |
1.88e-10 |
|
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: 65.09 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 411 QHLLkEVEKRSYPVGIGKEPDTLVEIKAL-------RARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 482
Cdd:COG4172 254 RKLL-AAEPRGDPRPVPPDAPPLLEARDLkvwfpikRGLFRRTVGHVKaVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 483 LGeLPPESGSVQVSGK----YS------------------YASQEPWLfnaSVRDNILFGL-----PMDK-QRYRTVLKr 534
Cdd:COG4172 333 LR-LIPSEGEIRFDGQdldgLSrralrplrrrmqvvfqdpFGSLSPRM---TVGQIIAEGLrvhgpGLSAaERRARVAE- 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 535 cALERdlellhgdgtiVGERGASL-------SGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:COG4172 408 -ALEE-----------VGLDPAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1072-1273 |
2.05e-10 |
|
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: 63.05 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1072 SFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIG---LHDLRSK-ISIIPQEPVLFSgtMRYNLD 1146
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLP--HRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1147 ----PFE------QYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATAN 1216
Cdd:cd03294 122 nvafGLEvqgvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1217 VDP------QTDAL-IQATIRNkfkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:cd03294 191 LDPlirremQDELLrLQAELQK-----TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1047-1273 |
2.33e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.10 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1047 GKLVTKDLSLRYEPDTnsPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLI---NALFrLSYNDGAILIDSLDTNDIG- 1119
Cdd:PRK13645 5 KDIILDNVSYTYAKKT--PFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIqltNGLI-ISETGQTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1120 ---LHDLRSKISIIPQEP--VLFSGTMRYNLdpfeQYPDDKLWKALEDVHLK-EEISELPSGLQSIISEGGTNFSVGQRQ 1193
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDI----AFGPVNLGENKQEAYKKvPELLKLVQLPEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1194 LVCLARAILRENRILVMDEATANVDPQTDA-LIQATIR-NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYE 1270
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
...
gi 28574259 1271 LLT 1273
Cdd:PRK13645 238 IFS 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
430-634 |
2.37e-10 |
|
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: 64.71 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEQHD-LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPesGSVQVSGKYSYASQEpwL 508
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPD--PAAHPSGSILFDGQD--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 509 FNAS------VRDN---ILFGLPM---------DKQ------RYRTVLKRCALERDLELLhgdgTIVG----ERGAS--- 557
Cdd:COG4172 79 LGLSerelrrIRGNriaMIFQEPMtslnplhtiGKQiaevlrLHRGLSGAAARARALELL----ERVGipdpERRLDayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 558 --LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFLED-ADLIV 627
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD------LLKDLqrelgmaLLLITHDLGVVRRfADRVA 228
|
....*..
gi 28574259 628 IMDKGHV 634
Cdd:COG4172 229 VMRQGEI 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
445-648 |
3.52e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 445 QEQHD--LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV-------------QVSGKYSYASQEP--W 507
Cdd:PRK13648 16 QYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGIVFQNPdnQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 LFNASVRDNILFGL-----PMDKQrYRTVLKrcALErDLELL-HGDgtivgERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:PRK13648 96 FVGSIVKYDVAFGLenhavPYDEM-HRRVSE--ALK-QVDMLeRAD-----YEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 582 DDPLSAVDTHVGRHLFDECMRGFLGKQLVIL-VTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQ 648
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1067-1266 |
3.68e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGA-------ILIDSLDTNDIGLHDLRSKISIIPQEPVLFS 1138
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELNEEArvegevrLFGRNIYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 GTMRYN-----------LDPFEQYPDDKLWkALEDVHLKEEISELpsglqsiISEGGTNFSVGQRQLVCLARAILRENRI 1207
Cdd:PRK14267 99 HLTIYDnvaigvklnglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1208 LVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHR-LNTIMDSDKVLVMDAGHVVEFG 1266
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1068-1267 |
3.73e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALF--------RLSYNDgailIDSLDTNDIGLHDLRSKISIIPQ------- 1132
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptggELYYQG----QDLLKADPEAQKLLRQKIQIVFQnpygsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1133 ----------EPVLfsgtMRYNLDPFEQypDDKLWKALEDVHLK-EEISELPSglqsiiseggtNFSVGQRQLVCLARAI 1201
Cdd:PRK11308 107 prkkvgqileEPLL----INTSLSAAER--REKALAMMAKVGLRpEHYDRYPH-----------MFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1202 LRENRILVMDEATANVDPQtdalIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGS 1267
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1049-1262 |
3.74e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDtndigLHDLRSKI 1127
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAP-----LAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 SIIPQEPVLFsgtmrynldPFEQYPD-----------DKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVC 1196
Cdd:PRK11247 84 RLMFQDARLL---------PWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1197 LARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLN-TIMDSDKVLVMDAGHV 1262
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
403-587 |
3.80e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 403 RDEKAEEEQHLLKEVEKRsypvgigkepDTLVEIKALRARWGqeqhDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI 482
Cdd:COG1245 321 RDEPIEFEVHAPRREKEE----------ETLVEYPDLTKSYG----GFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKIL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 483 LGELPPESGSVQVSGKYSYASQ--EPwLFNASVRDNI--LFGLPMDKQRYRT-VLKRCALERDLEllhgdgtivgERGAS 557
Cdd:COG1245 387 AGVLKPDEGEVDEDLKISYKPQyiSP-DYDGTVEEFLrsANTDDFGSSYYKTeIIKPLGLEKLLD----------KNVKD 455
|
170 180 190
....*....|....*....|....*....|
gi 28574259 558 LSGGQRARICLARAVYRRADVYLLDDPlSA 587
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
451-641 |
5.35e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSV------------------------------------- 493
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 494 ----QVSGKYSYAsqEPWLFNASVRDNILFG---LPMDKQRyrtvlkrcALERDLELLHgdgtIVG------ERGA-SLS 559
Cdd:PRK13651 102 eirrRVGVVFQFA--EYQLFEQTIEKDIIFGpvsMGVSKEE--------AKKRAAKYIE----LVGldesylQRSPfELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 560 GGQRARICLARAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgflGKQlVILVTHQL-QFLEDADLIVIMDK 631
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgvkeileIFDNLNKQ------GKT-IILVTHDLdNVLEWTKRTIFFKD 240
|
250
....*....|.
gi 28574259 632 GHVSACG-TYE 641
Cdd:PRK13651 241 GKIIKDGdTYD 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1083-1267 |
7.21e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1083 IVGRTGAGKSSLINALFRLSYND-GAILIdsldtNDIGLHDLRSKISIIP---------QEPVLF-----SGTMRYNLDP 1147
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQkGRIVL-----NGRVLFDAEKGICLPPekrrigyvfQDARLFphykvRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1148 FEQYPDDKLWKALEDVHLkeeISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVD-PQTDALIQ 1226
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28574259 1227 --ATIRNKFKdCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGS 1267
Cdd:PRK11144 170 ylERLAREIN-IPILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1068-1262 |
8.72e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILIDSLDTNDIGLHDL-RSKISIIPQEPVLF----- 1137
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgTY-EGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 ------------SGTMRYNldpfEQYPDDKLWkaLEDVHLkeEIS-ELPSGlqsiiseggtNFSVGQRQLVCLARAILRE 1204
Cdd:PRK13549 100 leniflgneitpGGIMDYD----AMYLRAQKL--LAQLKL--DINpATPVG----------NLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 1205 NRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVM-DAGHV 1262
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIrDGRHI 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1072-1273 |
9.37e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 62.04 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1072 SFTIQPMEKVGIVGRTGAGKSSLINAL----------FRLsynDGAILIDSldTNDIGL--HdlRSKISIIPQEPVLFSG 1139
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdsgrIRL---GGEVLQDS--ARGIFLppH--RRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 -TMRYNLdpfeQYPDDKLWKALEDVHLkEEISEL----------PSGLqsiiseggtnfSVGQRQLVCLARAILRENRIL 1208
Cdd:COG4148 92 lSVRGNL----LYGRKRAPRAERRISF-DEVVELlgighlldrrPATL-----------SGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1209 VMDEATANVDPQTDALIQ---ATIRNKFkDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLT 1273
Cdd:COG4148 156 LMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
458-589 |
9.42e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 458 SLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-KYSYASQ--EPwLFNASVRDnILFGLPMDK---QRYRT- 530
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQyiKA-DYEGTVRD-LLSSITKDFythPYFKTe 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 531 VLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:cd03237 99 IAKPLQIEQILD----------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
451-645 |
1.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGS---VQVSG-------------KYSYASQEP--WLFNAS 512
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGitltaktvwdireKVGIVFQNPdnQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGLPmDKQRYRTVLKRcaLERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHv 592
Cdd:PRK13640 102 VGDDVAFGLE-NRAVPRPEMIK--IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 593 GRHLFDECMRGFLGKQ--LVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK13640 178 GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
415-584 |
1.23e-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: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 415 KEVEKRsYPVGIGKEPDTLVEIKALRARwgqeqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQ 494
Cdd:COG1129 239 RELEDL-FPKRAAAPGEVVLEVEGLSVG-------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 495 VSGK-YSYASqePW------------------LF-NASVRDNILFGLpMDKQRYRTVLKRcALERDL-----ELLH---- 545
Cdd:COG1129 311 LDGKpVRIRS--PRdairagiayvpedrkgegLVlDLSIRENITLAS-LDRLSRGGLLDR-RRERALaeeyiKRLRiktp 386
|
170 180 190
....*....|....*....|....*....|....*....
gi 28574259 546 GDGTIVGergaSLSGGQRARICLARAVYRRADVYLLDDP 584
Cdd:COG1129 387 SPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
450-677 |
1.24e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-----------------KYSYASQEPWLF-NA 511
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMpHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 SVRDNILFGL-----PMDKQRYRTV--LKRCALErdlELLHGdgtivgeRGASLSGGQRARICLARAVYRRADVYLLDDP 584
Cdd:PRK10070 122 TVLDNTAFGMelagiNAEERREKALdaLRQVGLE---NYAHS-------YPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 585 LSAVDTHVGRHLFDECMRGFLGKQ-LVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKS-GQDFAQLLVESTQNS 661
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpANDYVRTFFRGVDIS 271
|
250
....*....|....*.
gi 28574259 662 gggdEIITSPNLSRQS 677
Cdd:PRK10070 272 ----QVFSAKDIARRT 283
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
451-633 |
1.32e-09 |
|
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: 62.26 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLI-------QAILGELPPESGSvqvsgKYSYASQEPWL-FNASVRDNILFGLP 522
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 523 MDKQ---RYRTVLKRCA---------------------------LERDLE-------LLHGDGTIvgergASLSGGQRAR 565
Cdd:TIGR03719 95 EIKDaldRFNEISAKYAepdadfdklaaeqaelqeiidaadawdLDSQLEiamdalrCPPWDADV-----TKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 566 ICLARAVYRRADVYLLDDPLSAVDTH----VGRHLfdecmRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGH 633
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHL-----QEYPGT--VVAVTHDRYFLDNvAGWILELDRGR 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1067-1266 |
1.71e-09 |
|
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: 59.47 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdlrskISIIPQ----EPVLFSGTM 1141
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGRVSSLLGLG-----GGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 rYNLDPfeQYPDDKLwkaledvhlkEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1221
Cdd:cd03220 112 -LGLSR--KEIDEKI----------DEIIEF-SELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28574259 1222 DALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1067-1276 |
1.71e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLS-------YNDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLF-- 1137
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 -------SGTMRYNLDPFEQYpddklwKALEDVHLKEeiSELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVM 1210
Cdd:PRK14271 116 simdnvlAGVRAHKLVPRKEF------RGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1211 DEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL-NTIMDSDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
431-618 |
1.80e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWlf 509
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 NASVR-DNILFGLpmdkQRYRTVLKRCALE------------------RDLELLHGDGtiVGER----GASLSGGQRARI 566
Cdd:PRK10584 82 RAKLRaKHVGFVF----QSFMLIPTLNALEnvelpallrgessrqsrnGAKALLEQLG--LGKRldhlPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 567 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFD---ECMRGFlgKQLVILVTHQLQ 618
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQ 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1068-1276 |
2.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALFRLSYndGAILIDSLD----TNDIGLHDLRSKISIIPQEP------ 1134
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIqniNALLKPTT--GTVTVDDITithkTKDKYIRPVRKRIGMVFQFPesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1135 ------VLFsGTMRYNLDpFEQYPDDKlWKALEDVHLKEEISELpSGLQsiiseggtnFSVGQRQLVCLARAILRENRIL 1208
Cdd:PRK13646 101 dtvereIIF-GPKNFKMN-LDEVKNYA-HRLLMDLGFSRDVMSQ-SPFQ---------MSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1209 VMDEATANVDPQTDALIQATIR------NKfkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKslqtdeNK----TIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1048-1276 |
2.12e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLI---NALfrLSYNDGAILI------------- 1110
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNAL--LLPDTGTIEWifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1111 --DSLDTNDIG---------LHDLRSKISIIPQ--EPVLFS---------GTMRYNLDPFEQYPDDKlwKALEDVHLKEE 1168
Cdd:PRK13651 80 keKVLEKLVIQktrfkkikkIKEIRRRVGVVFQfaEYQLFEqtiekdiifGPVSMGVSKEEAKKRAA--KYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1169 -ISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLN 1246
Cdd:PRK13651 158 yLQRSPFEL-----------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLD 226
|
250 260 270
....*....|....*....|....*....|.
gi 28574259 1247 TIMD-SDKVLVMDAGHVVEFGSPYELLTASK 1276
Cdd:PRK13651 227 NVLEwTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
434-634 |
2.20e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWL---- 508
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 509 ---------FN--AS--VRDNILFGLPMDKQRYRTVLKRCAlerdlELLhgdgTIVG--ERG----ASLSGGQRARICLA 569
Cdd:PRK11153 82 rqigmifqhFNllSSrtVFDNVALPLELAGTPKAEIKARVT-----ELL----ELVGlsDKAdrypAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 570 RAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQL-------VILVTHQLQFL-EDADLIVIMDKGHV 634
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILE------LLKDInrelgltIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
447-589 |
2.52e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 447 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG----KYSYASQEPWLF---------NASV 513
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQKQLCFvghrsginpYLTL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 514 RDNILFglpmDKQRYRTVLKRCALERDLELLHgdgtIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:PRK13540 92 RENCLY----DIHFSPGAVGITELCRLFSLEH----LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
434-639 |
2.68e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAI-LGELPpESGSVQVSGKYSYASQEP------ 506
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLNIAGNHFDFSKTPsdkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 ---------------WLfNASVRDNiLFGLPMdkqRYRTVLKRCALERDLELLHgdgTIVGERGAS-----LSGGQRARI 566
Cdd:PRK11124 79 elrrnvgmvfqqynlWP-HLTVQQN-LIEAPC---RVLGLSKDQALARAEKLLE---RLRLKPYADrfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 567 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecmrgfLGKQLV------ILVTHQLQFLED-ADLIVIMDKGHVSACGT 639
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVS------IIRELAetgitqVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1049-1274 |
2.84e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAIL--------------IDSLD 1114
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1115 TNDIGLHDLR-SKISIIPQEPVLfsgtmryNLDPF----EQYP-----------DDKLWKA---LEDVHLKEEiselpsg 1175
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMT-------SLNPVftvgEQIAesirlhqgasrEEAMVEAkrmLDQVRIPEA------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1176 lQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCT--VLTIAHRLNTIMD-SD 1252
Cdd:PRK10261 159 -QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiAD 237
|
250 260
....*....|....*....|..
gi 28574259 1253 KVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHA 259
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
452-645 |
3.14e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGK----------YSYASQEPWLFNA-SVRDNI 517
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFG--LPMDKQRYRTVlKRCALE---RDLELLHGDGTIVGERGA--SLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:TIGR00955 121 MFQahLRMPRRVTKKE-KRERVDevlQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 591 ----HVGRHLFDECMRGflgkQLVILVTHQ--LQFLEDADLIVIMDKGHVSACGTYEEMLK 645
Cdd:TIGR00955 200 fmaySVVQVLKGLAQKG----KTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
452-636 |
4.84e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QEPWLFNA-SVRDN 516
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIRSprdaialgigmvhQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 ILFGLP------MDKQRYRTVLKRCA----LERDLEllhgdgTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPlS 586
Cdd:COG3845 101 IVLGLEptkggrLDRKAARARIRELSerygLDVDPD------AKVED----LSVGEQQRVEILKALYRGARILILDEP-T 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 587 AVDT--HVgRHLFDEcMRGFLGKQL-VILVTHQLQ-FLEDADLIVIMDKGHVSA 636
Cdd:COG3845 170 AVLTpqEA-DELFEI-LRRLAAEGKsIIFITHKLReVMAIADRVTVLRRGKVVG 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
390-619 |
5.12e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 390 MREEanvidMSERRD---------EKAEEEQHLLKEVEKRSYPVGiGKepdTLVeikalrarwgqeqhdlvlNNVNMSLR 460
Cdd:PRK11147 291 LRRE-----RSERREvmgtakmqvEEASRSGKIVFEMENVNYQID-GK---QLV------------------KDFSAQVQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 461 RGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQ-----EPwlfNASVRDNILFGlpmdKQ------R 527
Cdd:PRK11147 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevAYFDQhraelDP---EKTVMDNLAEG----KQevmvngR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 528 YRTVL----------KRCAlerdlellhgdgTIVgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVgRHLF 597
Cdd:PRK11147 417 PRHVLgylqdflfhpKRAM------------TPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET-LELL 479
|
250 260
....*....|....*....|..
gi 28574259 598 DECMRGFLGKqlVILVTHQLQF 619
Cdd:PRK11147 480 EELLDSYQGT--VLLVSHDRQF 499
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
458-633 |
6.64e-09 |
|
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: 56.21 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 458 SLRRGQLVAVIGPVGSGKSSLIQAILgelppesgsvqvsgkysyasqepwlfnasvrdnILFGLPMDKQRYRTVLKRCAL 537
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVKAGCI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 538 ERDLELlhgdgTIVGERGaSLSGGQRARICLARAV----YRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILV 613
Cdd:cd03227 64 VAAVSA-----ELIFTRL-QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI 137
|
170 180
....*....|....*....|
gi 28574259 614 THQLQFLEDADLIVIMDKGH 633
Cdd:cd03227 138 THLPELAELADKLIHIKKVI 157
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1049-1274 |
7.14e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILI---DSLDTNDIG 1119
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYPSGDIRFhgeSLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1120 LHDLR-SKISIIPQEPVLfsgtmryNLDPFEQypddkLWKALEDV---H--LKEEI--SELPSGLQSI--------ISEG 1183
Cdd:PRK15134 86 LRGVRgNKIAMIFQEPMV-------SLNPLHT-----LEKQLYEVlslHrgMRREAarGEILNCLDRVgirqaakrLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1184 GTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTIMD-SDKVLVMDAG 1260
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|....
gi 28574259 1261 HVVEFGSPYELLTA 1274
Cdd:PRK15134 234 RCVEQNRAATLFSA 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1067-1268 |
7.38e-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: 57.15 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYN--DGAILIDSLDTNDIGLHDlRSK--ISIIPQEPVLFSGtm 1141
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYEvtEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 rynldpfeqypddklwkaledVHLKEEISELPSGlqsiiseggtnFSVGQRQLVCLARAILRENRILVMDEATANVDpqT 1221
Cdd:cd03217 92 ---------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD--I 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1222 DAL--IQATIRN-KFKDCTVLTIAH--RLNTIMDSDKVLVMDAGHVVEFGSP 1268
Cdd:cd03217 138 DALrlVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
435-645 |
7.74e-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: 57.15 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE--SGSVQVSGKYsyasqepwLFNAS 512
Cdd:cd03217 2 EIKDLHVSVGGKE---ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILFGLPMDKQRYRTV--LKRCALERDLellhgdgtivgerGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:cd03217 71 PEERARLGIFLAFQYPPEIpgVKNADFLRYV-------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 591 HVGRHLFDECMRGFLGKQLVILVTHQLQFLE--DADLIVIMDKGHVSACGTYEEMLK 645
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1071-1266 |
9.83e-09 |
|
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: 56.92 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIqPMEKVGIVGRTGAGKSSLINALFRLS-------YNDGAILIDSldTNDIGLHDLRSKISIIPQEPVLFSG-TMR 1142
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEkpdggtiVLNGTVLFDS--RKKINLPPQQRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNLDPFEQYPDDKlwkalEDVHLKEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD 1222
Cdd:cd03297 94 ENLAFGLKRKRNR-----EDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 28574259 1223 ALIQATIRNKFKD--CTVLTIAHRLNTI-MDSDKVLVMDAGHVVEFG 1266
Cdd:cd03297 168 LQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
430-666 |
1.19e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPW 507
Cdd:PRK10636 309 PNPLLKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 508 LFnasvrdnilfgLPMDKQ--RYRTVLKRCALERDL-ELLHG---DGTIVGERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:PRK10636 386 EF-----------LRADESplQHLARLAPQELEQKLrDYLGGfgfQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 582 DDPLSAVDTHVgRHLFDECMRGFLGKQLVilVTHQLQFLEDA--DLIVIMDkghvsacGTYEEMLKSGQDFAQLLVESTQ 659
Cdd:PRK10636 455 DEPTNHLDLDM-RQALTEALIDFEGALVV--VSHDRHLLRSTtdDLYLVHD-------GKVEPFDGDLEDYQQWLSDVQK 524
|
....*..
gi 28574259 660 NSGGGDE 666
Cdd:PRK10636 525 QENQTDE 531
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1048-1283 |
1.95e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDIGLHDLRSK 1126
Cdd:PRK10253 7 RLRGEQLTLGYGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1127 ISIIPQEPVLFSGTMRYNLDPFEQYPDDKL---WKALEDVHLKEEISelPSGLQSIISEGGTNFSVGQRQLVCLARAILR 1203
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAMQ--ATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1204 ENRILVMDEATA--NVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAKVF 1280
Cdd:PRK10253 161 ETAIMLLDEPTTwlDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
...
gi 28574259 1281 HGM 1283
Cdd:PRK10253 241 YGL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1058-1295 |
2.31e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1058 YEPdtNSPCVLKGL---SFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSlDTNDIGLHDLRSKIS 1128
Cdd:PRK13643 11 YQP--NSPFASRALfdiDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqptegKVTVGDIVVSS-TSKQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1129 IIPQEP--VLFSGTM-------RYNLDPFEQYPDDKLWKALEDVHLKEEISElpsglqsiisEGGTNFSVGQRQLVCLAR 1199
Cdd:PRK13643 88 VVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1200 AILRENRILVMDEATANVDPQTDALIQATIRNKFKDC-TVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL------ 1271
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVfqevdf 237
|
250 260
....*....|....*....|....*....
gi 28574259 1272 -----LTASKAKVFHGMVMQTGKASFDHL 1295
Cdd:PRK13643 238 lkaheLGVPKATHFADQLQKTGAVTFEKL 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
452-589 |
2.97e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY----------------------SYASQEPWLf 509
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglsgrelrplrrrmqmvfqdPYASLNPRM- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 510 naSVRDnILfGLPMDKQRYRTVLKRcaLERDLELLhgdgTIVGERGASL-------SGGQRARICLARAVYRRADVYLLD 582
Cdd:COG4608 113 --TVGD-II-AEPLRIHGLASKAER--RERVAELL----ELVGLRPEHAdryphefSGGQRQRIGIARALALNPKLIVCD 182
|
....*..
gi 28574259 583 DPLSAVD 589
Cdd:COG4608 183 EPVSALD 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
436-654 |
3.01e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 436 IKALRARWgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSG-------------KYSYA 502
Cdd:TIGR01271 1220 VQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswnsvtlqtwrkAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCALERDLELLHGDGTIVGERGAS-LSGGQRARICLARAVYRRADVYLL 581
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 582 DDP---LSAVDTHVGR----HLFDECMrgflgkqlVILVTHQLQFLEDADLIVIMDKGHVSACGTYEEMLKSGQDFAQLL 654
Cdd:TIGR01271 1378 DEPsahLDPVTLQIIRktlkQSFSNCT--------VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1067-1274 |
3.26e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDS-----LDTNdIGLH-DL--RskisiipqEPVLF 1137
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEVNGrvsalLELG-AGFHpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1138 SGTMrYNLDPFEqyPDDKlwkaLEDVhlkEEISEL------P-----SGLQSIISeggtnFSVgqrqlvclarAILRENR 1206
Cdd:COG1134 112 NGRL-LGLSRKE--IDEK----FDEI---VEFAELgdfidqPvktysSGMRARLA-----FAV----------ATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1207 ILVMDEATAnVdpqTDALIQATIRNKFKD-----CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:COG1134 167 ILLVDEVLA-V---GDAAFQKKCLARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
451-675 |
3.31e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.89 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG--ELPPESGSV-----------------------QVSGKySYASQE 505
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcPVCGG-TLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 P--WLFNASVRDNIL----------FGLPMDKQRYRTVLK---------RCALERDLELLhgDGTIVGER----GASLSG 560
Cdd:TIGR03269 94 VdfWNLSDKLRRRIRkriaimlqrtFALYGDDTVLDNVLEaleeigyegKEAVGRAVDLI--EMVQLSHRithiARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 561 GQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVT-HQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIEDlSDKAIWLENGEIKEEG 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 28574259 639 TYEEMLKSgqdFAQLL--VESTQNSGGGDEIITSPNLSR 675
Cdd:TIGR03269 252 TPDEVVAV---FMEGVseVEKECEVEVGEPIIKVRNVSK 287
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
447-645 |
3.59e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 447 QHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSY----------------------A 502
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLngeplaaidaprlarlravlpqA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 503 SQEPWLFnaSVRDNILFGlpmdkqRYRTVLKRCALE-RDLEL------LHGDGTIVGERGASLSGGQRARICLARAV--- 572
Cdd:PRK13547 92 AQPAFAF--SAREIVLLG------RYPHARRAGALThRDGEIawqalaLAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 573 ------YRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQL-VILVTHQLQF-LEDADLIVIMDKGHVSACGTYEEML 644
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
.
gi 28574259 645 K 645
Cdd:PRK13547 244 T 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1071-1266 |
3.88e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDS--LDT-NDIGLHDLRSKISIIPQEPVLfsgtmryNLD 1146
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPYA-------SLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1147 PfEQYPDDKLWKALEdVH--------------LKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAILRENRILVMDE 1212
Cdd:PRK10261 416 P-RQTVGDSIMEPLR-VHgllpgkaaaarvawLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574259 1213 ATANVDPQtdalIQATIRNKFKD------CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:PRK10261 490 AVSALDVS----IRGQIINLLLDlqrdfgIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
432-642 |
3.96e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARWGQEqhdLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-------YSYAS- 503
Cdd:PRK11300 4 PLLSVSGLMMRFGGL---LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpgHQIARm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ------QEPWLFNA-------------SVRDNILFGLpMDKQRYRTVlKRCALERDLELLHGDG-TIVGERGA-SLSGGQ 562
Cdd:PRK11300 81 gvvrtfQHVRLFREmtvienllvaqhqQLKTGLFSGL-LKTPAFRRA-ESEALDRAATWLERVGlLEHANRQAgNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 563 RARICLARAVYRRADVYLLDDP---LSAVDTHVGRHLFDECMRGFlgKQLVILVTHQLQFLED-ADLIVIMDKGHVSACG 638
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPaagLNPKETKELDELIAELRNEH--NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
....
gi 28574259 639 TYEE 642
Cdd:PRK11300 237 TPEE 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
434-646 |
5.83e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQvsgkysyasqepWLFNASV 513
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 ------------RDNILFGLpM--------DKQRYRTVLKRcalerdleLLHGDGTIvGERGASLSGGQRARICLARAVY 573
Cdd:PRK15064 385 gyyaqdhaydfeNDLTLFDW-MsqwrqegdDEQAVRGTLGR--------LLFSQDDI-KKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 574 RRADVYLLDDPLSAVDTHVGRHLFD--ECMRGFLgkqlvILVTHQLQFLED--ADLIVIMDKGHVSACGTYEEMLKS 646
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMalEKYEGTL-----IFVSHDREFVSSlaTRIIEITPDGVVDFSGTYEEYLRS 526
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1068-1263 |
6.75e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILIDSLDTNDIGlHDLRSK--ISIIPQE-PVLFSGTMRY 1143
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1144 NLdPFEQYPDDKLWKA----LEDVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANV-D 1218
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 28574259 1219 PQTDAL--IQATIRNKFKdcTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:PRK09700 179 KEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
450-589 |
7.21e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA------------SQEPWLFNASVRDni 517
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvfsqhhvdgldlSSNPLLYMMRCFP-- 600
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 518 lfGLPmdKQRYRTVLKRCALERDLELlhgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:PLN03073 601 --GVP--EQKLRAHLGSFGVTGNLAL---------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1026-1264 |
7.49e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1026 DPEGDFNSPaekQPPKSWPKegkLVTKDLSLRYEPDTNSpcvLKGLSFTIQPMEKVGIVGRTGAGKSS---LINALFRLS 1102
Cdd:PRK10522 306 PYKAEFPRP---QAFPDWQT---LELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQPQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1103 ynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSGTmrynLDPFEQYPDDKL---WkaLEDVHLKEEISElpsglqsi 1179
Cdd:PRK10522 377 --SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALvekW--LERLKMAHKLEL-------- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1180 isEGG----TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ------TDALIQATIRNKfkdcTVLTIAHRLNTIM 1249
Cdd:PRK10522 441 --EDGrisnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFI 514
|
250
....*....|....*
gi 28574259 1250 DSDKVLVMDAGHVVE 1264
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1068-1262 |
7.60e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILIDSLDTNDIGLHDLRSK-ISIIPQEPVLFsgtmr 1142
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgTW-DGEIYWSGSPLKASNIRDTERAgIVIIHQELTLV----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 ynldpfeqypddKLWKALEDVHLKEEISeLPSGLQ--------------------SIISEGGTNFSVGQRQLVCLARAIL 1202
Cdd:TIGR02633 91 ------------PELSVAENIFLGNEIT-LPGGRMaynamylraknllrelqldaDNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1203 RENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVM-DAGHV 1262
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIrDGQHV 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
434-643 |
8.83e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSliqailGELPpesgsVQVSGkySYASQEPWLFNA-- 511
Cdd:NF000106 14 VEVRGLVKHFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**R------GALP-----AHV*G--PDAGRRPWRF*Twc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 ----SVRDNILFGLPMDKQRYRTVLKRCALE---RDLELLHGDG--------------TIVGERGASLSGGQRARICLAR 570
Cdd:NF000106 78 anrrALRRTIG*HRPVR*GRRESFSGRENLYmigR*LDLSRKDAraradellerfsltEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 571 AVYRRADVYLLDDPLSAVDTHVGRHLFDEcMRGFLGKQLVILVThqLQFLEDADL----IVIMDKGHVSACGTYEEM 643
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLT--TQYMEEAEQlaheLTVIDRGRVIADGKVDEL 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1049-1266 |
1.44e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNspcvLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDSLDTNDIGLHDLRSki 1127
Cdd:PRK11701 7 LSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLAPDAGEVHYRMRDGQLRDLYALSE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1128 siiPQEPVLfsgtMRYNLDPFEQYPDDKL-------------------------------WkaLEDVHLKEE-ISELPsg 1175
Cdd:PRK11701 81 ---AERRRL----LRTEWGFVHQHPRDGLrmqvsaggnigerlmavgarhygdiratagdW--LERVEIDAArIDDLP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1176 lqsiiseggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTI-MDSD 1252
Cdd:PRK11701 150 ---------TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElgLAVVIVTHDLAVArLLAH 220
|
250
....*....|....
gi 28574259 1253 KVLVMDAGHVVEFG 1266
Cdd:PRK11701 221 RLLVMKQGRVVESG 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1067-1268 |
1.46e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSldtndiglHDLR-----SKISIIPQEPVLFSGTM 1141
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN--------GKLRigyvpQKLYLDTTLPLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 RynLDPFEQYPDdkLWKALEDV---HLKEEISELPSGlqsiiseggtnfsvGQRQLVCLARAILRENRILVMDEATANVD 1218
Cdd:PRK09544 91 R--LRPGTKKED--ILPALKRVqagHLIDAPMQKLSG--------------GETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1219 PQTDA----LIQaTIRNKFkDCTVLTIAHRLNTIM-DSDKVLVMDaGHVVEFGSP 1268
Cdd:PRK09544 153 VNGQValydLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCLN-HHICCSGTP 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
452-655 |
1.64e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKySYAS---------------QEPWLFNA-SVRD 515
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NYNKldhklaaqlgigiiyQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 516 NILFG-LPMDK-------------QRYRTVLKRCALERDLEllhgdgtivgERGASLSGGQRARICLARAVYRRADVYLL 581
Cdd:PRK09700 100 NLYIGrHLTKKvcgvniidwremrVRAAMMLLRVGLKVDLD----------EKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 582 DDPLSAVDTHVGRHLFdecmrgFLGKQL------VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMlkSGQDFAQLL 654
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF------LIMNQLrkegtaIVYISHKLaEIRRICDRYTVMKDGSSVCSGMVSDV--SNDDIVRLM 241
|
.
gi 28574259 655 V 655
Cdd:PRK09700 242 V 242
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1071-1274 |
1.76e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGLHDL----RSK-----ISIIPQEPvlfsgtm 1141
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLspreRRKlvghnVSMIFQEP------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 RYNLDPFE--------------------QYPDDKLWKALEDVHlKEEISELPSGLQSIISEggtnFSVGQRQLVCLARAI 1201
Cdd:PRK15093 99 QSCLDPSErvgrqlmqnipgwtykgrwwQRFGWRKRRAIELLH-RVGIKDHKDAMRSFPYE----LTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1202 LRENRILVMDEATANVDPQTDALI--QATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTA 1274
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIfrLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1048-1245 |
1.77e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1048 KLVTKDLSLRYepdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLsyND--------GAILI--DSLDTND 1117
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL--NDlipgfrveGKVTFhgKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1118 IGLHDLRSKISIIPQEPVLFSGTMRYNL------DPFEQYPDDKLWKALEDVHLKEEISELpsglqsiISEGGTNFSVGQ 1191
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1192 RQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTIAHRL 1245
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
416-498 |
1.89e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 416 EVEKRSYPVGigkepDTLVEIKALRARwgQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV 495
Cdd:COG3845 245 RVEKAPAEPG-----EVVLEVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
...
gi 28574259 496 SGK 498
Cdd:COG3845 318 DGE 320
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
445-590 |
2.19e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 445 QEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPES--GSV---------QVSGKYSYASQEPWLF-NAS 512
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTIlannrkptkQILKRTGFVTQDDILYpHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 513 VRDNILF----GLPMDKQRYRTVLKRCALERDLELLHGDGTIVGE---RGasLSGGQRARICLARAVYRRADVYLLDDPL 585
Cdd:PLN03211 157 VRETLVFcsllRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....*
gi 28574259 586 SAVDT 590
Cdd:PLN03211 235 SGLDA 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
402-644 |
2.31e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.19 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 402 RRDEKAEEEQHLLK--EVEKRSYPVGIGKepdtlveIKALrarwgqeqhdlvlNNVNMSLRRGQLVAVIGPVGSGKSSLI 479
Cdd:TIGR03269 268 EKECEVEVGEPIIKvrNVSKRYISVDRGV-------VKAV-------------DNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 480 QAILGELPPESGSVQV-------------------SGKY-SYASQEPWLF-NASVRDN----ILFGLPMDKQRYRTV--L 532
Cdd:TIGR03269 328 KIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrgrAKRYiGILHQEYDLYpHRTVLDNlteaIGLELPDELARMKAVitL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 533 KRCALERDLELlhgdgTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM--RGFLGKQLV 610
Cdd:TIGR03269 408 KMVGFDEEKAE-----EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkaREEMEQTFI 482
|
250 260 270
....*....|....*....|....*....|....*
gi 28574259 611 IlVTHQLQFLED-ADLIVIMDKGHVSACGTYEEML 644
Cdd:TIGR03269 483 I-VSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
419-592 |
2.62e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 419 KRSYPV--GIGKEPDTLveiKALrarwgqeqhdlvlNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 496
Cdd:PRK11308 12 KKHYPVkrGLFKPERLV---KAL-------------DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 497 G----KYS------------------YAS-----------QEPWLFNASvrdnilfglpMDKQRYRtvlkrcalERDLEL 543
Cdd:PRK11308 76 GqdllKADpeaqkllrqkiqivfqnpYGSlnprkkvgqilEEPLLINTS----------LSAAERR--------EKALAM 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 544 LhgdgTIVGERGAS-------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHV 592
Cdd:PRK11308 138 M----AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1067-1266 |
3.06e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSY-NDGAILID------SLDTNDIGLHDLRSKISIIPQEpvlfsg 1139
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMpRSGTLNIAgnhfdfSKTPSDKAIRELRRNVGMVFQQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 tmrYNLDPF------------------EQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAI 1201
Cdd:PRK11124 91 ---YNLWPHltvqqnlieapcrvlglsKDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1202 LRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFG 1266
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1067-1271 |
3.75e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.93 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNdiGLHDLRSKISIIPQEPVLFSG-TMRYN 1144
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 LD------PFEQYP-----DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:PRK10851 95 IAfgltvlPRRERPnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1214 TANVDPQTDALIQATIRN-----KFkdcTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQlheelKF---TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
433-634 |
4.31e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA- 511
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 --------------SVRDNI-LFGLPMDKQRYRTVLKRC--ALERDLELLHgdgtivgERGASLSGGQRARICLARAVYR 574
Cdd:PRK11614 82 vaivpegrrvfsrmTVEENLaMGGFFAERDQFQERIKWVyeLFPRLHERRI-------QRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 575 RADVYLLDDPLSAVDTHVGRHLFD-------ECMRGFLGKQlvilvtHQLQFLEDADLIVIMDKGHV 634
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDtieqlreQGMTIFLVEQ------NANQALKLADRGYVLENGHV 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
451-589 |
4.45e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKY--SYASQEP------WLFNASVRDNILFGLP 522
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqHYASKEVarriglLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 523 MDKQRY--RTVLKRCALErDLELLH------GDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:PRK10253 102 VARGRYphQPLFTRWRKE-DEEAVTkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
736-935 |
4.79e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 53.19 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 736 VVLIMLCIgtqILASGGDYFLSYWVKNT--ASSSTLDIYYFTAINVGLVICALLRTLLFF--NITMHS-----STELHNT 806
Cdd:cd18552 1 LALAILGM---ILVAATTAALAWLLKPLldDIFVEKDLEALLLVPLAIIGLFLLRGLASYlqTYLMAYvgqrvVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 807 MFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMM-LAFYYWR 885
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLpLAALPIR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 886 dfylKTSRDVKRL-----EAVARspMYSHFSATLVGLPTIRAMGAQQTLIGQYDN 935
Cdd:cd18552 158 ----RIGKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFGAEDYEIKRFRK 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
450-621 |
4.88e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA--SQEPWLFNASVRDNILFGlpmDKQr 527
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAwvNQETPALPQPALEYVIDG---DRE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 528 YRtvlkrcALERDLE------------LLHG-----DGTIVGERGASL------------------SGGQRARICLARAV 572
Cdd:PRK10636 91 YR------QLEAQLHdanerndghaiaTIHGkldaiDAWTIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 28574259 573 YRRADVYLLDDPLSAVDTHVGRHLfDECMRGFLGKqlVILVTHQLQFLE 621
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWL-EKWLKSYQGT--LILISHDRDFLD 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
452-617 |
4.89e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK-YSYAS-------------QE----PWLfnaSV 513
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASttaalaagvaiiyQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFG-LPmdkQRYRTVLKRCALERDLELLHGDGTIV--GERGASLSGGQRARICLARAVYRRADVYLLDDP---LSA 587
Cdd:PRK11288 97 AENLYLGqLP---HKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPtssLSA 173
|
170 180 190
....*....|....*....|....*....|....
gi 28574259 588 VDTH----VGRHLFDEcmrgflGKqLVILVTHQL 617
Cdd:PRK11288 174 REIEqlfrVIRELRAE------GR-VILYVSHRM 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1066-1230 |
6.52e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.41 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1066 CVLKGLSFTIQPMEKVGIVGRTGAGKSSL---INALFRLSynDGAIlidSLDTNDIGLHDLRSKISII----PQEPVLfs 1138
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLPPA--AGTI---KLDGGDIDDPDVAEACHYLghrnAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 gTMRYNLDpfeqypddkLWKAL---EDVHLKEEISELpsGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:PRK13539 89 -TVAENLE---------FWAAFlggEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*
gi 28574259 1216 NVDPQTDALIQATIR 1230
Cdd:PRK13539 157 ALDAAAVALFAELIR 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
412-642 |
7.45e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 412 HLLKEVEKRSY-PVGI-----GKEPDTLVEIKALRARWGqeqhDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG 484
Cdd:NF033858 239 ALLPEEKRRGHqPVVIpprpaDDDDEPAIEARGLTMRFG----DFTaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 485 ELPPESGSVQVSGK------------YSYASQEPWLFNA-SVRDNI-----LFGLPMDK--QRYRTVLKRCALERDLEll 544
Cdd:NF033858 315 LLPASEGEAWLFGQpvdagdiatrrrVGYMSQAFSLYGElTVRQNLelharLFHLPAAEiaARVAEMLERFDLADVAD-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 545 hgdgtivgERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDThVGRHLFDECMRGFLGKQLV-ILV-THqlqFLED 622
Cdd:NF033858 393 --------ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP-VARDMFWRLLIELSREDGVtIFIsTH---FMNE 460
|
250 260
....*....|....*....|...
gi 28574259 623 A---DLIVIMDKGHVSACGTYEE 642
Cdd:NF033858 461 AercDRISLMHAGRVLASDTPAA 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1049-1275 |
7.55e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEpdtNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF---RLSYNDGAILidSLDTNDIGLHDLrs 1125
Cdd:PRK15056 7 IVVNDVTVTWR---NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRLASGKISIL--GQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1126 kISIIPQE-------PVLFSGTM---RYNLDPFEQYPDDK----LWKALEDVHLKE----EISELpsglqsiiseggtnf 1187
Cdd:PRK15056 80 -VAYVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRRAKKRdrqiVTAALARVDMVEfrhrQIGEL--------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFG 1266
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
....*....
gi 28574259 1267 SPYELLTAS 1275
Cdd:PRK15056 224 PTETTFTAE 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
431-619 |
8.38e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGqeqhDLVL-NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQV--SGKYSYASQ--- 504
Cdd:PRK11819 322 DKVIEAENLSKSFG----DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQsrd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 505 --EPwlfNASVRDNILFGLPMDKQRYRTVLKRCALER------DLEllhgdgTIVGErgasLSGGQRARICLARAVYRRA 576
Cdd:PRK11819 398 alDP---NKTVWEEISGGLDIIKVGNREIPSRAYVGRfnfkggDQQ------KKVGV----LSGGERNRLHLAKTLKQGG 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28574259 577 DVYLLDDPLSAVDTHVGRHLfDECMRGFLGKQLVI---------LVTHQLQF 619
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRAL-EEALLEFPGCAVVIshdrwfldrIATHILAF 515
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1027-1264 |
8.57e-07 |
|
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: 53.26 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1027 PEGDFNSPAEKQPPKSWpkeGKLVTKDLSLRYEPDTNSPC-VLKGLSFTIQPMEKVGIVGRTGAGKSSLIN---ALFRLS 1102
Cdd:COG4615 309 AEPAAADAAAPPAPADF---QTLELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKlltGLYRPE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1103 ynDGAILIDSLDTNDIGLHDLRSKISIIPQEPVLFSgtmryNLDPFEQYPDDKLWKA-LEDVHLKEEISelpsglqsiIS 1181
Cdd:COG4615 386 --SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-----RLLGLDGEADPARARElLERLELDHKVS---------VE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1182 EGG---TNFSVGQRQLVCLARAILrENR-ILVMDEATANVDPQ------TDALIQATIRNKfkdcTVLTIAHrlntimD- 1250
Cdd:COG4615 450 DGRfstTDLSQGQRKRLALLVALL-EDRpILVFDEWAADQDPEfrrvfyTELLPELKARGK----TVIAISH------Dd 518
|
250
....*....|....*....
gi 28574259 1251 -----SDKVLVMDAGHVVE 1264
Cdd:COG4615 519 ryfdlADRVLKMDYGKLVE 537
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
733-1019 |
8.91e-07 |
|
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: 52.39 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 733 LVFVVLIMLciGTQILASGGDYFLSYWVKNTASSSTLDIyyftainvglvicallRTLLFFNItmhsstelhntmfQGLS 812
Cdd:cd18544 40 LLLLALLYL--GLLLLSFLLQYLQTYLLQKLGQRIIYDL----------------RRDLFSHI-------------QRLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 813 rtaLYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPWYLINTFAMMLAFYYWRDFYLKTS 892
Cdd:cd18544 89 ---LSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 893 RDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDNYQDLHssgYYTFVSTSRAFGYY---LDLFCVAYVISV 969
Cdd:cd18544 166 RKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEY---RKANLKSIKLFALFrplVELLSSLALALV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 970 ILHnFFNPPLHNAGQIGL--AITQALGM-----TGMVQwgmrQSAELENAMTSVERV 1019
Cdd:cd18544 243 LWY-GGGQVLSGAVTLGVlyAFIQYIQRffrpiRDLAE----KFNILQSAMASAERI 294
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1052-1266 |
1.08e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.72 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlsyndgailidsldTNDIGlhdlrSKISIip 1131
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL----------------ANRTE-----GNVSV-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1132 qepvlfSGTMRYN---LDPF-EQYPDDKLWKALEDVHLKE-------EISELPSGLQSIiseggTNFSVGQRQLVCLARA 1200
Cdd:cd03233 64 ------EGDIHYNgipYKEFaEKYPGEIIYVSEEDVHFPTltvretlDFALRCKGNEFV-----RGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1201 ILRENRILVMDEATANVDPQTDALIQATIR---NKFKDCTVLTIAHRLNTIMDS-DKVLVMDAGHVVEFG 1266
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRtmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
451-633 |
1.37e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 451 VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYS--YASQEPWL-FNASVRDNI---------- 517
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKvgYLPQEPQLdPEKTVRENVeegvaevkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 ---------LFGLPMDKqrYRTVLKRCA-------------LERDLE-------LLHGDGTIvgergASLSGGQRARICL 568
Cdd:PRK11819 102 ldrfneiyaAYAEPDAD--FDALAAEQGelqeiidaadawdLDSQLEiamdalrCPPWDAKV-----TKLSGGERRRVAL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 569 ARAVYRRADVYLLDDPLSAVDTH----VGRHLfdecmRGFLGKqlVILVTHQLQFLED-ADLIVIMDKGH 633
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAEsvawLEQFL-----HDYPGT--VVAVTHDRYFLDNvAGWILELDRGR 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1067-1285 |
1.48e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKISIIPQE-PVLFSGTMRyN 1144
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVR-E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1145 LDPFEQYPddklWK-AL-----EDVHLKEEISELpSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVD 1218
Cdd:PRK10575 105 LVAIGRYP----WHgALgrfgaADREKVEEAISL-VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1219 --PQTD--ALIQATIRNkfKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELLTASKAKVFHGMVM 1285
Cdd:PRK10575 180 iaHQVDvlALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1067-1230 |
1.63e-06 |
|
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: 50.18 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIdsldtNDIGLHDLRSKIsiipQEPVLFSG---TMR 1142
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLL-----NGGPLDFQRDSI----ARGLLYLGhapGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNLDPFEQ-------YPDDKLWKALEDVHLkeeiselpSGLQSIISeggTNFSVGQRQLVCLARAILRENRILVMDEATA 1215
Cdd:cd03231 86 TTLSVLENlrfwhadHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....*
gi 28574259 1216 NVDPQTDALIQATIR 1230
Cdd:cd03231 155 ALDKAGVARFAEAMA 169
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1083-1271 |
1.68e-06 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 51.73 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1083 IVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHdLRSkISIIPQEPVLFSG-TMRYNLdpfeQYP-------- 1152
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDsGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFPHmTVEENV----AFGlkmrkvpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1153 ---DDKLWKALEDVHLKEEISELPSGLqsiiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ--- 1226
Cdd:TIGR01187 75 aeiKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlel 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28574259 1227 ATIRNKFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVVEFGSPYEL 1271
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1040-1271 |
1.79e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1040 PKSWPKEGKLVTKDLSLRYEPDT-NSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINAL--FRLSyNDGAILIDSLDTN 1116
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSfDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLagFEQP-TAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1117 DIGLHdlRSKISIIPQEPVLFSG-TMRYNLD-PFEQypdDKLWKA---------LEDVHLKEEISELPSGLqsiiseggt 1185
Cdd:PRK11607 85 HVPPY--QRPINMMFQSYALFPHmTVEQNIAfGLKQ---DKLPKAeiasrvnemLGLVHMQEFAKRKPHQL--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1186 nfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFK--DCTVLTIAHRLNTIMD-SDKVLVMDAGHV 1262
Cdd:PRK11607 151 --SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKF 228
|
....*....
gi 28574259 1263 VEFGSPYEL 1271
Cdd:PRK11607 229 VQIGEPEEI 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
452-636 |
1.94e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYA-SQEPWLFNASV-------RDNILFGLPM 523
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrSPQDGLANGIVyisedrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 524 DKQRYRTVL-----KRCALERDLELLHGDGTI-------------VGErgasLSGGQRARICLARAVYRRADVYLLDDPL 585
Cdd:PRK10762 348 KENMSLTALryfsrAGGSLKHADEQQAVSDFIrlfniktpsmeqaIGL----LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 586 SAVDTHVGRHLFDeCMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSA 636
Cdd:PRK10762 424 RGVDVGAKKEIYQ-LINQFKAEGLsIILVSSEMpEVLGMSDRILVMHEGRISG 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1006-1268 |
2.18e-06 |
|
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: 52.71 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1006 SAELENAMTSVERVLE-YKDLD-PEGDFNSPAEKQPPKSWPKegkLVTKDLSLRYEPdTNSPCVLKgLSFTIQPMEKVGI 1083
Cdd:TIGR01257 887 STREERALEKTEPLTEeMEDPEhPEGINDSFFERELPGLVPG---VCVKNLVKIFEP-SGRPAVDR-LNITFYENQITAF 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1084 VGRTGAGKSSLINALF-RLSYNDGAILIDSLDTnDIGLHDLRSKISIIPQEPVLFSG-TMRYNLDPFEQYPDdklwKALE 1161
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTgLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKG----RSWE 1036
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1162 DVHLKEEISELPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRNKFKDCTVLTI 1241
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMS 1116
|
250 260
....*....|....*....|....*...
gi 28574259 1242 AHRLNTI-MDSDKVLVMDAGHVVEFGSP 1268
Cdd:TIGR01257 1117 THHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
452-635 |
2.61e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSYAS--------------QEPWLF-NASVR 514
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASnirdteragiviihQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFG----LPMDKQRYRTVLKRC-ALERDLEL-LHGDGTIVGERGaslsGGQRARICLARAVYRRADVYLLDDPLSAV 588
Cdd:TIGR02633 97 ENIFLGneitLPGGRMAYNAMYLRAkNLLRELQLdADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 28574259 589 DTHVGRHLFDeCMRGFLGKQLV-ILVTHQLQFLED-ADLI-VIMDKGHVS 635
Cdd:TIGR02633 173 TEKETEILLD-IIRDLKAHGVAcVYISHKLNEVKAvCDTIcVIRDGQHVA 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1188-1271 |
2.65e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVdpqtDALIQATIRNKFK------DCTVLTIAH-RLNTIMDSDKVLVMDAG 1260
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNL----DANLRRSMREKIRelqqqfNITSLYVTHdQSEAFAVSDTVIVMNKG 213
|
90
....*....|.
gi 28574259 1261 HVVEFGSPYEL 1271
Cdd:PRK11432 214 KIMQIGSPQEL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
430-643 |
2.72e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 430 PDTLvEIKALRArwgqEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPP----ESGSVQVSGKYSYAS-- 503
Cdd:PRK10418 2 PQQI-ELRNIAL----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCal 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 504 ---------QEPW-LFN------ASVRDNIL-FGLPMDKQRYRTVLKRCALERdlellhgDGTIVGERGASLSGGQRARI 566
Cdd:PRK10418 77 rgrkiatimQNPRsAFNplhtmhTHARETCLaLGKPADDATLTAALEAVGLEN-------AARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 567 CLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECM-----RGfLGkqlVILVTHQLQFLED-ADLIVIMDKGHVSACGTY 640
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsivqkRA-LG---MLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
...
gi 28574259 641 EEM 643
Cdd:PRK10418 226 ETL 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1074-1258 |
3.08e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 50.10 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1074 TIQPMEKVGIVGRTGAGKSSLINALF-RLSYNDGAILIDsldtndiglhdlRSKISIIPQE-PVLFSGTMRYNLdpfeqy 1151
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAgVLKPDEGDIEIE------------LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1152 pDDKLWKALEDVHLKEEISElPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRn 1231
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR- 159
|
170 180 190
....*....|....*....|....*....|.
gi 28574259 1232 KF---KDCTVLTIAHRLNTI-MDSDKVLVMD 1258
Cdd:cd03237 160 RFaenNEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1185-1305 |
3.22e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.40 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1185 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR--NKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGH 1261
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGH 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 28574259 1262 VvefgspyelltaskakVFHGMVMQTGKASFDHLLKVAENTKQN 1305
Cdd:PRK09984 231 V----------------FYDGSSQQFDNERFDHLYRSINRVEEN 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
981-1244 |
3.43e-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: 51.29 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 981 NAGQIGLAITQALGMTGMVQWGMRQSAELENAMTSVERVLEykDLDpEGDFNSPAEKQPPKS---------WPKEGKLVT 1051
Cdd:TIGR00954 371 NNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLD--DVK-SGNFKRPRVEEIESGreggrnsnlVPGRGIVEY 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1052 KDLSLRYEpdtNSPCV-------LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL--SYNdGAILIDSldtndiglhd 1122
Cdd:TIGR00954 448 QDNGIKFE---NIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpVYG-GRLTKPA---------- 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1123 lRSKISIIPQEPVLFSGTMR----YNLDPFEQ----YPDDKLWKALEDVHLkEEISELPSGLqSIISEGGTNFSVGQRQL 1194
Cdd:TIGR00954 514 -KGKLFYVPQRPYMTLGTLRdqiiYPDSSEDMkrrgLSDKDLEQILDNVQL-THILEREGGW-SAVQDWMDVLSGGEKQR 590
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 28574259 1195 VCLARAILRENRILVMDEATANVDPQTDALIQATIRNkfKDCTVLTIAHR 1244
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1071-1262 |
4.26e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1071 LSFTIQPMEKVGIVGRTGAGKSSLINALFRlSYN---DGAILIDS--LDTNDIgLHDLRSKISIIPQE-------PVL-- 1136
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPgkfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1137 -----------FSGTMRYNldpfEQYPDDKLWKALEDVHLKEEISELPSGlqsiiseggtNFSVGQRQLVCLARAILREN 1205
Cdd:TIGR02633 357 gknitlsvlksFCFKMRID----AAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 1206 RILVMDEATANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHV 1262
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1068-1260 |
4.34e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTN-DIGLHDLRSKISIIPQE--PVLFSGTM-- 1141
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDfKSSKEALENGISMVHQElnLVLQRSVMdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 ----RYNL-----DPFEQYPDDK-LWKALE-DVHLKEEISELpsglqsiiseggtnfSVGQRQLVCLARAILRENRILVM 1210
Cdd:PRK10982 94 mwlgRYPTkgmfvDQDKMYRDTKaIFDELDiDIDPRAKVATL---------------SVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 1211 DEATANV-DPQTDALIqaTIRNKFKD--CTVLTIAHRLNTIMD-SDKVLVMDAG 1260
Cdd:PRK10982 159 DEPTSSLtEKEVNHLF--TIIRKLKErgCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1049-1226 |
4.58e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.43 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTNSPCVLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL-SYNDGAILIDSLDTNDI---GLHDLR 1124
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLssaAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1125 S-KISIIPQ---------------EPVLFSGTMRynldpfeQYPDDKLWKALEDVHLKEEISELPSGLqsiiseggtnfS 1188
Cdd:PRK11629 86 NqKLGFIYQfhhllpdftalenvaMPLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSEL-----------S 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 28574259 1189 VGQRQLVCLARAILRENRILVMDEATANVDPQT-DALIQ 1226
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNaDSIFQ 186
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
776-1019 |
5.05e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 49.82 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 776 AINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLT 855
Cdd:cd18563 51 GAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 856 LTGIICVLCVTNPWY----LINTFAMMLAFYYWRD----FYLKTSRdvkrleavARSPMYSHFSATLVGLPTIRAMGAQQ 927
Cdd:cd18563 131 IIGIGVVLFSLNWKLallvLIPVPLVVWGSYFFWKkirrLFHRQWR--------RWSRLNSVLNDTLPGIRVVKAFGQEK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 928 TLIGQYDNY-QDLhssgYYTFVSTSRAFGYYLDLFCVAYVISVILHNFFNPPLHNAGQIGL-AITQALGMTGM----VQW 1001
Cdd:cd18563 203 REIKRFDEAnQEL----LDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLgTLVAFLSYLGMfygpLQW 278
|
250
....*....|....*...
gi 28574259 1002 GMRQSAELENAMTSVERV 1019
Cdd:cd18563 279 LSRLNNWITRALTSAERI 296
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1175-1271 |
5.38e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1175 GLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT----DALIqATIRNKFkDCTVLTIAHRLNTIMD 1250
Cdd:PRK11300 142 GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKEtkelDELI-AELRNEH-NVTVLLIEHDMKLVMG 219
|
90 100
....*....|....*....|..
gi 28574259 1251 -SDKVLVMDAGHVVEFGSPYEL 1271
Cdd:PRK11300 220 iSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
432-632 |
5.99e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 432 TLVEIKALRARWGQEQHD-LVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE-----SGSVQVSGKYSYASQE 505
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 506 PWLfnASVRDN---ILFGLPM---------DKQRYRtVLkrcALERDLELLHGDGTI------VGERGAS---------L 558
Cdd:PRK15134 84 QTL--RGVRGNkiaMIFQEPMvslnplhtlEKQLYE-VL---SLHRGMRREAARGEIlncldrVGIRQAAkrltdyphqL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 559 SGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDEcMRGFLGKQLvILVTHQLQFLED-ADLIVIMDKG 632
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQilqLLRE-LQQELNMGL-LFITHNLSIVRKlADRVAVMQNG 233
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1081-1100 |
7.68e-06 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 49.38 E-value: 7.68e-06
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
422-636 |
7.70e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 422 YPvgigKEP----DTLVEIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE-SGSVQVS 496
Cdd:TIGR02633 246 YP----HEPheigDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 497 GKySYASQEPwlfNASVRDNILFgLPMDKQRY-------------RTVLKRCALERDLELLHGDGTIVGE------RGAS 557
Cdd:TIGR02633 322 GK-PVDIRNP---AQAIRAGIAM-VPEDRKRHgivpilgvgknitLSVLKSFCFKMRIDAAAELQIIGSAiqrlkvKTAS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 558 -------LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecMRGFLGKQ--LVILVTHQL-QFLEDADLIV 627
Cdd:TIGR02633 397 pflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK--LINQLAQEgvAIIVVSSELaEVLGLSDRVL 474
|
....*....
gi 28574259 628 IMDKGHVSA 636
Cdd:TIGR02633 475 VIGEGKLKG 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1067-1264 |
7.84e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYNDGAILIDSLDTNDIGlhdlrSKISIIPQEPVLFSgtmrynld 1146
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG-----REASLIDAIGRKGD-------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1147 pfeqyPDDKLwKALEDVHLkeeiSELPSGLQSIiseggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQ 1226
Cdd:COG2401 112 -----FKDAV-ELLNAVGL----SDAVLWLRRF-----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 28574259 1227 ATIRnkfKDC-----TVLTIAHRLNTI--MDSDKVLVMDAGHVVE 1264
Cdd:COG2401 177 RNLQ---KLArragiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
452-644 |
9.78e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.68 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPEsGSVQVSGK----YSYAS----------QEPWLFNASVRDNI 517
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRplsdWSAAElarhraylsqQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 518 LFGLP---MDKQRYRTVLKRCaleRDLEL---LHgdgtivgeRGAS-LSGG--QRARicLARA---VYRRADVY----LL 581
Cdd:COG4138 91 ALHQPagaSSEAVEQLLAQLA---EALGLedkLS--------RPLTqLSGGewQRVR--LAAVllqVWPTINPEgqllLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 582 DDPLSAVD-THVGrhLFDECMRGFLGKQL-VILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEML 644
Cdd:COG4138 158 DEPMNSLDvAQQA--ALDRLLRELCQQGItVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1067-1263 |
1.60e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF---RLSynDGAILIDSLDTNDIGLHD-LRSKISIIPQEPVLFSG-TM 1141
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgdpRAT--SGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 RYNLDPFEQYPDDKLWKAledvHLKEEISELPSGLQSIISEGGTnFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1221
Cdd:PRK11614 98 EENLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 28574259 1222 DALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVV 1263
Cdd:PRK11614 173 IQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1080-1100 |
1.61e-05 |
|
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: 45.30 E-value: 1.61e-05
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1049-1281 |
1.69e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.18 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1049 LVTKDLSLRYEPDTnspcVLKGLSFTIQPMEKVGIVGRTGAGKSSLI-NALFRLSYNDGAIL-----IDSLDTNDIG-LH 1121
Cdd:COG4152 2 LELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILAPDSGEVLwdgepLDPEDRRRIGyLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1122 D---LRSKISIIPQepVLFSGTMRyNLDPFEQYPDDKLWkaLEDVHLKE----EISELpsglqsiiseggtnfSVGQRQL 1194
Cdd:COG4152 78 EergLYPKMKVGEQ--LVYLARLK-GLSKAEAKRRADEW--LERLGLGDrankKVEEL---------------SKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1195 VCLARAILRENRILVMDEATANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSPYELL 1272
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIR 217
|
....*....
gi 28574259 1273 TASKAKVFH 1281
Cdd:COG4152 218 RQFGRNTLR 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
452-645 |
1.70e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNASVrdniLFG--------LP- 522
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGV----VFGqrsqlwwdLPa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 523 ------------MDKQRYRTVLKRCAlerdlELLHgdgtiVGE------RgaSLSGGQRARICLARAVYRRADVYLLDDP 584
Cdd:COG4586 114 idsfrllkaiyrIPDAEYKKRLDELV-----ELLD-----LGElldtpvR--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 585 LSAVDTHVGRHLfdecmRGFLgKQL-------VILVTHQLQFLED-ADLIVIMDKGHVSACGTYEEMLK 645
Cdd:COG4586 182 TIGLDVVSKEAI-----REFL-KEYnrergttILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1068-1260 |
1.89e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRLSYND-GAILIDSLDTNDIGLHDLR-SKISIIPQE----PVL----- 1136
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSILYLGKEVTFNGPKSSQeAGIGIIHQElnliPQLtiaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1137 -FSGtmRYNLDPF------EQYPD-DKLWKALEDVH-LKEEISELpsglqsiiseggtnfSVGQRQLVCLARAILRENRI 1207
Cdd:PRK10762 100 iFLG--REFVNRFgridwkKMYAEaDKLLARLNLRFsSDKLVGEL---------------SIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1208 LVMDEAT-ANVDPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAG 1260
Cdd:PRK10762 163 IIMDEPTdALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1082-1125 |
2.43e-05 |
|
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: 45.41 E-value: 2.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1082 GIVGRTGAGKSSLINALFRLS---------------------YNDGAILIDSLDTNDIGLHDLRS 1125
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEvaavgdrrpttraaqayvwqtGGDGLVLLDLPGVGERGRRDREY 65
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
431-484 |
2.92e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 28574259 431 DTLVEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILG 484
Cdd:CHL00131 5 KPILEIKNLHASVNENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1067-1267 |
4.55e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYN--DGAILIDSLDTNDIGlHDLRSKISIIP--QEPVLFSGT- 1140
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHPAYKilEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGVs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1141 ------MRYN----------LDP--FEQYPDDKlwkaLEDVHLKeeiselPSGLQSIISEGgtnFSVGQRQLVCLARAIL 1202
Cdd:CHL00131 101 nadflrLAYNskrkfqglpeLDPleFLEIINEK----LKLVGMD------PSFLSRNVNEG---FSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1203 RENRILVMDEATANVDpqTDAL-IQATIRNKFKDCT--VLTIAH--RLNTIMDSDKVLVMDAGHVVEFGS 1267
Cdd:CHL00131 168 LDSELAILDETDSGLD--IDALkIIAEGINKLMTSEnsIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1188-1271 |
4.94e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1188 SVGQRQLVCLARAILRENRILVMDEATANVDPqtdAL-----IQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGH 1261
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA---ALrvqmrIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGR 211
|
90
....*....|
gi 28574259 1262 VVEFGSPYEL 1271
Cdd:PRK11000 212 VAQVGKPLEL 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1067-1263 |
5.13e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL------SYNDGAILIDSLDTNDigLHDLRSK-ISIIPQepvlfsg 1139
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLdkptsgTYRVAGQDVATLDADA--LAQLRREhFGFIFQ------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1140 tmRYNLDPF---EQYPD-DKLWKALEDVHLKEEISELPS--GLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1213
Cdd:PRK10535 94 --RYHLLSHltaAQNVEvPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 1214 TANVDPQTDALIQATIRN-KFKDCTVLTIAHRLNTIMDSDKVLVMDAGHVV 1263
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-635 |
5.25e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELP--PESGSVQVSGKYSYAS--------------QEPWLF-NASVR 514
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASnirdteragiaiihQELALVkELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFG---LPMDKQRYRTVLKRC-ALERDLELLHGDGTIVGErgasLSGGQRARICLARAVYRRADVYLLDDPLSAVDT 590
Cdd:PRK13549 101 ENIFLGneiTPGGIMDYDAMYLRAqKLLAQLKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 591 HVGRHLFDecmrgfLGKQL------VILVTHQLQFLED-ADLI-VIMDKGHVS 635
Cdd:PRK13549 177 SETAVLLD------IIRDLkahgiaCIYISHKLNEVKAiSDTIcVIRDGRHIG 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
435-589 |
6.02e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 435 EIKALRARWGQEQHDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLFNA-SV 513
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQlTG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574259 514 RDNI-LFGLPM--DKQRYRTVLKRCALERDLellhgdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVD 589
Cdd:PRK13545 103 IENIeLKGLMMglTKEKIKEIIPEIIEFADI------GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
94-292 |
6.14e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 46.79 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 94 IMSGITIAALELGTRATVPLLLAGLIsefsehGNGHSYNAQIYAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAI 173
Cdd:cd18565 20 LLIGVAIDAVFNGEASFLPLVPASLG------PADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 174 YRKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRclihfhFL--------WLGPLELLIASYFLYEQIGMASFygisiLVL 245
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLER------FLddgansiiRVVVTVLGIGAILFYLNWQLALV-----ALL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 246 YLPLQTYLSRVTSKL--RLQTALRtdQRVRMMNEI----ISGIQVIKMYTWER 292
Cdd:cd18565 163 PVPLIIAGTYWFQRRiePRYRAVR--EAVGDLNARlennLSGIAVIKAFTAED 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1068-1268 |
6.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSS---LINALfrLSYNDGAILIDSLD-TNDIGLHDL---RSKISIIPQ--EPVLFS 1138
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTimqLLNGL--HVPTQGSVRVDDTLiTSTSKNKDIkqiRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 GT----MRYNLDPFEQYPDDKLWKALEDVHLKEeISElpsglqSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEAT 1214
Cdd:PRK13649 101 ETvlkdVAFGPQNFGVSQEEAEALAREKLALVG-ISE------SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 1215 ANVDPQTDALIQATIRNKFKD-CTVLTIAHRLNTIMD-SDKVLVMDAGHVVEFGSP 1268
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
452-660 |
6.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG--KYSYASQEPWLFNA-SVRDNILFGL------- 521
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlIVARLQQDPPRNVEgTVYDFVAEGIeeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 522 -------------PMDK---------------------QRYRTVLKRCALERDLELlhgdgtivgergASLSGGQRARIC 567
Cdd:PRK11147 99 kryhdishlvetdPSEKnlnelaklqeqldhhnlwqleNRINEVLAQLGLDPDAAL------------SSLSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 568 LARAVYRRADVYLLDDPLSavdthvgrHLfD----ECMRGFLG--KQLVILVTHQLQFLED-ADLIVIMDKGH-VSACGT 639
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTN--------HL-DietiEWLEGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKlVSYPGN 237
|
250 260
....*....|....*....|.
gi 28574259 640 YEEMLKSGQDfaQLLVESTQN 660
Cdd:PRK11147 238 YDQYLLEKEE--ALRVEELQN 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
436-648 |
8.23e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 436 IKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQvsgkysyaSQEPWL------ 508
Cdd:PRK10261 15 VENLNIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ--------CDKMLLrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 509 -------FNASVRD------NILFGLPMD---------KQRYRTVLKRCALERDLELLHGD-----------GTIVGERG 555
Cdd:PRK10261 87 vielseqSAAQMRHvrgadmAMIFQEPMTslnpvftvgEQIAESIRLHQGASREEAMVEAKrmldqvripeaQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 556 ASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDecMRGFLGKQL---VILVTHQLQFLED-ADLIVIMDK 631
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|....*..
gi 28574259 632 GHVSACGTYEEMLKSGQ 648
Cdd:PRK10261 245 GEAVETGSVEQIFHAPQ 261
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1073-1300 |
1.39e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1073 FTIQPMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSldtndiglhDLrsKISIIPQEP---VlfSGTM------- 1141
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIYEQ---------DL--IVARLQQDPprnV--EGTVydfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1142 ---------RYN--LDPFEQYPDDKLWKALEdvHLKEEIS-----ELPSGLQSIISEGG-------TNFSVGQRQLVCLA 1198
Cdd:PRK11147 91 ieeqaeylkRYHdiSHLVETDPSEKNLNELA--KLQEQLDhhnlwQLENRINEVLAQLGldpdaalSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1199 RAILRENRILVMDEATANVDPQTDALIQATIRNkFKDCTVLtIAH------RLNT-IMDsdkvlvMDAGHVVEFGSPYEL 1271
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHdrsfirNMATrIVD------LDRGKLVSYPGNYDQ 240
|
250 260
....*....|....*....|....*....
gi 28574259 1272 LTASKAKVFHGMVMQTgkASFDHllKVAE 1300
Cdd:PRK11147 241 YLLEKEEALRVEELQN--AEFDR--KLAQ 265
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
734-869 |
1.98e-04 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 45.09 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 734 VFVVLIMLCIGTqILASGGDYFLSY----WVKNTASSSTLDIYYFTAINVGLVICALLRTLLFF-------NITMHSSTE 802
Cdd:cd18547 1 LILVIILAIIST-LLSVLGPYLLGKaidlIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYlqnrlmaRVSQRTVYD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 803 LHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIFLTLTGIICVLCVTNPW 869
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPL 146
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
486-646 |
2.17e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 486 LPPESGSVQVSGKYSYASQEPWLFNASVRDNILFGLPMDKQRYRTVLKRCaLERdLELLH--GDGTIVGERGA-SLSGGQ 562
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEI-RER-LGFLIdvGLDYLSLSRAAgTLSGGE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 563 RARICLARAVYRR--ADVYLLDDP---LSAVDTH----VGRHLFDecmrgfLGKQlVILVTHQLQFLEDADLIVIMDK-- 631
Cdd:TIGR00630 494 AQRIRLATQIGSGltGVLYVLDEPsigLHQRDNRrlinTLKRLRD------LGNT-LIVVEHDEDTIRAADYVIDIGPga 566
|
170
....*....|....*....
gi 28574259 632 ----GHVSACGTYEEMLKS 646
Cdd:TIGR00630 567 gehgGEVVASGTPEEILAN 585
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
459-640 |
2.87e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 459 LRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG-KYSYASQEpwlfnasvrdnilfglpmdkqryrtvlkrcal 537
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 538 erdlellhgdgtivgergASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTH-------VGRHLFDEcmrgflGKQLV 610
Cdd:cd03222 70 ------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSEE------GKKTA 125
|
170 180 190
....*....|....*....|....*....|
gi 28574259 611 ILVTHQLQFLEDADLIVIMDKGHVSACGTY 640
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPGVYGIA 155
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
453-636 |
3.23e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 453 NNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGK--------------YSYASQ---EPWLF-NASVR 514
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrDNGFFpNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 515 DNILFGLPMDKQRYRTVL--------KRCAlERDLELLHGDGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLS 586
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMglfhevdeQRTA-ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 587 AVDT-------HVGRHLFDEcmrgflGKqLVILVTHQL-QFLEDADLIVIMDKGHVSA 636
Cdd:PRK09700 439 GIDVgakaeiyKVMRQLADD------GK-VILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
431-617 |
4.04e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 431 DTLVEIKALRARWGQEQHDLV-LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPE---SGSVQVSGKYSYASQEP 506
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 507 WLfNASVRDNI--LFGLPMDK---------------QRYRTVLKRCALERDLELLhgDGTIVGERGASL-------SGGQ 562
Cdd:PRK09473 90 EL-NKLRAEQIsmIFQDPMTSlnpymrvgeqlmevlMLHKGMSKAEAFEESVRML--DAVKMPEARKRMkmyphefSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 28574259 563 RARICLARAVYRRADVYLLDDPLSAVDTHVGRH---LFDECMRGFlgKQLVILVTHQL 617
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQimtLLNELKREF--NTAIIMITHDL 222
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
802-935 |
4.19e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.95 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 802 ELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPA----VMLDCIQIFLtltgIICVLCVTNPW-----YLI 872
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTglmnIWLDMITIII----AICIMLVLNPKltfvsLVI 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574259 873 NTFAMMLAFYYWRDFylktsRDVKRLEAVARSPMYSHFSATLVGLPTIRAMGAQQTLIGQYDN 935
Cdd:cd18554 156 FPFYILAVKYFFGRL-----RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDK 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-590 |
5.28e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 352 CVTAFYNILRRTVSKFFPSGMSQfAELLVSMRRITNFMMR----EEANVIDMSERRDEKAEEEQHLLKEVEKRSYpvgig 427
Cdd:TIGR00956 677 GFTVFFFFVYILLTEFNKGAKQK-GEILVFRRGSLKRAKKagetSASNKNDIEAGEVLGSTDLTDESDDVNDEKD----- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 428 KEPDTLVEIKALRARWGQEQ----HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGEL--------------PPE 489
Cdd:TIGR00956 751 MEKESGEDIFHWRNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgvitggdrlvngRPL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 490 SGSVQVSGKYSyASQEPWLFNASVRDNILFGLPM-------DKQRYRTVLKRCALerdLELLHGDGTIVGERGASLSGGQ 562
Cdd:TIGR00956 831 DSSFQRSIGYV-QQQDLHLPTSTVRESLRFSAYLrqpksvsKSEKMEYVEEVIKL---LEMESYADAVVGVPGEGLNVEQ 906
|
250 260
....*....|....*....|....*....
gi 28574259 563 RARICLARAVYRRADVYL-LDDPLSAVDT 590
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
422-593 |
5.83e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 422 YPvgigKEPDTLVEIkALRAR----WGQEQ-HDLVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPpesgsvqvs 496
Cdd:PRK13549 248 YP----REPHTIGEV-ILEVRnltaWDPVNpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 497 GKYsyaSQEPWLFNASV-----RDNILFGLPM---DKQRYRTVL-----------------KRCALERDLELlhgdGTIV 551
Cdd:PRK13549 314 GRW---EGEIFIDGKPVkirnpQQAIAQGIAMvpeDRKRDGIVPvmgvgknitlaaldrftGGSRIDDAAEL----KTIL 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 552 GE-------------RGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDthVG 593
Cdd:PRK13549 387 ESiqrlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID--VG 439
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1068-1264 |
6.35e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALfrlSYN----DGAILIDSLDTNDIGLHD-LRSKISIIPQE----PVLfs 1138
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKIL---SGNyqpdAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1139 gTMRYNLdPFEQYP------DDKLWKA-----LEdvHLKEEIS-ELPSGlqsiiseggtNFSVGQRQLVCLARAILRENR 1206
Cdd:PRK11288 95 -TVAENL-YLGQLPhkggivNRRLLNYeareqLE--HLGVDIDpDTPLK----------YLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1207 ILVMDEATANVD-PQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:PRK11288 161 VIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
328-498 |
6.65e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.08 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 328 RIAIFVSLLGFVLGGGELTAERAFCVTAFYNILRRTVSKFFPSGMSQFAELLVSMRRITNFMMREEAnviDMSERRDEKA 407
Cdd:COG3899 187 LALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAA---RLLGLAGAAA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 408 EEEQHLLKEVEKRSYPVGIGKEPDTLV----EIKALRARWGQeqhdlvlnnvnMSLRRGQLVAVIGPVGSGKSSLIQAIL 483
Cdd:COG3899 264 LLLLGLLAAAAAGRRLLARRLIPQPLVgreaELAALLAALER-----------ARAGRGELVLVSGEAGIGKSRLVRELA 332
|
170
....*....|....*
gi 28574259 484 GELPPESGSVqVSGK 498
Cdd:COG3899 333 RRARARGGRV-LRGK 346
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
763-945 |
6.75e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 43.34 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 763 TASSSTLdiyYFTAINVGLVICA-----LLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFaNDLGQ 837
Cdd:cd18566 35 NESIPTL---QVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 838 VDEV----MPAVMLDC--IQIFLTLTGIIcvlcvtNPWYLINTFAMMLAFYYWRDFYLKTSRDV--KRLEAVARSpmYSH 909
Cdd:cd18566 111 IREFltgqALLALLDLpfVLIFLGLIWYL------GGKLVLVPLVLLGLFVLVAILLGPILRRAlkERSRADERR--QNF 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 28574259 910 FSATLVGLPTIRAMGAQQTLIGQYDNYQDLHSSGYY 945
Cdd:cd18566 183 LIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGF 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
771-965 |
8.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 42.93 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 771 IYYFTAINVGLVICALLRTLLFfNITMHS-STELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDC 849
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLF-NIAGERiVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 850 IQIFLTLTGIICVLCVTNPwyliNTFAMMLAF---------YYWRdFYLKTSRDVkrLEAVARSPmySHFSATLVGLPTI 920
Cdd:cd18557 118 LRNILQVIGGLIILFILSW----KLTLVLLLVipllliaskIYGR-YIRKLSKEV--QDALAKAG--QVAEESLSNIRTV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 28574259 921 RAMGAQQTLIGQYDNYQD------LHSSGYYTFVSTSRAFGYYLDLFCVAY 965
Cdd:cd18557 189 RSFSAEEKEIRRYSEALDrsyrlaRKKALANALFQGITSLLIYLSLLLVLW 239
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
747-902 |
8.32e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 747 ILASGGDYFLSYW---------VKNTASSSTLDIYYFTAINVGLVICALLRTLLFfNITMHSST-ELHNTMFQGLSRTAL 816
Cdd:cd18784 6 LAAAVGEIFIPYYtgqvidgivIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLF-TLAMARLNiRIRNLLFRSIVSQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 817 YFFHTNPSGRILNRFANDLgqvdEVMPAVMLDCIQIFL--TLTGI-ICVLCVTNPWYL-INTFA----MMLAFYYWRDFY 888
Cdd:cd18784 85 GFFDTVKTGDITSRLTSDT----TTMSDTVSLNLNIFLrsLVKAIgVIVFMFKLSWQLsLVTLIglplIAIVSKVYGDYY 160
|
170
....*....|....
gi 28574259 889 LKTSRDVKRLEAVA 902
Cdd:cd18784 161 KKLSKAVQDSLAKA 174
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
774-935 |
9.32e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 42.84 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 774 FTAINVGLVICALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQVDEVMPAVMLDCIQIF 853
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 854 LTLTGIICVLCVTNPWYLINTFA----MMLAFYYWRDFYLKTSRDVKRleavARSPMYSHFSATLVGLPTIRAMGAQQTL 929
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAvlplLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREDEN 201
|
....*.
gi 28574259 930 IGQYDN 935
Cdd:cd18545 202 EEIFDE 207
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
450-645 |
1.02e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 450 LVLNNVNMS---------LRRGQLVAVIGPVGSGKSSLIQAILGeLPPESGSVQVSGK-------YSYASQEPWLfnaSV 513
Cdd:PRK03695 1 MQLNDVAVStrlgplsaeVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQpleawsaAELARHRAYL---SQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 514 RDNILFGLPM------------DKQRYRTVLKR-CALERDLELLHgdgtivgeRGAS-LSGGQRARICLARA---VYRRA 576
Cdd:PRK03695 77 QQTPPFAMPVfqyltlhqpdktRTEAVASALNEvAEALGLDDKLG--------RSVNqLSGGEWQRVRLAAVvlqVWPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574259 577 DVY----LLDDPLSAVDthVGRH-LFDECMRGFLGKQLVILVT-HQL-QFLEDADLIVIMDKGHVSACGTYEEMLK 645
Cdd:PRK03695 149 NPAgqllLLDEPMNSLD--VAQQaALDRLLSELCQQGIAVVMSsHDLnHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1068-1095 |
1.15e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.77 E-value: 1.15e-03
10 20
....*....|....*....|....*...
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLI 1095
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTI 65
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
557-648 |
1.24e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 557 SLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLfdecmRGFLGK--QLVILVTHQLQFLED--ADLIVIMDKG 632
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-----ETYLLKwpKTFIVVSHAREFLNTvvTDILHLHGQK 418
|
90 100
....*....|....*....|...
gi 28574259 633 HVSACGTY-------EEMLKSGQ 648
Cdd:PLN03073 419 LVTYKGDYdtfertrEEQLKNQQ 441
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
1082-1100 |
1.26e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 41.08 E-value: 1.26e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
452-639 |
1.35e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL-----------GELPPESGSV---QVSGKYSYASQEPwlFNASVRDN- 516
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkKEQPGNHDRIeglEHIDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 517 -----------ILFGLPMDKQRY-RTVL------KRCA-------------------LERDLELLH--GDGTI-VGERGA 556
Cdd:cd03271 89 atytgvfdeirELFCEVCKGKRYnRETLevrykgKSIAdvldmtveealeffenipkIARKLQTLCdvGLGYIkLGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 557 SLSGGQRARICLARAVYRRAD---VYLLDDPLSAVDTHVGRHLFDECMRGFLGKQLVILVTHQLQFLEDADLIVIM---- 629
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpeg 248
|
250
....*....|..
gi 28574259 630 -DK-GHVSACGT 639
Cdd:cd03271 249 gDGgGQVVASGT 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1068-1264 |
1.54e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1068 LKGLSFTIQPMEKVGIVGRTGAGKSSLINALFRL----SYnDGAILidsLDTNDIGLHDLRSK----ISIIPQE----PV 1135
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgSY-EGEIL---FDGEVCRFKDIRDSealgIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1136 L------FSGTMRYN---LDPFEQYPDDKlwKALEDVHLKEEiselPsglQSIISEGGtnfsVGQRQLVCLARAILRENR 1206
Cdd:NF040905 93 LsiaeniFLGNERAKrgvIDWNETNRRAR--ELLAKVGLDES----P---DTLVTDIG----VGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1207 ILVMDEATANV-DPQTDALIQATIRNKFKDCTVLTIAHRLNTIMD-SDKVLVMDAGHVVE 1264
Cdd:NF040905 160 LLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
763-868 |
1.76e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 42.09 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 763 TASSSTLDIYYFTAINVGLVI----CALLRTLLFFNITMHSSTELHNTMFQGLSRTALYFFHTNPSGRILNRFANDLGQV 838
Cdd:cd18576 27 LGGGDTASLNQIALLLLGLFLlqavFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQI 106
|
90 100 110
....*....|....*....|....*....|
gi 28574259 839 DEVMPAVMLDCIQIFLTLTGIICVLCVTNP 868
Cdd:cd18576 107 QDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1077-1250 |
2.25e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1077 PMEKVGIVGRTGAGKSSLINALFR-LSYNDGAILIDSLDTNDIGLHDLRSKIsiipqepvlfsgtmrynldpfeqypddk 1155
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1156 lwkaledvhlkeeiselpsglqsIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIR----- 1230
Cdd:smart00382 53 -----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|..
gi 28574259 1231 --NKFKDCTVLTIAHRLNTIMD 1250
Cdd:smart00382 110 llKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
135-347 |
2.31e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 41.73 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 135 IYAVLLIACILASVLLT--HPYMMG--MMHLAMKMRVAVssaiYRKALRLSRTSLGGTTTGQVVNLLSNDLNRfdrclIH 210
Cdd:cd18563 44 LLVLGLAGAYVLSALLGilRGRLLArlGERITADLRRDL----YEHLQRLSLSFFDKRQTGSLMSRVTSDTDR-----LQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 211 fHFLWLGPLELLIasyflyeQIGMasFYGISILVLYL------------PLQTYLSRVTSKlRLQTA-LRTDQRVRMMN- 276
Cdd:cd18563 115 -DFLSDGLPDFLT-------NILM--IIGIGVVLFSLnwklallvlipvPLVVWGSYFFWK-KIRRLfHRQWRRWSRLNs 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 277 ---EIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRqMNLLRGILLSFEITLGriAIFVSLLG--FVLGG----G 343
Cdd:cd18563 184 vlnDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEK-LWATFFPLLTFLTSLG--TLIVWYFGgrQVLSGtmtlG 260
|
....
gi 28574259 344 ELTA 347
Cdd:cd18563 261 TLVA 264
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
452-483 |
2.49e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|..
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAIL 483
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTL 655
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
456-496 |
2.60e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 28574259 456 NMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVS 496
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ 63
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1074-1258 |
3.00e-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: 41.69 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1074 TIQPMEKVGIVGRTGAGKSSLINALfrlsynDGAILIDSldtndiGLHDLRSKISIIPQEPV-LFSGTMRYNLdpFEQYP 1152
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL------AGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL--RSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1153 DDklwkaLEDVHLKEEISElPSGLQSIISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP----QTDALIQAT 1228
Cdd:COG1245 428 DD-----FGSSYYKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRF 501
|
170 180 190
....*....|....*....|....*....|.
gi 28574259 1229 IRNkfKDCTVLTIAHRLNTI-MDSDKVLVMD 1258
Cdd:COG1245 502 AEN--RGKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
433-646 |
3.14e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 433 LVEIKALRARWGQEQHDL-VLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGeLPPESGSVQVSgKYSYASQEPWLFNA 511
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAE-KLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 512 SVRDNI-------LFGLPMdkqryrTVLKRC---------AL------------ERDLELLhgdgTIVG-ERGAS----- 557
Cdd:PRK11022 81 KERRNLvgaevamIFQDPM------TSLNPCytvgfqimeAIkvhqggnkktrrQRAIDLL----NQVGiPDPASrldvy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 558 ---LSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFD--------ECMRgflgkqlVILVTHQLQFL-EDADL 625
Cdd:PRK11022 151 phqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElllelqqkENMA-------LVLITHDLALVaEAAHK 223
|
250 260
....*....|....*....|.
gi 28574259 626 IVIMDKGHVSACGTYEEMLKS 646
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRA 244
|
|
| YlqF_related_GTPase |
cd01849 |
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ... |
1080-1125 |
3.38e-03 |
|
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.
Pssm-ID: 206746 [Multi-domain] Cd Length: 146 Bit Score: 39.29 E-value: 3.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 28574259 1080 KVGIVGRTGAGKSSLINAL---FRLSYNDGAIL----IDSLDTNDIGLHDLRS 1125
Cdd:cd01849 93 RVGVVGLPNVGKSSFINALlnkFKLKVGSIPGTtklqQDVKLDKEIYLYDTPG 145
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
452-650 |
3.58e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 452 LNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSGKYSYASQEPWLfNASVR--DNILFG-LPMDKQRY 528
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEFKmLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 529 RTVLKRCALERDLELlhgdGTIVGERGASLSGGQRARICLARAVYRRADVYLLDDPLSAVDTHVGRHLFDECMRGFLGKQ 608
Cdd:PRK13546 119 EIKAMTPKIIEFSEL----GEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 28574259 609 LVILVTHQL-QFLEDADLIVIMDKGHVSACGTYEEMLKSGQDF 650
Cdd:PRK13546 195 TIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAF 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
434-497 |
3.67e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574259 434 VEIKALRARWGQEQhdlVLNNVNMSLRRGQLVAVIGPVGSGKSSLIQAILGELPPESGSVQVSG 497
Cdd:NF033858 2 ARLEGVSHRYGKTV---ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1067-1268 |
4.06e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLS--YNDGAILIDSL--------------DTNDIglHDlrskisi 1129
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgRKTggYIEGDIRISGFpkkqetfarisgycEQNDI--HS------- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1130 iPQ----EPVLFSGTMRYnldPFEQYPDDKL------WKALEDVHLKEEISELPsglqsiiseGGTNFSVGQRQLVCLAR 1199
Cdd:PLN03140 966 -PQvtvrESLIYSAFLRL---PKEVSKEEKMmfvdevMELVELDNLKDAIVGLP---------GVTGLSTEQRKRLTIAV 1032
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574259 1200 AILRENRILVMDEATANVDPQTDALIQATIRNKFKD--CTVLTIAHRLNTIMDS-DKVLVMDAGHVVEFGSP 1268
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgrTVVCTIHQPSIDIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
446-489 |
4.30e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.54 E-value: 4.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 28574259 446 EQHDLVLNNVNMSLRRGQ-LVAVIGPVGSGKSSLIQAILGELPPE 489
Cdd:COG3267 26 PSHREALARLEYALAQGGgFVVLTGEVGTGKTTLLRRLLERLPDD 70
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
1080-1100 |
4.44e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 39.40 E-value: 4.44e-03
10 20
....*....|....*....|.
gi 28574259 1080 KVGIVGRTGAGKSSLINALFR 1100
Cdd:cd04164 5 KVVIAGKPNVGKSSLLNALAG 25
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
457-491 |
6.40e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 39.41 E-value: 6.40e-03
10 20 30
....*....|....*....|....*....|....*
gi 28574259 457 MSlRRGQLVAVIGPVGSGKSSLIQAILGELPPESG 491
Cdd:COG3709 1 MS-GPGRLIYVVGPSGAGKDSLLAAARARLAADPR 34
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
465-491 |
6.91e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 38.75 E-value: 6.91e-03
10 20
....*....|....*....|....*....
gi 28574259 465 VAVIGPVGSGKSSLIQAILGE--LPPESG 491
Cdd:pfam00350 1 IAVVGDQSSGKSSVLNALLGRdiLPRGPG 29
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
466-493 |
6.94e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 6.94e-03
10 20
....*....|....*....|....*...
gi 28574259 466 AVIGPVGSGKSSLIQAILGELPPESGSV 493
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV 28
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1067-1266 |
7.35e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.63 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1067 VLKGLSFTIQPMEKVGIVGRTGAGKSSLINALF-RLSYND--GAILIDsldtNDIGLHDLRSKISIIPQEPVLFSG-TMR 1142
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNftGTILAN----NRKPTKQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1143 YNLD-------PFEQYPDDKLWKAlEDVhlkeeISELpsGL----QSIIsegGTNF----SVGQRQLVCLARAILRENRI 1207
Cdd:PLN03211 159 ETLVfcsllrlPKSLTKQEKILVA-ESV-----ISEL--GLtkceNTII---GNSFirgiSGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 1208 LVMDEATANVDpQTDA--LIQ--ATIRNKFKdcTVLTIAH----RLNTIMDSdkVLVMDAGHVVEFG 1266
Cdd:PLN03211 228 LILDEPTSGLD-ATAAyrLVLtlGSLAQKGK--TIVTSMHqpssRVYQMFDS--VLVLSEGRCLFFG 289
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
1082-1099 |
7.41e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 7.41e-03
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-362 |
7.84e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 39.83 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 97 GITIAALELGTRA--TVPLLLAGLISEFSEHGNGHSYNAQIyAVLLIACILASVLLTHPYMMGMMHLAMKMRVAVSSAIY 174
Cdd:cd18778 2 ILTLLCALLSTLLglVPPWLIRELVDLVTIGSKSLGLLLGL-ALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 175 RKALRLSRTSLGGTTTGQVVNLLSNDLNRFDRCLIHfhflwlgPLELLIASYFlyeqigmaSFYGISILVLY-------- 246
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIAD-------GIPQGITNVL--------TLVGVAIILFSinpklall 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 247 ----LPLQTYLSRVTSKlRLQTALRTDQRVR-----MMNEIISGIQVIKMYTWERP----FGKLIGQMRRSEMSSIRQMN 313
Cdd:cd18778 146 tlipIPFLALGAWLYSK-KVRPRYRKVREALgelnaLLQDNLSGIREIQAFGREEEeakrFEALSRRYRKAQLRAMKLWA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 28574259 314 LLRGiLLSFEITLGriaiFVSLLGF----VLGG----GELTAERAFcVTAFYNILRR 362
Cdd:cd18778 225 IFHP-LMEFLTSLG----TVLVLGFggrlVLAGeltiGDLVAFLLY-LGLFYEPITS 275
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
1081-1100 |
9.72e-03 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 38.65 E-value: 9.72e-03
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1036-1258 |
9.81e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1036 EKQPPKSWPKEGKLV-----TKDL---SLRYEPdtnspcvlkGlsfTIQPMEKVGIVGRTGAGKSSLINALfrlsynDGA 1107
Cdd:PRK13409 327 EERPPRDESERETLVeypdlTKKLgdfSLEVEG---------G---EIYEGEVIGIVGPNGIGKTTFAKLL------AGV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574259 1108 ILIDSldtndiGLHDLRSKISIIPQE-PVLFSGTMRYNLdpfEQYPDDklwkaLEDVHLKEEISElPSGLQSIISEGGTN 1186
Cdd:PRK13409 389 LKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLL---RSITDD-----LGSSYYKSEIIK-PLQLERLLDKNVKD 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28574259 1187 FSVGQRQLVCLARAILRENRILVMDEATANVDPQTDALIQATIRN--KFKDCTVLTIAHRLNTI-MDSDKVLVMD 1258
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDHDIYMIdYISDRLMVFE 528
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
1080-1098 |
9.85e-03 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 40.03 E-value: 9.85e-03
|
| |
