|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
83-1369 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 859.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 83 EKVLPENpraRSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKNDgrSPSLVRALLRV 162
Cdd:PLN03130 224 EQICPER---HANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP--KPWLLRALNNS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 163 FG---WQLGF----PGLAIFVvelglrtlQPIFLVKLI-SYFSGEPdaANAGFYYAVAQIVISALTVMILTPTTFGIHHV 234
Cdd:PLN03130 299 LGgrfWLGGFfkigNDLSQFV--------GPLLLNLLLeSMQNGEP--AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRV 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 235 CFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVL 314
Cdd:PLN03130 369 GFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 315 FMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDfa 394
Cdd:PLN03130 449 MLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN-- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 395 rRIVLSRVAIFLSLVG---YVILGKVFTPEIAFMITAYYNVLLAAMSIYvPSAIIQTAQFLTSIRRVEQFMQSEELGSSD 471
Cdd:PLN03130 527 -SFILNSIPVLVTVVSfgvFTLLGGDLTPARAFTSLSLFAVLRFPLFML-PNLITQAVNANVSLKRLEELLLAEERVLLP 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 472 ksegpskdtvpgNPPSnnnEADLlkSAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGEL 551
Cdd:PLN03130 605 ------------NPPL---EPGL--PAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 552 KANS-GQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKA 630
Cdd:PLN03130 668 PPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQ 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 631 RISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 711 KTG-----LITGLGSLSKTDKAKTEEQEPLNLNSPDNKNEVTPIKENSEQT--VGGSSSGKEHVERQESGGISLALYRKY 783
Cdd:PLN03130 828 NNGplfqkLMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKkkSKEGKSVLIKQEERETGVVSWKVLERY 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 784 FQAGGGLVAFLVMLSSSVLAQVAVTGGDYFLTYWVkKESTAAGHGEMedmesksmdVYK--YTLIIILSVIMNLSSSFLL 861
Cdd:PLN03130 908 KNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWT-DQGTPKTHGPL---------FYNliYALLSFGQVLVTLLNSYWL 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 862 FNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLV 941
Cdd:PLN03130 978 IMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLW 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 942 PTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQ 1021
Cdd:PLN03130 1058 AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNR 1137
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1022 AFGYCMNCICVIYIsIITLSFFAFPPGNGAD-------VGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEYESIE 1094
Cdd:PLN03130 1138 WLAIRLETLGGLMI-WLTASFAVMQNGRAENqaafastMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLP 1216
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1095 PEGMLEApDDKKPPKTWPEQGEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD- 1173
Cdd:PLN03130 1217 SEAPLVI-ENNRPPPGWPSSGSIKFEDVVLRYRPELPP--VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELEr 1293
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1174 GSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGT 1253
Cdd:PLN03130 1294 GRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGE 1373
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1254 NFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEF 1333
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEF 1453
|
1290 1300 1310
....*....|....*....|....*....|....*.
gi 442622995 1334 GSPYELMTKSDSkVFHNLVNQSGRASYEGLLKIAQE 1369
Cdd:PLN03130 1454 DTPENLLSNEGS-AFSKMVQSTGAANAQYLRSLVFG 1488
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
90-1356 |
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: 834.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 90 PRARSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKNDG------------------- 150
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRkqpvsavygkkdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 151 --------------------RSPSLVRALLRVFGwqlgfpglAIFVVELGLRTLQPIF------LVKLISYFSGEPDAAN 204
Cdd:TIGR00957 283 sqldaneevealivksphkpRKPSLFKVLYKTFG--------PYFLMSFCFKAIHDLMmfigpqILSLLIRFVNDPMAPD 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 205 -AGFYYAVAQIVISALTVMILTPttfgIHHVCF----KMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPR-LD 278
Cdd:TIGR00957 355 wQGYFYTGLLFVCACLQTLILHQ----YFHICFvsgmRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRfMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 279 SAPYtVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVL 358
Cdd:TIGR00957 431 LATY-INMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 359 KMYAWEQPFEQMVTHAREKEMNTIRQGQYIRG---FDFARR---IVLSRVAIFLslvgYVILGKVFTPEIAFMITAYYNV 432
Cdd:TIGR00957 510 KLYAWELAFLDKVEGIRQEELKVLKKSAYLHAvgtFTWVCTpflVALITFAVYV----TVDENNILDAEKAFVSLALFNI 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 433 LLAAMSIyVPSAIIQTAQFLTSIRRVEQFMQSEELgssdksEGPSKDTVPGNPPSNNneadllksAISIRDLKAKWDPNS 512
Cdd:TIGR00957 586 LRFPLNI-LPMVISSIVQASVSLKRLRIFLSHEEL------EPDSIERRTIKPGEGN--------SITVHNATFTWARDL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 513 PDyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQR 592
Cdd:TIGR00957 651 PP-TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 593 YEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCV--RGH 670
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGV 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 671 LRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLK-------------------------TGLITGLG------ 719
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQrdgafaeflrtyapdeqqghledswTALVSGEGkeakli 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 720 --SLSKTDKAKTEEQEPLNLNSPDNKNEVTPIKENSEQTVGGS--SSGK-EHVERQESGGISLALYRKYFQAGGGLVAFL 794
Cdd:TIGR00957 890 enGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAkeETWKlMEADKAQTGQVELSVYWDYMKAIGLFITFL 969
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 795 VMLSSsVLAQVAVTGGDYFLTYWVkkeSTAAGHGEMEDMESKsMDVYKYTLIIILSVIMNLSSSFLLFNIakKASIRLHN 874
Cdd:TIGR00957 970 SIFLF-VCNHVSALASNYWLSLWT---DDPMVNGTQNNTSLR-LSVYGALGILQGFAVFGYSMAVSIGGI--QASRVLHQ 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 875 TIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYHLR 954
Cdd:TIGR00957 1043 DLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQ 1122
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 955 NLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCI--CV 1032
Cdd:TIGR00957 1123 RFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgnCI 1202
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1033 IYISII--TLSFFAFPPGNgadVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEYESIEPEgmleAP---DDKKP 1107
Cdd:TIGR00957 1203 VLFAALfaVISRHSLSAGL---VGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE----APwqiQETAP 1275
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1108 PKTWPEQGEIIFKELNLRYTPNAkaENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQM 1186
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYREDL--DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRiNESAEGEIIIDGLNIAKI 1353
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1187 GLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLA 1266
Cdd:TIGR00957 1354 GLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLA 1433
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDsk 1346
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG-- 1511
|
1370
....*....|
gi 442622995 1347 VFHNLVNQSG 1356
Cdd:TIGR00957 1512 IFYSMAKDAG 1521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-1373 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 831.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 74 ENNSAQNEKEKVLP--EN--PRARSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKND 149
Cdd:PLN03232 208 NNESLDNVEYDALRggENicPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 150 grSPSLVRALLRVFGWQLGFPGlaIFVVELGL-RTLQPIFLVKLISYFSgEPDAANAGFYYAVaqIVISALTVMILTPTT 228
Cdd:PLN03232 288 --KPWLLRALNNSLGGRFWLGG--IFKIGHDLsQFVGPVILSHLLQSMQ-EGDPAWVGYVYAF--LIFFGVTFGVLCESQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 229 FGIH--HVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIG 306
Cdd:PLN03232 361 YFQNvgRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLG 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 307 ISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQ 386
Cdd:PLN03232 441 VASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQ 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 387 YIRGFDfarRIVLSRVAIFLSLVG---YVILGKVFTPEIAFMITAYYNVLLAAMSIyVPSAIIQTAQFLTSIRRVEQFMQ 463
Cdd:PLN03232 521 LLSAFN---SFILNSIPVVVTLVSfgvFVLLGGDLTPARAFTSLSLFAVLRSPLNM-LPNLLSQVVNANVSLQRIEELLL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 464 SEElgssdKSEGPSKDTVPGNPpsnnneadllksAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSL 543
Cdd:PLN03232 597 SEE-----RILAQNPPLQPGAP------------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSL 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 544 IQAILGELK-ANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGA 622
Cdd:PLN03232 660 ISAMLGELShAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGV 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 623 TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKA 702
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 703 LGDYESLLKTGLitgLGSLSKTDKAKTEEQEPLNLNSpDNKNEVTPIKEN--SEQTVGGSSSGKE------HVERQESGG 774
Cdd:PLN03232 820 EGTFAELSKSGS---LFKKLMENAGKMDATQEVNTND-ENILKLGPTVTIdvSERNLGSTKQGKRgrsvlvKQEERETGI 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 775 ISLALYRKYFQAGGGLVAFLVMLSSSVLAQVAVTGGDYFLTYWVKkESTAAGHgemedmeSKSMDVYKYTLIIILSVIMN 854
Cdd:PLN03232 896 ISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTD-QSTPKSY-------SPGFYIVVYALLGFGQVAVT 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 855 LSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIAN 934
Cdd:PLN03232 968 FTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGT 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 935 VNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDahSSAFF 1014
Cdd:PLN03232 1048 VSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD--NNIRF 1125
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1015 MYISTSQAFGYCMNCICVIYISI-ITLSFFAFPPGN-------GADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVER 1086
Cdd:PLN03232 1126 TLANTSSNRWLTIRLETLGGVMIwLTATFAVLRNGNaenqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVER 1205
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1087 VVEYESIEPEgmleAPD---DKKPPKTWPEQGEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLI 1163
Cdd:PLN03232 1206 VGNYIDLPSE----ATAiieNNRPVSGWPSRGSIKFEDVHLRYRPGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1164 NALFRLSYTD-GSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPD 1242
Cdd:PLN03232 1280 NALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPF 1359
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1243 GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKV 1322
Cdd:PLN03232 1360 GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKI 1439
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1323 MVMDAGRVVEFGSPYELMTKsDSKVFHNLVNQSGRASYEGLLKIAQETFES 1373
Cdd:PLN03232 1440 LVLSSGQVLEYDSPQELLSR-DTSAFFRMVHSTGPANAQYLSNLVFERREN 1489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
89-1343 |
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: 687.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 89 NPRARSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKNDGRSPSLVRALLRVFGWQLG 168
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLNALRRCFFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 169 FPGLAIFVVELGlRTLQPIFLVKLISYFsgepDAANA-----GFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMG 243
Cdd:TIGR01271 84 FYGILLYFGEAT-KAVQPLLLGRIIASY----DPFNApereiAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 244 SMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQ 323
Cdd:TIGR01271 159 SLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 324 MYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVA 403
Cdd:TIGR01271 239 ACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 404 IFLSLVGY-----VILGKVFTpeiafmiTAYYN-VLLAAMSIYVPSAIIQTAQFLTSIRRVEQFMQSEELGSSdksegps 477
Cdd:TIGR01271 319 VFLSVVPYalikgIILRRIFT-------TISYCiVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTL------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 478 kdtvpgnppsnnnEADLLKSAISIRDLKAKWD-------------------PNSPDY------------TLSGINLEIKP 526
Cdd:TIGR01271 385 -------------EYNLTTTEVEMVNVTASWDegigelfekikqnnkarkqPNGDDGlffsnfslyvtpVLKNISFKLEK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 527 GSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDF 606
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 607 DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFL 686
Cdd:TIGR01271 532 ALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHL 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 687 PHVDQIVILANGQIKALG----------DYESLL-------------KTGLIT------------GLGSLSKTDKAKTEE 731
Cdd:TIGR01271 612 KKADKILLLHEGVCYFYGtfselqakrpDFSSLLlgleafdnfsaerRNSILTetlrrvsidgdsTVFSGPETIKQSFKQ 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 732 QEP-----------LN-LNS----------------------------------PDNkNEVTPIKENSEQ---------- 755
Cdd:TIGR01271 692 PPPefaekrkqsiiLNpIASarkfsfvqmgpqkaqattiedavrepserkfslvPED-EQGEESLPRGNQyhhglqhqaq 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 756 ---------TVGGSSSGKEHVERQESGGISLA------------------------------------------------ 778
Cdd:TIGR01271 771 rrqsvlqlmTHSNRGENRREQLQTSFRKKSSItqqnelaseldiysrrlskdsvyeiseeineedlkecfaderenvfet 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 779 ----LYRKYFQAGGGLVAFLVMLSSSVLAQVAVTggdyFLTYWVKKESTAAGHGEMEDMESKSMDVYKYTLII------- 847
Cdd:TIGR01271 851 ttwnTYLRYITTNRNLVFVLIFCLVIFLAEVAAS----LLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIItptsayy 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 848 ILSVIMNLSSSFL---------LFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDV 918
Cdd:TIGR01271 927 IFYIYVGTADSVLalgffrglpLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF 1006
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 919 MQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVL 998
Cdd:TIGR01271 1007 IQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYF 1086
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 999 EKEFDSYQDAHSSAFFMYISTSQAFGYCMNCICVIYISIITLSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELE 1078
Cdd:TIGR01271 1087 ETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVD 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1079 NTMTAVERVVEYESIEPEGMLEAP-------------DDKKPPKTWPEQGEIIFKELNLRYTPNAKAenVLKSLSFVIQP 1145
Cdd:TIGR01271 1167 GLMRSVSRVFKFIDLPQEEPRPSGgggkyqlstvlviENPHAQKCWPSGGQMDVQGLTAKYTEAGRA--VLQDLSFSVEG 1244
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1146 REKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLW 1225
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIW 1324
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1226 GCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCT 1305
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404
|
1450 1460 1470
....*....|....*....|....*....|....*...
gi 442622995 1306 VLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKS 1343
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
155-1357 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 649.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 155 LVRALLRVFGWQLGFPGLAifvvelglrTLQPIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHV 234
Cdd:PTZ00243 238 LFAALPYYVWWQIPFKLLS---------DVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 235 CFK----MRVAMGSMIFRKALRLTKGALG--DTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGIS 308
Cdd:PTZ00243 309 SIRcglqYRSALNALIFEKCFTISSKSLAqpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 309 AVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYI 388
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 389 RGFDFARRIVLSRVAIFLSLVGYVILGKVFTPEIAFMITAYYNVLlaAMSIY-VPSAIIQTAQFLTSIRRVEQFMQSE-- 465
Cdd:PTZ00243 469 RVATSFVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVL--RMPFFmIPWVFTTVLQFLVSIKRISTFLECDna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 466 -------------------------------------------------------------ELGSSDKSEGP-------- 476
Cdd:PTZ00243 547 tcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklprapkvktsllsralrmlccEQCRPTKRHPSpsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 477 --------SKDTVPGNPPSNNNEADllksaISIRDLKAKWDPNS------PDYTLSGINLEIKPGSVVAVIGLTGSGKSS 542
Cdd:PTZ00243 627 dygspssaSRHIVEGGTGGGHEATP-----TSERSAKTPKMKTDdffelePKVLLRDVSVSVPRGKLTVVLGATGSGKST 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 543 LIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGA 622
Cdd:PTZ00243 702 LLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 623 TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKA 702
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 703 LGDYESLLKTGLITGLGSLSKTDKAKTE---EQEPLNLNSPD------NKNEVTPIK--ENSEQTVGGSSSGK-EHVERQ 770
Cdd:PTZ00243 862 SGSSADFMRTSLYATLAAELKENKDSKEgdaDAEVAEVDAAPggavdhEPPVAKQEGnaEGGDGAALDAAAGRlMTREEK 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 771 ESGGISLALYRKYFQA-GGGLVAFLVMLSSSVLAQVAVTGGdYFLTYWVKKESTaaghgemedmESKSMDVYKYTLIIIL 849
Cdd:PTZ00243 942 ASGSVPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSG-VWLSMWSTRSFK----------LSAATYLYVYLGIVLL 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 850 SVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGII 929
Cdd:PTZ00243 1011 GTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSI 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 930 IVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAH 1009
Cdd:PTZ00243 1091 LVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVV 1170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1010 SSAFFMYISTSQAFGY---CMNCICVIYISIITLSFfAFPPGNGADVGLV---ITQAMGLIDMVQWGVRQTAELENTMTA 1083
Cdd:PTZ00243 1171 YSCSYLENVANRWLGVrveFLSNIVVTVIALIGVIG-TMLRATSQEIGLVslsLTMAMQTTATLNWLVRQVATVEADMNS 1249
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1084 VERVVEY-ESIEPEGMLE-------------APDDK---------KPPKTWP---EQGEIIFKELNLRYTPNAKAenVLK 1137
Cdd:PTZ00243 1250 VERLLYYtDEVPHEDMPEldeevdalerrtgMAADVtgtvviepaSPTSAAPhpvQAGSLVFEGVQMRYREGLPL--VLR 1327
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1138 SLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYT-DGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPF 1216
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPF 1407
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1217 DEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAIL-RENRILVMDEATANVDPQTDGLIQA 1295
Cdd:PTZ00243 1408 LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQA 1487
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1296 TIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDSKvFHNLVNQSGR 1357
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSI-FHSMVEALGR 1548
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1115-1336 |
4.31e-131 |
|
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: 402.64 E-value: 4.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYTPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:cd03244 1 GDIEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVElSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILREN 1273
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1274 RILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSP 1336
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
845-1343 |
5.78e-112 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 364.87 E-value: 5.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDS 1004
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1005 YQDAHSSAFFMYISTSQAFGYCMNCICVIyISIITLSFFAFPPGNGA----DVGLVITQAMGLIDMVQWGVRQTAELENT 1080
Cdd:COG1132 229 ANEELRRANLRAARLSALFFPLMELLGNL-GLALVLLVGGLLVLSGSltvgDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1081 MTAVERVVEYESIEPEgMLEAPDDKKPPktwPEQGEIIFKELNLRYTPNakaENVLKSLSFVIQPREKVGIVGRTGAGKS 1160
Cdd:COG1132 308 LASAERIFELLDEPPE-IPDPPGAVPLP---PVRGEIEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1161 SLINALFRLsY--TDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKE 1235
Cdd:COG1132 381 TLVNLLLRF-YdpTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1236 VVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHT 1315
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
490 500
....*....|....*....|....*...
gi 442622995 1316 IIDSDKVMVMDAGRVVEFGSPYELMTKS 1343
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
499-699 |
1.01e-111 |
|
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: 349.46 E-value: 1.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNS--PDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSG 576
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDA 656
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442622995 657 SVARHLFDQCVRGHLR-GSTVVLVTHQEQFLPHVDQIVILANGQ 699
Cdd:cd03250 161 HVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1111-1336 |
1.07e-95 |
|
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: 305.88 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1111 WPEQGEIIFKELNLRYTPNAkaENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS-YTDGSVLIDTRDTRQMGLH 1189
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDL--PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1190 DLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLeevklkevvsdlpdglasKISEGGTNFSVGQRQLVCLARAI 1269
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1270 LRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSP 1336
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
845-1354 |
8.26e-94 |
|
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: 318.70 E-value: 8.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFtKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:COG2274 204 LALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLF 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDS 1004
Cdd:COG2274 283 VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1005 YQD---------AHSSAFFMYISTS-QAFGYcmncICVIYISI-------ITL-SFFAFppgNGAdVGLVITQAMGLIDM 1066
Cdd:COG2274 363 LLAkylnarfklRRLSNLLSTLSGLlQQLAT----VALLWLGAylvidgqLTLgQLIAF---NIL-SGRFLAPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1067 VQwgvrqtaELENTMTAVERVVEYESIEPEgmleAPDDKKPPKTWPEQGEIIFKELNLRYTPNAKaeNVLKSLSFVIQPR 1146
Cdd:COG2274 435 LQ-------RFQDAKIALERLDDILDLPPE----REEGRSKLSLPRLKGDIELENVSFRYPGDSP--PVLDNISLTIKPG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1147 EKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL---DPfdEYSD 1221
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGL-YepTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATD 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1222 EKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKF 1301
Cdd:COG2274 579 EEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1302 RDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKsdSKVFHNLVNQ 1354
Cdd:COG2274 659 KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR--KGLYAELVQQ 709
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
789-1090 |
2.04e-93 |
|
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: 303.86 E-value: 2.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 789 GLVAFLVMLSSSVLAQVAVTGGDYFLTYWVKKESTAAGHGEMEDMESKS-MD---------VYKYTLIIILSVIMNLSSS 858
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTnVDiedldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 859 FLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPL 938
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 939 LLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYIS 1018
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1019 TSQAFGYCMNCICVIYISIITL-SFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFgSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
171-458 |
2.56e-93 |
|
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: 302.48 E-value: 2.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 171 GLAIFVVELGLRTLQPIFLVKLISYFSGEPDA-ANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRK 249
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 250 ALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYLGTR 329
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 330 TSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVAIFLSLV 409
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442622995 410 GYVILGKVFTPEIAFMITAYYNvLLAAMSIYVPSAIIQTAQFLTSIRRV 458
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFN-LLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
793-1090 |
3.36e-92 |
|
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: 299.80 E-value: 3.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWVKKESTAAGHGEmedmeSKSMDVYkYTLIIILSVIMNLSSSFLLFNIAKKASIRL 872
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSS-----GYYLGVY-AALLVLASVLLVLLRWLLFVLAGLRASRRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 873 HNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYH 952
Cdd:cd18580 75 HDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 953 LRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCICV 1032
Cdd:cd18580 155 LQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1033 IYISIITLSFFAFPPG-NGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18580 235 LLALVVALLAVLLRSSiSAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
169-458 |
1.46e-86 |
|
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: 283.73 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 169 FPGLAIFVVELgLRTLQPIFLVKLISYFSG--EPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMI 246
Cdd:cd18593 1 LLGIFLFLEEA-IRVVQPIFLGKLIRYFEGngSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 247 FRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYL 326
Cdd:cd18593 80 YRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 327 GTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVAIFL 406
Cdd:cd18593 160 GKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 407 SLVGYVILGKVFTPEIAFMITAYYNVLLAAMSIYVPSAIIQTAQFLTSIRRV 458
Cdd:cd18593 240 TFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
910-1342 |
2.46e-75 |
|
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: 261.62 E-value: 2.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 910 VLPVVLVDVMQIALWLAGIIIVIAnvnpLLLVPTLMLsvifyhlrnLYLKTSRDL--KRVEAINR-SpvySHLAASLNGL 986
Cdd:COG4988 144 LVPLLILVAVFPLDWLSGLILLVT----APLIPLFMI---------LVGKGAAKAsrRQWRALARlS---GHFLDRLRGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 987 TTIRALDA----QRVLEKEFDSYQDAH---------SSA---FFMYISTsqafgycmnCICVIYISI----ITLSFFAfp 1046
Cdd:COG4988 208 TTLKLFGRakaeAERIAEASEDFRKRTmkvlrvaflSSAvleFFASLSI---------ALVAVYIGFrllgGSLTLFA-- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1047 pgngadvGLVItqamgLI----------DM-VQWGVRQTAelentMTAVERVVEyesiepegMLEAPDDKKPPKT----W 1111
Cdd:COG4988 277 -------ALFV-----LLlapefflplrDLgSFYHARANG-----IAAAEKIFA--------LLDAPEPAAPAGTaplpA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1112 PEQGEIIFKELNLRYtpnAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHD 1190
Cdd:COG4988 332 AGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILINGVDLSDLDPAS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLAR 1267
Cdd:COG4988 409 WRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALAR 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1268 AILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
166-459 |
1.58e-74 |
|
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: 249.86 E-value: 1.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 166 QLGFPGLaifvVELGLRTLQPIFLVKLISYFSGEPDAANA-GFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGS 244
Cdd:cd18594 1 LLGILLF----LEESLKIVQPLLLGRLVAYFVPDSTVTKTeAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 245 MIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQM 324
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 325 YLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVAI 404
Cdd:cd18594 157 YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 405 FLSLVGYVILGKVFTPEIAFMITAYYNVLLAAMSIYVPSAIIQTAQFLTSIRRVE 459
Cdd:cd18594 237 FATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1115-1352 |
1.39e-72 |
|
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: 242.89 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:cd03288 18 GEIKIHDLCVRYENNLKP--VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILREN 1273
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1274 RILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDSkVFHNLV 1352
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDG-VFASLV 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1115-1342 |
6.43e-72 |
|
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: 239.82 E-value: 6.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYTPNakaENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLR 1192
Cdd:cd03254 1 GEIEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-YdpQKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLW-GCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILR 1271
Cdd:cd03254 77 SMIGVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1272 ENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
151-713 |
1.62e-66 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 236.60 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 151 RSPSLVRALLRVFG---WQLGFpGLAIFVVELGLRTLQPIFLVKLISYFSGEPDAANAgFYYAVAQIVISALTVMILTPT 227
Cdd:COG1132 4 SPRKLLRRLLRYLRpyrGLLIL-ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSAL-LLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 228 TFGIHHVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSA-PYTVHYLWVGPLQVLVITYLMyqeIG 306
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFlAHGLPQLVRSVVTLIGALVVL---FV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 307 ISAVFGvLFMLLFMPI----QMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTI 382
Cdd:COG1132 159 IDWRLA-LIVLLVLPLlllvLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 383 RQGQYIRGFDFARRIVLSRVAIFLSLV--GYVILGKVFTPEIAFMITAYYNVLLAAMSIYVpSAIIQTAQFLTSIRRVEQ 460
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLvgGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA-NVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 461 FMQSEElgssDKSEGPSKDTVPGnppsnnneadlLKSAISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGK 540
Cdd:COG1132 317 LLDEPP----EIPDPPGAVPLPP-----------VRGEIEFENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 541 SSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNILFGQP-MDSQRYEEVVKKCALERDF 606
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 607 DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFdQCVRGHLRGSTVVLVTHQEQFL 686
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ-EALERLMKGRTTIVIAHRLSTI 538
|
570 580
....*....|....*....|....*..
gi 442622995 687 PHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
793-1090 |
3.19e-66 |
|
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: 226.19 E-value: 3.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWvkkeSTAAGHGEMEDMESKSMDVY--KYTLIIILSVIMNLSSSFLLFNIAKKASI 870
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW----ASAYETSSALPPSEVSVLYYlgIYALISLLSVLLGTLRYLLFFFGSLRASR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 871 RLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIF 950
Cdd:cd18604 77 KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 951 YHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCI 1030
Cdd:cd18604 157 VYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1031 CVIYISIITLSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18604 237 GALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
232-712 |
8.16e-63 |
|
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: 225.42 E-value: 8.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 232 HHVCFK----MRVAmgsmIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSApytvhYL-WVGPLQVLVITYL------ 300
Cdd:COG4987 80 HDATLRlladLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL-----YLrVLLPLLVALLVILaavafl 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 301 --MYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAeRTDNRIRMVnEIISAIQVLKMY-AWEQPFEQMvtHAREK 377
Cdd:COG4987 151 afFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAA-RAALRARLT-DLLQGAAELAAYgALDRALARL--DAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 378 EMNTIRQGQyirgfdfARRIVLSR-----------VAIFLSLVGYVILGKVFTPEIAFmitayynVLLAAMSIY-----V 441
Cdd:COG4987 227 RLAAAQRRL-------ARLSALAQallqlaaglavVAVLWLAAPLVAAGALSGPLLAL-------LVLAALALFealapL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 442 PSAIIQTAQFLTSIRRVEQFMqseelgssdksEGPSKDTVPGNPPSNNNEADLlksaiSIRDLKAKWdPNSPDYTLSGIN 521
Cdd:COG4987 293 PAAAQHLGRVRAAARRLNELL-----------DAPPAVTEPAEPAPAPGGPSL-----ELEDVSFRY-PGAGRPVLDGLS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 522 LEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNILFGQPM 588
Cdd:COG4987 356 LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 589 -DSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQcV 667
Cdd:COG4987 436 aTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-L 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 442622995 668 RGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKT 712
Cdd:COG4987 515 LEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
793-1090 |
2.18e-61 |
|
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: 212.34 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWvkkeSTAAGHGEMEDMESKSMDVYKYTLIIILSVIMNLSSSFLLFNIAKKASIRL 872
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEW----SDDPALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 873 HNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYH 952
Cdd:cd18603 77 HNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 953 LRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTS-------QAFGY 1025
Cdd:cd18603 157 IQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNrwlavrlEFLGN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1026 CMNCICVIYISIITLSffafppGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18603 237 LIVLFAALFAVLSRDS------LSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1117-1342 |
4.76e-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: 4.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLRRQ 1194
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF-YdvSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSGTMRYNLdpfdEY-----SDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAI 1269
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1270 LRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1117-1329 |
1.76e-59 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 201.84 E-value: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSGTMRYNLdpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnFSVGQRQLVCLARAILRENRI 1275
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1276 LVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGR 1329
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
793-1090 |
3.07e-59 |
|
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: 205.79 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWVkkestaaghgemEDMESKSMDVYK--YTLIIILSVIMNLSSSFLLFNIAKKASI 870
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWT------------EDFFGLSQGFYIgiYAGLGVLQAIFLFLFGLLLAYLGIRASK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 871 RLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIF 950
Cdd:cd18606 69 RLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 951 YHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCI 1030
Cdd:cd18606 149 YFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1031 CVIYISIITL--SFFAFPPgNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18606 229 GSLLVLIVALlcVTRRFSI-SPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
181-457 |
5.54e-59 |
|
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: 205.01 E-value: 5.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 181 LRTLQPIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRLTKGALGD 260
Cdd:cd18595 12 LLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLSNSARKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 261 TTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAER 340
Cdd:cd18595 92 STVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 341 TDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFdfarRIVLSRVAIFL-SLV---GYVILG- 415
Cdd:cd18595 172 KDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAV----SSFLWTCAPFLvSLAtfaTYVLSDp 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442622995 416 -KVFTPEIAFMITAYYNVLLAAMSIyVPSAIIQTAQFLTSIRR 457
Cdd:cd18595 248 dNVLDAEKAFVSLSLFNILRFPLSM-LPMVISNLVQASVSLKR 289
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
793-1090 |
5.30e-58 |
|
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: 202.83 E-value: 5.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWVKKESTAAGHGEMEDMESKSMDVYK-----YTLIIILSVIMNLSSSFLLFNIAKK 867
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSyyisvYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 868 ASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLS 947
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 948 VIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCM 1027
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1028 NCI--CVIYISIITLSFFAFPPG-NGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18602 241 DYLgaVIVFLAALSSLTAALAGYiSPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1115-1357 |
2.03e-57 |
|
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: 200.08 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTRDTRQMGLHDLRRQ 1194
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENR 1274
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1275 ILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMtkSDSKVFHNLVNQ 1354
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL--NEKSHFKQAISP 236
|
...
gi 442622995 1355 SGR 1357
Cdd:cd03289 237 SDR 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
233-711 |
2.30e-57 |
|
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: 212.39 E-value: 2.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 233 HVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLIsNDIPRL-DSAPYTVHYLWVGPLQVLVITYLMYQeigISAVF 311
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTALLDLLFVLIFLIVLFF---YSPPL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 312 gVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVN----EIISAIQVLKMYA--------WEQPFEQMVTHAREKEM 379
Cdd:COG2274 298 -ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQsllvETLRGIETIKALGaesrfrrrWENLLAKYLNARFKLRR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 380 NTIRQGQYIRGFdfarrIVLSRVAIFLsLVGYVILGKVFTPE--IAFMItayynvllaaMSIYVPSAIIQTAQFL----- 452
Cdd:COG2274 377 LSNLLSTLSGLL-----QQLATVALLW-LGAYLVIDGQLTLGqlIAFNI----------LSGRFLAPVAQLIGLLqrfqd 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 453 --TSIRRVEQFMQSEelgsSDKSEGPSKDTVPGnppsnnneadlLKSAISIRDLKAKWDPNSPdYTLSGINLEIKPGSVV 530
Cdd:COG2274 441 akIALERLDDILDLP----PEREEGRSKLSLPR-----------LKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERV 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 531 AVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNILFGQP-MDSQRYEEV 596
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPdATDEEIIEA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 VKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQcVRGHLRGSTV 676
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTV 663
|
490 500 510
....*....|....*....|....*....|....*
gi 442622995 677 VLVTHQEQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
789-1090 |
2.62e-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: 201.25 E-value: 2.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 789 GLVAFLVMLSSSVLAQVAVTGGDYFLTYWVKK---------ESTAAGHGEMEDMESKSMDVYKYTLIIILSVIMNLSSSF 859
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQgsgnttnnvDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 860 LLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLL 939
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 940 LVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYIST 1019
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1020 SQAFGYCMNCICVIYISIITLSFFAF----PPgngADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLkgsiSP---AFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
845-1340 |
7.23e-57 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 208.03 E-value: 7.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVN-PLLLVPTLMLSVIFYHLRnlylktsRDLKRVEAINRspvysHLAASLNGLTTI--RALDAQRVLeKE 1001
Cdd:TIGR02203 142 VIGLFIVLLYYSwQLTLIVVVMLPVLSILMR-------RVSKRLRRISK-----EIQNSMGQVTTVaeETLQGYRVV-KL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1002 FDSYQ------DAHSSA---FFMYISTSQAFGYCMNCICvIYISIITLSFFA-FPPGNGA----DVGLVITQAMGLIDmv 1067
Cdd:TIGR02203 209 FGGQAyetrrfDAVSNRnrrLAMKMTSAGSISSPITQLI-ASLALAVVLFIAlFQAQAGSltagDFTAFITAMIALIR-- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1068 qwGVRQTAELENTM----TAVERVVEYESIEPEgmleaPDDKKPPKTWPEqGEIIFKELNLRYTPNAKAenVLKSLSFVI 1143
Cdd:TIGR02203 286 --PLKSLTNVNAPMqrglAAAESLFTLLDSPPE-----KDTGTRAIERAR-GDVEFRNVTFRYPGRDRP--ALDSISLVI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1144 QPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL---DPfDEY 1219
Cdd:TIGR02203 356 EPGETVALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1220 SDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS 1299
Cdd:TIGR02203 435 DRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALER 514
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 442622995 1300 KFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:TIGR02203 515 LMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1117-1354 |
1.07e-56 |
|
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: 196.61 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLRRQ 1194
Cdd:cd03249 1 IEFKNVSFRY-PSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YdpTSGEILLDGVDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSGTMRYNLdpfdEYSDEKlwGCLEEVK-------LKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLAR 1267
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENI----RYGKPD--ATDEEVEeaakkanIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1268 AILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDskV 1347
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG--V 230
|
....*..
gi 442622995 1348 FHNLVNQ 1354
Cdd:cd03249 231 YAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1117-1340 |
1.22e-55 |
|
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: 193.22 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:cd03251 1 VEFKNVTFRYPG--DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRE 1272
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1273 NRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
246-713 |
4.39e-54 |
|
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: 199.21 E-value: 4.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 246 IFRKALRLTKGALGDTTSGHVVNLISNDIPRLDsaPYTVHYLwvgPLQVLVIT-------YLMYQEIgISAVFgVLFMLL 318
Cdd:COG4988 97 LLEKLLALGPAWLRGKSTGELATLLTEGVEALD--GYFARYL---PQLFLAALvpllilvAVFPLDW-LSGLI-LLVTAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 319 FMPIQMYLgtrtsaIQLKAAERTDNRIRMVN-------EIISAIQVLKMYaweqpfeqmvtHAREKEMNTIRQgqyiRGF 391
Cdd:COG4988 170 LIPLFMIL------VGKGAAKASRRQWRALArlsghflDRLRGLTTLKLF-----------GRAKAEAERIAE----ASE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 392 DFaRRI---VLsRVAiFLS-----------------LVGYVILGKVFTPEIAFMitayynVLLAAMSIYVPsaIIQTAQF 451
Cdd:COG4988 229 DF-RKRtmkVL-RVA-FLSsavleffaslsialvavYIGFRLLGGSLTLFAALF------VLLLAPEFFLP--LRDLGSF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 452 -------LTSIRRVEQFMQSEElgssdKSEGPSKDTVPGNPPSnnneadllksAISIRDLKAKWDPNSPdyTLSGINLEI 524
Cdd:COG4988 298 yharangIAAAEKIFALLDAPE-----PAAPAGTAPLPAAGPP----------SIELEDVSFSYPGGRP--ALDGLSLTI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 525 KPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNILFGQP-MDS 590
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 591 QRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQcVRGH 670
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRL 519
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 442622995 671 LRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:COG4988 520 AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1114-1342 |
1.06e-53 |
|
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: 199.28 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1114 QGEIIFKELNLRYTPNAKaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDL 1191
Cdd:COG5265 355 GGEVRFENVSFGYDPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF-YdvTSGRILIDGQDIRDVTQASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 RRQISIIPQEPVLFSGTMRYNLdpfdEY-----SDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLA 1266
Cdd:COG5265 431 RAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
517-709 |
1.95e-53 |
|
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: 188.91 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEV 596
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 VKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTV 676
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190
....*....|....*....|....*....|...
gi 442622995 677 VLVTHQEQFLPHVDQIVILANGQIKALGDYESL 709
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
508-698 |
1.21e-52 |
|
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: 184.07 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 508 WDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVN-----------------GSLSYTSQE 570
Cdd:cd03290 10 WGSGLA--TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 571 SWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDP 650
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 651 LSAVDASVARHLFDQCVRGHLRGS--TVVLVTHQEQFLPHVDQIVILANG 698
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
170-458 |
3.99e-52 |
|
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: 185.35 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 170 PGLAIFVVELGLRTLQPIFLVKLI-----SYFSGEPDAANAGFYYAVAqivisaLTVMILTpTTFGIHH-------VCFK 237
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLInfvedAYLGGPPPSIGYGIGYAIG------LFLLQLL-SSLLLNHffyrsmlTGAQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 238 MRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFML 317
Cdd:cd18597 74 VRAALTKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 318 LFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRI 397
Cdd:cd18597 154 LSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 398 VLSRVAIFLSLVGYVILGKVFTPEIAFMITAYYNVLLAAMSiYVPSAIIQTAQFLTSIRRV 458
Cdd:cd18597 234 SLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
847-1344 |
4.09e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 193.79 E-value: 4.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 847 IILSVIMNLSSSFL------LFNIA-KKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVM 919
Cdd:TIGR00958 204 IFFMCLLSIASSVSaglrggSFNYTmARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 920 QIALWLAGIIIVIANVNP------LLLVPTLMLSVIFYHLRnlYLKTSRDLKrvEAINRSpvySHLA-ASLNGLTTIRAL 992
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrltmvtLINLPLVFLAEKVFGKR--YQLLSEELQ--EAVAKA---NQVAeEALSGMRTVRSF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 993 DAQrvlEKEFDSYQDAHSSAFfmYISTSQAFGYcmncicVIYISIITLSffafppGNGADVG-------LVITQAM---G 1062
Cdd:TIGR00958 357 AAE---EGEASRFKEALEETL--QLNKRKALAY------AGYLWTTSVL------GMLIQVLvlyyggqLVLTGKVssgN 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1063 LIDMV----QWG--VRQTAELENTMT----AVERVVEY----ESIEPEGMLeAPDdkkppktwPEQGEIIFKELNLRYtP 1128
Cdd:TIGR00958 420 LVSFLlyqeQLGeaVRVLSYVYSGMMqavgASEKVFEYldrkPNIPLTGTL-APL--------NLEGLIEFQDVSFSY-P 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1129 NAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFS 1206
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL-YqpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFS 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1207 GTMRYNLD-PFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANV 1285
Cdd:TIGR00958 569 GSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1286 DPQTDGLIQATirSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:TIGR00958 649 DAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
793-1090 |
8.33e-51 |
|
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: 181.96 E-value: 8.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWVKKESTAAGHGEMEDMESKSMdvyKYTLIIILSVIMNLSSSFLLFNIAKKASIRL 872
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFFLT---VYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 873 HNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYH 952
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 953 LRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTS-------QAFGY 1025
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASqwlsirlQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1026 CMNCICVIYISIITLSFFAFPPGNgadVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEY 1090
Cdd:cd18605 238 LIVTFVALTAVVQHFFGLSIDAGL---IGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1115-1331 |
2.18e-50 |
|
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: 177.78 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYtPNAKAEnVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHDLR 1192
Cdd:cd03245 1 GRIEFRNVSFSY-PNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL-YkpTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSGTMRYNLDPFDEY-SDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILR 1271
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1272 ENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVV 1331
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
910-1325 |
6.24e-50 |
|
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: 186.34 E-value: 6.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 910 VLPVVLVDVMQIALWLAGIIIVIAnvnpLLLVPTLMLSVifyhlrnLYLKTSRDLKRVEAINRspVYSHLAASLNGLTTI 989
Cdd:TIGR02857 130 IVPLAILAAVFPQDWISGLILLLT----APLIPIFMILI-------GWAAQAAARKQWAALSR--LSGHFLDRLRGLPTL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 990 RALDAQRVLEKEFDSYQDAHSSAffmyistsqafgyCMNCICVIYISIITLSFFAfppgnGADVGLV------------I 1057
Cdd:TIGR02857 197 KLFGRAKAQAAAIRRSSEEYRER-------------TMRVLRIAFLSSAVLELFA-----TLSVALVavyigfrllagdL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1058 TQAMGLIDMV----------QWGVRQTAELENtMTAVERVVEYESIEPegmleAPDDKKPPKTWPEQGEIIFKELNLRYt 1127
Cdd:TIGR02857 259 DLATGLFVLLlapefylplrQLGAQYHARADG-VAAAEALFAVLDAAP-----RPLAGKAPVTAAPASSLEFSGVSVAY- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1128 pnAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFS 1206
Cdd:TIGR02857 332 --PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1207 GTMRYNL---DPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:TIGR02857 410 GTIAENIrlaRP--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 442622995 1284 NVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVM 1325
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
186-433 |
8.09e-47 |
|
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: 170.04 E-value: 8.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 186 PIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRLTKGALGDTTSGH 265
Cdd:cd18598 17 PLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKALRVRSSSLSKFSTGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 266 VVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRI 345
Cdd:cd18598 97 IVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 346 RMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGF-DF---ARRIVLSrvaiFLSLVGYVILGKVFTPE 421
Cdd:cd18598 177 KLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALcVYfwaTTPVLIS----ILTFATYVLMGNTLTAA 252
|
250
....*....|..
gi 442622995 422 IAFMITAYYNVL 433
Cdd:cd18598 253 KVFTSLALFNML 264
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1073-1342 |
1.93e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.22 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1073 QTAELENTMTAVERVVEyesiepegMLEAPDDKKPPKTWP-EQGEIIFKELNLRYTPNakaENVLKSLSFVIQPREKVGI 1151
Cdd:PRK10790 304 QQSMLQQAVVAGERVFE--------LMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVAL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1152 VGRTGAGKSSLINALfrLSY---TDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCL 1228
Cdd:PRK10790 373 VGHTGSGKSTLASLL--MGYyplTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1229 EEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLT 1308
Cdd:PRK10790 451 ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV 530
|
250 260 270
....*....|....*....|....*....|....
gi 442622995 1309 IAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK10790 531 IAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1116-1354 |
1.43e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 171.57 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1116 EIIFKELNLrYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINAL--FrLSYTdGSVLIDTRDTRQMGLHDLRR 1193
Cdd:PRK11174 349 TIEAEDLEI-LSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgF-LPYQ-GSLKINGIELRELDPESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAIL 1270
Cdd:PRK11174 424 HLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1271 RENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMtkSDSKVFHN 1350
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS--QAGGLFAT 579
|
....
gi 442622995 1351 LVNQ 1354
Cdd:PRK11174 580 LLAH 583
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1117-1342 |
1.58e-44 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 161.50 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:cd03252 1 ITFEHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVpENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSGTMRYNLDPFDEYSD-EKLwgcLEEVKLK---EVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILR 1271
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSmERV---IEAAKLAgahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1272 ENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1057-1342 |
2.80e-44 |
|
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: 172.82 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1057 ITQAMGLIDMVQwgvrqtaELENTMTAVERVVEYEsIEPEGMLEAPDDKKPPKTWPEQGEIifkEL-NLRYTPNAKAENV 1135
Cdd:TIGR03796 426 VNNLVGFGGTLQ-------ELEGDLNRLDDVLRNP-VDPLLEEPEGSAATSEPPRRLSGYV---ELrNITFGYSPLEPPL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRLSytDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYN 1212
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTiakLVAGLYQPW--SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDN 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 LDPFDE-YSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDG 1291
Cdd:TIGR03796 573 LTLWDPtIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1292 LIQATIRSkfRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:TIGR03796 653 IIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV 701
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
499-699 |
2.71e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 152.54 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03228 1 IEFKNVSFSY-PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNIlfgqpmdsqryeevvkkcalerdfdllplrdntivgergatLSGGQKARISLARSVYRKASIY 645
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 646 LLDDPLSAVDAsVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQ 699
Cdd:cd03228 119 ILDEATSALDP-ETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
184-458 |
6.32e-42 |
|
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: 156.50 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 184 LQPIFLVKLISYF-SGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRL--------- 253
Cdd:cd18596 15 APPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 254 ----------TKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQ 323
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 324 MYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIrgfDFARRIVLSRVA 403
Cdd:cd18596 175 GYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL---DLLLSLLWFLIP 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 404 IFLSLVGY----VILGKVFTPEIAFMITAYYNVLLAAMSIyVPSAIIQTAQFLTSIRRV 458
Cdd:cd18596 252 ILVTVVTFatytLVMGQELTASVAFTSLALFNMLRGPLNV-LPELITQLLQAKVSLDRI 309
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
510-704 |
7.73e-42 |
|
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: 153.13 E-value: 7.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSG 576
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQPM-DSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442622995 656 ASVARHLFDQcVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03245 173 MNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
186-458 |
8.29e-42 |
|
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: 155.41 E-value: 8.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 186 PIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRLtkGALGDTTSGH 265
Cdd:cd18592 18 TILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRL--RSLGDKSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 266 VVNLISNDIPRL-DSAPYTVhYLWVGPLQ-VLVITYLMYqEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDN 343
Cdd:cd18592 96 LINIFSNDGQRLfDAAVFGP-LVIGGPVVlILGIVYSTY-LLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 344 RIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVAIFLSLVGYVILGKVFTPEIA 423
Cdd:cd18592 174 RVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAAQA 253
|
250 260 270
....*....|....*....|....*....|....*
gi 442622995 424 FMITAYYNVLLAAMSIyVPSAIIQTAQFLTSIRRV 458
Cdd:cd18592 254 FTVIAVFNSMRFSLRM-LPYAVKALAEAKVALQRI 287
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
845-1340 |
6.76e-41 |
|
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: 162.22 E-value: 6.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:TIGR01193 204 IAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWIL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LA-GIIIVIANVNPLL--LVPTLMLSVIFYHLRNLYLKTSRDLKRVEAInrspVYSHLAASLNGLTTIRALDAQRV---- 997
Cdd:TIGR01193 284 VIvGLFLVRQNMLLFLlsLLSIPVYAVIIILFKRTFNKLNHDAMQANAV----LNSSIIEDLNGIETIKSLTSEAErysk 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 998 LEKEFDSYqdAHSSafFMYISTSQAFGYCMNCICVIyISIITLSFFAFppgngadvgLVITQAMGLIDMVQWGVRQ---T 1074
Cdd:TIGR01193 360 IDSEFGDY--LNKS--FKYQKADQGQQAIKAVTKLI-LNVVILWTGAY---------LVMRGKLTLGQLITFNALLsyfL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1075 AELENTMTAVERV----VEYESIEPEGMLEAPDDKKPPKTWPEQ--GEIIFKELNLRYTPNAkaeNVLKSLSFVIQPREK 1148
Cdd:TIGR01193 426 TPLENIINLQPKLqaarVANNRLNEVYLVDSEFINKKKRTELNNlnGDIVINDVSYSYGYGS---NILSDISLTIKMNSK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1149 VGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL--DPFDEYSDEKLW 1225
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFfQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIW 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1226 GCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIrSKFRDCT 1305
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKT 661
|
490 500 510
....*....|....*....|....*....|....*
gi 442622995 1306 VLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:TIGR01193 662 IIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1076-1352 |
6.97e-41 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 162.05 E-value: 6.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1076 ELENTMTAVERVV-EYESIEPegMLEAP----DDKKPPKtwPEQGEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVG 1150
Cdd:TIGR03797 410 QLSNTLISILAVIpLWERAKP--ILEALpevdEAKTDPG--KLSGAIEVDRVTFRYRPDGPL--ILDDVSLQIEPGEFVA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1151 IVGRTGAGKSSLinalFRL-----SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLW 1225
Cdd:TIGR03797 484 IVGPSGSGKSTL----LRLllgfeTPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAW 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1226 GCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIrSKFRdCT 1305
Cdd:TIGR03797 560 EAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERLK-VT 637
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 442622995 1306 VLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDskVFHNLV 1352
Cdd:TIGR03797 638 RIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG--LFAQLA 682
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
846-1342 |
4.46e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 157.87 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 846 IIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQ----- 920
Cdd:PRK11176 74 LMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegasi 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 921 IAL--------W-LAGIIIVIAnvnPLLLVPTLMLSVIFyhlRNLylktSRDLKRVeainrspvYSHLAAS----LNGLT 987
Cdd:PRK11176 154 IGLfimmfyysWqLSLILIVIA---PIVSIAIRVVSKRF---RNI----SKNMQNT--------MGQVTTSaeqmLKGHK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 988 TIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCI------CVIYISIITLSFFAFPPGNgadVGLVITQAM 1061
Cdd:PRK11176 216 EVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIaslalaFVLYAASFPSVMDTLTAGT---ITVVFSSMI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1062 GLIDMVQWGVRQTAELENTMTAVERVVEYESIEPE---GMLEAPddkkppktwPEQGEIIFKELNLRYTpnAKAENVLKS 1138
Cdd:PRK11176 293 ALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEkdeGKRVIE---------RAKGDIEFRNVTFTYP--GKEVPALRN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1139 LSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLD--P 1215
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDeGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1216 FDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQA 1295
Cdd:PRK11176 442 TEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 442622995 1296 TIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK11176 522 ALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
230-457 |
1.27e-39 |
|
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: 149.69 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 230 GIHhvcfkMRVAMGSMIFRKALRLTKGAL--GDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGI 307
Cdd:cd18591 84 GIR-----LKTALQAMIYEKALRLSSWNLssGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 308 SAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMntirqgQY 387
Cdd:cd18591 159 SALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL------KL 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 388 IRGFDFARRIV-----LSRVAI-FLSLVGYVIL-GKVFTPEIAFMITAYYNVLLAAMSIyVPSAIIQTAQFLTSIRR 457
Cdd:cd18591 233 LLKDAVYWSLMtfltqASPILVtLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFI-FPVVIPILINAVVSTRR 308
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
780-1090 |
2.90e-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: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 780 YRKYFQAGGGLVAFLVMLSSSVLAQVAVTGGDYFLtywVKKESTAAGHGEMEDMESKSMDVYKYT-LIIILSVIMNLSSS 858
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWL---LRSQADRVNTTRPESSSNTYAVIVTFTsSYYVFYIYVGVADS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 859 FLLFNIAK---------KASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGII 929
Cdd:cd18600 83 LLAMGFFRglplvhtliTVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 930 IVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAH 1009
Cdd:cd18600 163 TVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1010 SSAFFMYISTSQAFGYCMNCICVIYISIITLSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVE 1089
Cdd:cd18600 243 TANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFK 322
|
.
gi 442622995 1090 Y 1090
Cdd:cd18600 323 F 323
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1080-1342 |
1.37e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.44 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1080 TMTAVERVVEYESIEPEgmLEAPDDKKPPktwPEQGEIIFKELNLRYtPNAkAENVLKSLSFVIQPREKVGIVGRTGAGK 1159
Cdd:PRK11160 307 VIASARRINEITEQKPE--VTFPTTSTAA---ADQVSLTLNNVSFTY-PDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1160 SSLINALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKE 1235
Cdd:PRK11160 380 STLLQLLTRaWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1236 VVSDlPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHT 1315
Cdd:PRK11160 458 LLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTG 536
|
250 260
....*....|....*....|....*..
gi 442622995 1316 IIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK11160 537 LEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1114-1330 |
3.91e-38 |
|
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: 142.61 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1114 QGEIIFKELNLRYtPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLR 1192
Cdd:cd03248 9 KGIVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSGTMRYNLD-PFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILR 1271
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1272 ENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRV 1330
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1114-1357 |
4.16e-38 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 152.04 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1114 QGEIIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLR 1192
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSGTMRYNL-----DPfdeySDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLAR 1267
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1268 AILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSpyelmtksdskv 1347
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS------------ 552
|
250
....*....|
gi 442622995 1348 FHNLVNQSGR 1357
Cdd:PRK13657 553 FDELVARGGR 562
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
510-711 |
3.70e-37 |
|
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: 148.74 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSG 576
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNI-LFGQPmDSqryEEVVKKCALERDFDL---LPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:COG4618 421 TIAENIaRFGDA-DP---EKVVAAAKLAGVHEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 653 AVDASVARHLFdQCVRgHL--RGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:COG4618 497 NLDDEGEAALA-AAIR-ALkaRGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
482-713 |
8.64e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 8.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 482 PGNPPSNNNEADLLKSAISI--RDLKAkwdpNSPD-YTLSG-INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANsGQ 557
Cdd:PRK11174 331 PLAHPQQGEKELASNDPVTIeaEDLEI----LSPDgKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 558 LQVNG-------------SLSYTSQESWLFSGTVRQNILFGQP-MDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGAT 623
Cdd:PRK11174 406 LKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 624 LSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFdQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKAL 703
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
250
....*....|
gi 442622995 704 GDYESLLKTG 713
Cdd:PRK11174 565 GDYAELSQAG 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
862-1313 |
1.08e-36 |
|
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: 146.74 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 862 FNIAKKASIRLhntiFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVN-PLLL 940
Cdd:TIGR02868 82 LRSLGALRVRV----YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSvPAAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 941 VPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQ-----RVLEKEFDSYQDAHSSAFFM 1015
Cdd:TIGR02868 158 ILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALpaalaQVEEADRELTRAERRAAAAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1016 YISTS-QAFGYCMNCICVIYISI----------ITLSFFAFPPgngadvgLVITQAMG-LIDMVQwgvrqtaELENTMTA 1083
Cdd:TIGR02868 238 ALGAAlTLLAAGLAVLGALWAGGpavadgrlapVTLAVLVLLP-------LAAFEAFAaLPAAAQ-------QLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1084 VERVVEYESIEPEGML-EAPDDKKPPKTWPEqgeIIFKELNLRYTPNAKaenVLKSLSFVIQPREKVGIVGRTGAGKSSL 1162
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEgSAPAAGAVGLGKPT---LELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1163 INALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNL---DPfdEYSDEKLWGCLEEVKLKEVVS 1238
Cdd:TIGR02868 378 LATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1239 DLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRL 1313
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
499-704 |
1.10e-36 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 138.40 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNI-LFGQPMDSQRYeEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASI 644
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 645 YLLDDPLSAVDASVARHLFdQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03244 161 LVLDEATASVDPETDALIQ-KTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
499-711 |
2.14e-36 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 137.74 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03254 3 IEFENVNFSYDEKKP--VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNILFGQPMDSqryEEVVKKCALERDFDL----LPLRDNTIVGERGATLSGGQKARISLARSVYRK 641
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNAT---DEEVIEAAKEAGAHDfimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 642 ASIYLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:cd03254 158 PKILILDEATSNID-TETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
517-695 |
2.77e-36 |
|
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: 145.51 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNIL 583
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQP-MDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHL 662
Cdd:TIGR02857 418 LARPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180 190
....*....|....*....|....*....|...
gi 442622995 663 FDQcVRGHLRGSTVVLVTHQEQFLPHVDQIVIL 695
Cdd:TIGR02857 498 LEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
434-710 |
2.80e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 146.12 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 434 LAAMSIYVP--SAIIQTAQFLTSIRRVEQFMQSEELGSSDKSEGPSKDTVpgnppsnnneadllksAISIRDLKAKWdPN 511
Cdd:PRK11160 288 LAAFEALMPvaGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQV----------------SLTLNNVSFTY-PD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 512 SPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTV 578
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 RQNILFGQP-MDSQRYEEVVKKCALErdfDLL----PLrdNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PRK11160 431 RDNLLLAAPnASDEALIEVLQQVGLE---KLLeddkGL--NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 654 VDASVARHLFdQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PRK11160 506 LDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
218-683 |
8.25e-36 |
|
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: 144.04 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 218 ALTVMILTPTTFGI-------------HHVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSapYTV 284
Cdd:TIGR02868 51 YLSVAAVAVRAFGIgravfrylerlvgHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD--LYV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 285 HYLW-------VGPLQVLVITYLmYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAA-ERTDNRIRMVNEIISAIQ 356
Cdd:TIGR02868 129 RVIVpagvalvVGAAAVAAIAVL-SVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 357 VLKmyAWEQPFEQMVthAREKEMNTIRQGQyirgfdfARRIVLSRVAIFLSlVGYVILGKVFTPEIAFM--------ITA 428
Cdd:TIGR02868 208 ASG--ALPAALAQVE--EADRELTRAERRA-------AAATALGAALTLLA-AGLAVLGALWAGGPAVAdgrlapvtLAV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 429 YYNVLLAAMSIY--VPSAIIQTAQFLTSIRRVEQfMQSEELGSSDKSEGPSKDTVPGNPPsnnneadllksaISIRDLKA 506
Cdd:TIGR02868 276 LVLLPLAAFEAFaaLPAAAQQLTRVRAAAERIVE-VLDAAGPVAEGSAPAAGAVGLGKPT------------LELRDLSA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 507 KWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LSYTSQESWL 573
Cdd:TIGR02868 343 GYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 574 FSGTVRQNILFGQP-MDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:TIGR02868 421 FDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
490 500 510
....*....|....*....|....*....|.
gi 442622995 653 AVDASVARHLFDQCVRGhLRGSTVVLVTHQE 683
Cdd:TIGR02868 501 HLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1123-1330 |
2.42e-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: 132.73 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGLHDLRRQISIIPQE 1201
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 PVLFSGTMRYNLdpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:cd03246 85 DELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 1282 TANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIIDSDKVMVMDAGRV 1330
Cdd:cd03246 124 NSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1098-1334 |
5.62e-35 |
|
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: 142.19 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1098 MLEAPDDKKPPKTWPE-QGEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGS 1175
Cdd:COG4618 311 LLAAVPAEPERMPLPRpKGRLSVENLTVVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVwPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1176 VLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLwgcLEEVKL---KEVVSDLPDGLASKISEGG 1252
Cdd:COG4618 389 VRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKV---VAAAKLagvHEMILRLPDGYDTRIGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1253 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTD-GLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVV 1331
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEaALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
...
gi 442622995 1332 EFG 1334
Cdd:COG4618 546 AFG 548
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
499-713 |
7.08e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 133.51 E-value: 7.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03253 1 IEFENVTFAYDPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNILFGQPMDS-QRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASI 644
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATdEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 645 YLLDDPLSAVDASVARHLFdQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:cd03253 159 LLLDEATSALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
499-713 |
1.24e-34 |
|
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: 133.00 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03252 1 ITFEHVRFRYKPDGP-VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNILFGQP-MDSQRYEEVVKkCALERDFDL-LPLRDNTIVGERGATLSGGQKARISLARSVYRKAS 643
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPgMSMERVIEAAK-LAGAHDFISeLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 644 IYLLDDPLSAVDASvARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:cd03252 159 ILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
488-1344 |
1.87e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 144.40 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 488 NNNEADLLKS--AISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-- 563
Cdd:PTZ00265 370 NNDDGKKLKDikKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShn 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 564 ------------LSYTSQESWLFSGTVRQNILFG-------------------------------------------QPM 588
Cdd:PTZ00265 450 lkdinlkwwrskIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsNTT 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 589 DS-------QRYEEV-------VKKCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PTZ00265 530 DSneliemrKNYQTIkdsevvdVSKKVLIHDFvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 654 VDaSVARHLFDQCVrGHLRGS---TVVLVTHQEQFLPHVDQIVILANGQ------------------------------- 699
Cdd:PTZ00265 610 LD-NKSEYLVQKTI-NNLKGNenrITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnn 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 700 ----------------IKALGDYESLLKTG------LITGLGSLSKTDKAKTEEQEPLNLNS----------PDNKNEVT 747
Cdd:PTZ00265 688 nnnnnnnnkinnagsyIIEQGTHDALMKNKngiyytMINNQKVSSKKSSNNDNDKDSDMKSSaykdsergydPDEMNGNS 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 748 PIKENSEQTVGGSSSGKEHVERQESGGiSLALYRKYFQAGGGLVAFLVMLSSSVLA----------QVAVTGGDY--FLT 815
Cdd:PTZ00265 768 KHENESASNKKSCKMSDENASENNAGG-KLPFLRNLFKRKPKAPNNLRIVYREIFSykkdvtiialSILVAGGLYpvFAL 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 816 YWVKKESTaaghgeMEDMESKSMDVYKYTLIIILSVIMNLSSSFL--LFN--IAKKASIRLHNTIFNRVTRADMHFFSIN 891
Cdd:PTZ00265 847 LYAKYVST------LFDFANLEANSNKYSLYILVIAIAMFISETLknYYNnvIGEKVEKTMKRRLFENILYQEISFFDQD 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 892 KH-----GSILNRftkdmsqvdevlpvvlvDVMQIALWLAGIIIVIANVNPLLLVPTLMlsvIFYHlrnlylktsrdlkr 966
Cdd:PTZ00265 921 KHapgllSAHINR-----------------DVHLLKTGLVNNIVIFTHFIVLFLVSMVM---SFYF-------------- 966
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 967 veainrSPVyshLAASLNGLTTIR----ALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFG----------YCMNCICV 1032
Cdd:PTZ00265 967 ------CPI---VAAVLTGTYFIFmrvfAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKdpsfliqeafYNMNTVII 1037
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1033 IYISiitlSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAEL----------------------------------- 1077
Cdd:PTZ00265 1038 YGLE----DYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLfinsfaywfgsflirrgtilvddfmkslftflftg 1113
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1078 -------------ENTMTAVERVveYESIEPEGMLEAPDDK--KPPKTWPEQGEIIFKELNLRYT--PNAKaenVLKSLS 1140
Cdd:PTZ00265 1114 syagklmslkgdsENAKLSFEKY--YPLIIRKSNIDVRDNGgiRIKNKNDIKGKIEIMDVNFRYIsrPNVP---IYKDLT 1188
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1141 FVIQPREKVGIVGRTGAGKSSLINALFRL--------------------------------------------------- 1169
Cdd:PTZ00265 1189 FSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsge 1268
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1170 SYT----DGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLdpfdEYSDEKlwGCLEEVK-------LKEVVS 1238
Cdd:PTZ00265 1269 DSTvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI----KFGKED--ATREDVKrackfaaIDEFIE 1342
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1239 DLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQAT---IRSKfRDCTVLTIAHRLHT 1315
Cdd:PTZ00265 1343 SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDK-ADKTIITIAHRIAS 1421
|
1130 1140 1150
....*....|....*....|....*....|....
gi 442622995 1316 IIDSDKVMVMD----AGRVVEF-GSPYELMTKSD 1344
Cdd:PTZ00265 1422 IKRSDKIVVFNnpdrTGSFVQAhGTHEELLSVQD 1455
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
499-713 |
3.82e-34 |
|
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: 131.58 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNILFGQPMDSQryEEVVK--KCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKA 642
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATR--EEVEEaaRAANAHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 643 SIYLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:cd03251 158 PILILDEATSALD-TESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
510-713 |
3.68e-33 |
|
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: 128.81 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LSYTSQESWLFS 575
Cdd:cd03249 11 PSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNILFGQPMDSQRYEEVVKKCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKANIHDFiMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 655 DASVaRHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:cd03249 171 DAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1117-1344 |
9.66e-33 |
|
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: 127.45 E-value: 9.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSL---INALfrLSYTDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:COG1122 1 IELENLSFSYPGGTPA---LDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGL--LKPTSGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPV--LFSGT---------MRYNLDPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQL 1262
Cdd:COG1122 76 KVGLVFQNPDdqLFAPTveedvafgpENLGLPR--EEIRERVEEALELVGLEHLADRPPHEL-----------SGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1263 VCLARAILRENRILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELM 1340
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
....
gi 442622995 1341 TKSD 1344
Cdd:COG1122 223 SDYE 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
517-711 |
2.16e-32 |
|
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: 126.90 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------SLSYTSQESWLFSG-TVRQNIL 583
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 F---GQPMDSQRYEEVVKKcaLERDFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAsVAR 660
Cdd:COG4555 97 YfaeLYGLFDEELKKRIEE--LIELLGLEEFLD-----RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 661 HLFdqcvRGHLR-----GSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESLLK 711
Cdd:COG4555 169 RLL----REILRalkkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELRE 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
499-711 |
2.63e-31 |
|
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: 123.21 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------SLSYTSQ--- 569
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 ------ESWLFSGTVRQNILFG---QPMDSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYR 640
Cdd:COG1122 79 lvfqnpDDQLFAPTVEEDVAFGpenLGLPREEIRERVEE-ALEL-VGLEHLADRPP-----HELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 641 KASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
499-704 |
2.78e-31 |
|
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: 121.27 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS------------LSY 566
Cdd:cd03247 1 LSINNVSFSY-PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 567 TSQESWLFSGTVRQNIlfgqpmdsqryeevvkkcalerdfdllplrdntivgerGATLSGGQKARISLARSVYRKASIYL 646
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 647 LDDPLSAVDASVARHLFDQcVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03247 122 LDEPTVGLDPITERQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1136-1283 |
2.98e-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: 120.06 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSG-TMRYNL 1213
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1214 -------DPFDEYSDEKLWGCLEEVklkevvsDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
498-710 |
3.37e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.28 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKAKWDpNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------SLSYTSQ 569
Cdd:COG1121 6 AIELENLTVSYG-GRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 ES---WLF---------SGTVRQNILFGQPmdSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLARS 637
Cdd:COG1121 83 RAevdWDFpitvrdvvlMGRYGRRGLFRRP--SRADREAVDE-ALER-VGLEDLADRPI-----GELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 638 VYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTH-QEQFLPHVDQIVILANGQIkALGDYESLL 710
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFDRVLLLNRGLV-AHGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1123-1341 |
4.04e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.64 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL----SYTDGSVLIDTRDTRQMGLHDLRRQISII 1198
Cdd:COG1123 9 DLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGRRIGMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1199 PQEP------------VLFsgTMRYNLDPFDEYSDEKLWgCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLA 1266
Cdd:COG1123 89 FQDPmtqlnpvtvgdqIAE--ALENLGLSRAEARARVLE-LLEAVGLERRLDRYPHQL-----------SGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1117-1339 |
4.19e-31 |
|
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: 122.69 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSL---INALFRlsYTDGSVLIDTRDTRQM---GLHD 1190
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER--PTSGSVLVDGTDLTLLsgkELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEPVLFSG-TMRYNLD-PFdeysdeKLWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLA 1266
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENVAlPL------EIAG-VPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1119-1339 |
4.25e-31 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 122.29 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1119 FKELNLRYTPNAkaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY------TDGSVLIDTRD--TRQMGLHD 1190
Cdd:cd03260 3 LRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDGKDiyDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEPVLFSGTMRYNLdpfdEYSDeKLWGCLEEVKLKEVVSD------LPDGLASKIseGGTNFSVGQRQLVC 1264
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNV----AYGL-RLHGIKLKEELDERVEEalrkaaLWDEVKDRL--HALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1265 LARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1117-1329 |
4.27e-31 |
|
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: 121.81 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAEN-VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRdtrqmglhdlrrq 1194
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSGTMRYNL---DPFDEYsdeklwgcleevKLKEVVSD---------LPDGLASKISEGGTNFSVGQRQL 1262
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDEE------------RYEKVIKAcalepdleiLPDGDLTEIGEKGINLSGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1263 VCLARAILRENRILVMDEATANVDPQT-DGLIQATIRSKFRDC-TVLTIAHRLHTIIDSDKVMVMDAGR 1329
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
517-714 |
4.59e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.48 E-value: 4.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------SLSYTSQESWLFSG-TVRQNI- 582
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 ----LFGQPMDS--QRYEEVvkkcaLERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDA 656
Cdd:COG1131 96 ffarLYGLPRKEarERIDEL-----LEL-FGLTDAAD-----RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 657 sVARHLFDQCVRGHL-RGSTVVLVTHQeqfLPHV----DQIVILANGQIKALGDYESLLKTGL 714
Cdd:COG1131 165 -EARRELWELLRELAaEGKTVLLSTHY---LEEAerlcDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1119-1334 |
6.13e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 122.23 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1119 FKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDL---RRQ 1194
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlKPTSGSIIFDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPvlFSgtmryNLDP---------------FDEYSDEKLwgcLEEVKLKEVVSDLPDGLASK-ISEggtnFSVG 1258
Cdd:cd03257 84 IQMVFQDP--MS-----SLNPrmtigeqiaeplrihGKLSKKEAR---KEAVLLLLVGVGLPEEVLNRyPHE----LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1259 QRQLVCLARAILRENRILVMDEATANVDPqtdgLIQATI-------RSKFrDCTVLTIAHRLHTI-IDSDKVMVMDAGRV 1330
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDV----SVQAQIldllkklQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKI 224
|
....
gi 442622995 1331 VEFG 1334
Cdd:cd03257 225 VEEG 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
510-700 |
8.43e-31 |
|
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: 121.81 E-value: 8.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDY-TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LSYTSQESWLFS 575
Cdd:cd03248 22 PTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNILFGqpMDSQRYEEVVK--KCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:cd03248 102 RSLQDNIAYG--LQSCSFECVKEaaQKAHAHSFiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442622995 653 AVDASvARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:cd03248 180 ALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
517-652 |
1.08e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 118.52 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSG-TVRQNI 582
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 583 LFGQPMDSQRYEEvvKKCALERDFDLLPLRD--NTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:pfam00005 81 RLGLLLKGLSKRE--KDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1117-1334 |
2.35e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 118.57 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGlHDLRRQI 1195
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSGTMRYNLdpfdeysdeklwgcleevklkevvsdlpdglaskisegGTNFSVGQRQLVCLARAILRENRI 1275
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1276 LVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFG 1334
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
517-694 |
3.20e-30 |
|
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: 119.12 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESW----LFSG---------TVRQNIL 583
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGhadglkpelTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 F-----GQPMDSQRYEEvvkkcALERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASv 658
Cdd:COG4133 98 FwaalyGLRADREAIDE-----ALEA-VGLAGLAD-----LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 442622995 659 ARHLFDQCVRGHL-RGSTVVLVTHQEQFLPHVDQIVI 694
Cdd:COG4133 166 GVALLAELIAAHLaRGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
500-699 |
6.47e-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: 118.34 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 500 SIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQ--------- 569
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLkelrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 -----ESWLFSGTVRQNILFGQPMDSQRYEEVVKKC--ALERdFDLLPLRDNTIvgergATLSGGQKARISLArSVY-RK 641
Cdd:cd03225 80 vfqnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVeeALEL-VGLEGLRDRSP-----FTLSGGQKQRVAIA-GVLaMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 642 ASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQ 699
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1123-1329 |
7.05e-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: 118.34 E-value: 7.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINAL-FRLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQE 1201
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 P------------VLFSgtMRYNLDPFDEySDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAI 1269
Cdd:cd03225 84 PddqffgptveeeVAFG--LENLGLPEEE-IEERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1270 LRENRILVMDEATANVDPQTDGLIQATIRsKFRDC--TVLTIAHRLHTIID-SDKVMVMDAGR 1329
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1119-1329 |
3.16e-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: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1119 FKELNLRYtpnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISI 1197
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLlKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1198 IPQepvlfsgtmrynldpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnFSVGQRQLVCLARAILRENRILV 1277
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1278 MDEATANVDPQTDGLIQATIRSKFRD-CTVLTIAHRLHTIID-SDKVMVMDAGR 1329
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
499-700 |
4.80e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 114.62 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LS 565
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNILfgqpmdsqryeevvkkcalerdfdllplrdntivgergatlSGGQKARISLARSVYRKASIY 645
Cdd:cd03246 80 YLPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 646 LLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
510-710 |
4.84e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.05 E-value: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSG----------QLQVN---GSLSYTSQESWLFSG 576
Cdd:PRK10789 324 PQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdirfhdipltKLQLDswrSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQPMDSQ-RYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:PRK10789 404 TVANNIALGRPDATQqEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 656 ASVARHLFdQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PRK10789 484 GRTEHQIL-HNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
517-704 |
5.06e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.09 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------SLSYTSQES---WLFSGTVRQNI--- 582
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRsidRDFPISVRDVVlmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQPMDSQRYEEVVKKC---ALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVA 659
Cdd:cd03235 95 LYGHKGLFRRLSKADKAKvdeALER-VGLSELADRQI-----GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 660 RHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILaNGQIKALG 704
Cdd:cd03235 169 EDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
793-1045 |
6.75e-29 |
|
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: 117.74 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 793 FLVMLSSSVLAQVAVTGGDYFLTYWVKkesTAAGHGEMEDMESKSMDVYkYTLIIILSVIMNLSSSFLLFNIAKKASIRL 872
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD---VLLPDGDPETQALNVYSLA-LLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 873 HNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYH 952
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 953 LRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCIcv 1032
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI-- 234
|
250
....*....|...
gi 442622995 1033 IYISIITLSFFAF 1045
Cdd:pfam00664 235 GYLSYALALWFGA 247
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
227-447 |
7.15e-29 |
|
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: 118.09 E-value: 7.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 227 TTFGIHHVCFK----MRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMY 302
Cdd:cd18559 54 TVFQYSMAVSIggifASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 303 QEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTI 382
Cdd:cd18559 134 LLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 383 RQGQYIRGFDFARRIVLSRVAIFLSLVGYVILG--------KVFTpeiAFMITAYYNVLLaAMSIYVPSAIIQ 447
Cdd:cd18559 214 PSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslaglvalKVFY---SLALTTYLNWPL-NMSPEVITNIVA 282
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1117-1342 |
7.25e-29 |
|
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: 116.50 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtpnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHdLRRQI 1195
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIDGEDVRKEPRE-ARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYNLDPFDEYSDekLWGCLEEVKLKEVVS--DLPDGLASKISEggtnFSVGQRQLVCLARAILRE 1272
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYG--LFDEELKKRIEELIEllGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1273 NRILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1086-1341 |
7.58e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.70 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1086 RVVEYESIE-----PEGMLEAPD---DKKPPKTWPEQGEII--FKELNLRYTPNAKAEN-VLKSLSFVIQPREKVGIVGR 1154
Cdd:COG1123 220 RIVEDGPPEeilaaPQALAAVPRlgaARGRAAPAAAAAEPLleVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1155 TGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLRRQISIIPQEPV--LF-----SGTMRYNLDPFDEYSDEK 1223
Cdd:COG1123 300 SGSGKSTLARLLLGLlRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGLLSRAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1224 LWGCLEEVkLKEVvsDLPDGLASK-ISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPqtdgLIQATIRSKFR 1302
Cdd:COG1123 380 RRERVAEL-LERV--GLPPDLADRyPHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 442622995 1303 D------CTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:COG1123 449 DlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
140-713 |
1.18e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.06 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 140 ASWERELKNDGRSPSLVRALLRVFGWQLGFPGLAIFVveLGLRTLQPIFlvklISYFSGE-PDAANAGFYYavaQIVISA 218
Cdd:TIGR00958 133 ASEKEAEQGQSETADLLFRLLGLSGRDWPWLISAFVF--LTLSSLGEMF----IPFYTGRvIDTLGGDKGP---PALASA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 219 LTVM-ILTPTTF---GIHHVCFkmRVAMGSM-------IFRKALRLTKGALGDTTSGHVVNLISNDIPRL-DSAPYTVHY 286
Cdd:TIGR00958 204 IFFMcLLSIASSvsaGLRGGSF--NYTMARInlriredLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsRSLSLNVNV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 287 LWVGPLQVLVITYLMYQeigISAVFGVLfMLLFMPIQMYL----GTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYA 362
Cdd:TIGR00958 282 LLRNLVMLLGLLGFMLW---LSPRLTMV-TLINLPLVFLAekvfGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 363 WEqpfEQMVTHAREKeMNTIRQGQYIRGFDFARRIVLSRV---AIFLSLVGY----VILGKVFTPE-IAFMI-----TAY 429
Cdd:TIGR00958 358 AE---EGEASRFKEA-LEETLQLNKRKALAYAGYLWTTSVlgmLIQVLVLYYggqlVLTGKVSSGNlVSFLLyqeqlGEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 430 YNVLLaamsiYVPSAIIQTAqflTSIRRVEQFMqseelgssdksegpskDTVPGNPPSNNNEADLLKSAISIRDLKAKWd 509
Cdd:TIGR00958 434 VRVLS-----YVYSGMMQAV---GASEKVFEYL----------------DRKPNIPLTGTLAPLNLEGLIEFQDVSFSY- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 510 PNSPDY-TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFS 575
Cdd:TIGR00958 489 PNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFS 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNILFGqpMDSQRYEEV--VKKCALERDFDL-LPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:TIGR00958 569 GSVRENIAYG--LTDTPDEEImaAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 653 AVDASVARHLFDQCVRGhlrGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:TIGR00958 647 ALDAECEQLLQESRSRA---SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1135-1341 |
1.98e-27 |
|
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: 112.83 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVL-FSGT---- 1208
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTvrel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 --M-RYN-LDPFDEYSDE---KLWGCLEEVKLkevvSDLPDGLASKISegGtnfsvGQRQLVCLARAILRENRILVMDEA 1281
Cdd:COG1120 96 vaLgRYPhLGLFGRPSAEdreAVEEALERTGL----EHLADRPVDELS--G-----GERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1282 TANVDP--QTDglIQATIR--SKFRDCTVLTIAHRL-HTIIDSDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:COG1120 165 TSHLDLahQLE--VLELLRrlARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
517-715 |
2.22e-27 |
|
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: 112.44 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWL-FSGTVRQNI 582
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFG-QP------MDSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:COG1120 97 ALGrYPhlglfgRPSAEDREAVEE-ALER-TGLEHLADRPV-----DELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 656 ASVARHLFDQCVR-GHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLKTGLI 715
Cdd:COG1120 170 LAHQLEVLELLRRlARERGRTVVMVLHDlNLAARYADRLVLLKDGRIVAQGPPEEVLTPELL 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
517-704 |
3.48e-27 |
|
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: 110.69 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNILF 584
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDYALFPHlTVAENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 G---QPMDSQRYEEVVKKcALERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARH 661
Cdd:cd03259 96 GlklRGVPKAEIRARVRE-LLEL-VGLEGLLN-----RYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 662 LfdqcvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03259 169 L-----REELKelqrelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
517-704 |
4.87e-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: 109.06 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLqvngslsytsqeswlfsgtvrqnILFGQPMDSQRYEEV 596
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 VKKCA-----LERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVR-GH 670
Cdd:cd03214 72 ARKIAyvpqaLEL-LGLAHLADRPF-----NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlAR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 442622995 671 LRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALG 704
Cdd:cd03214 146 ERGKTVVMVLHDlNLAARYADRVILLKDGRIVAQG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
499-704 |
9.55e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.32 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdpnsPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYT---SQES--- 571
Cdd:COG1118 3 IEVRNISKRF----GSFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlpPRERrvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 572 WLFSG-------TVRQNILFG---QPMDSQRYEEVVKKCaLERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRK 641
Cdd:COG1118 79 FVFQHyalfphmTVAENIAFGlrvRPPSKAEIRARVEEL-LEL-VQLEGLAD-----RYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 642 ASIYLLDDPLSAVDASVARHLfdqcvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKEL-----RRWLRrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
517-700 |
9.72e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSGTVRQNIL 583
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 F-----GQPMDSQRYEEVVKkcALERDFDLLplrDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:COG4619 96 FpfqlrERKFDRERALELLE--RLGLPPDIL---DKPV-----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 659 ARH---LFDQCVRGHlrGSTVVLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:COG4619 166 TRRveeLLREYLAEE--GRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
499-702 |
1.37e-26 |
|
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: 109.10 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------SLSYTSQ 569
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 ES----WLfsgTVRQNILFG---QPM-DSQRYEEV---VKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSV 638
Cdd:cd03293 81 QDallpWL---TVLDNVALGlelQGVpKAEARERAeelLELVGLSGFENAYP-----------HQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 639 YRKASIYLLDDPLSAVDASVARHLFDQCVRgHLR--GSTVVLVTH--QEQ-FLPhvDQIVILAN--GQIKA 702
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLD-IWRetGKTVLLVTHdiDEAvFLA--DRVVVLSArpGRIVA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1135-1357 |
1.40e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.77 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGlHDLRRQISIIPQEPVLFSG-TMRYN 1212
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 LDPFDEY---SDEKLWGCLEEVkLKEVvsDLPDGLASKISeggtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1289
Cdd:COG1131 94 LRFFARLyglPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1290 dgliqatiRSKFRDcTVLTIAHRLHTIIDS-----------DKVMVMDAGRVVEFGSPYELMTKSDSKVFHNLVNQSGR 1357
Cdd:COG1131 167 --------RRELWE-LLRELAAEGKTVLLSthyleeaerlcDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEAR 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1120-1334 |
1.78e-26 |
|
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: 107.52 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNakaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISII 1198
Cdd:cd03214 3 ENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLlKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1199 PQepvlfsgtmrynldpfdeysdeklwgCLEEVklkevvsdlpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILVM 1278
Cdd:cd03214 79 PQ--------------------------ALELL-----------GLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1279 DEATANVDP----QTDGLIQATIRSkfRDCTVLTIAHRL-HTIIDSDKVMVMDAGRVVEFG 1334
Cdd:cd03214 122 DEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
499-712 |
2.42e-26 |
|
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: 109.13 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSYTS------ 568
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAElyrlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 ------QESWLFSG-TVRQNILFGQPMDSQRYEEVVKKCALER--------DFDLLPlrdntivgergATLSGGQKARIS 633
Cdd:cd03261 78 rmgmlfQSGALFDSlTVFENVAFPLREHTRLSEEEIREIVLEKleavglrgAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 634 LARSVYRKASIYLLDDPLSAVDaSVARHLFDQCVRgHLR---GSTVVLVTHQEQF-LPHVDQIVILANGQIKALGDYESL 709
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLD-PIASGVIDDLIR-SLKkelGLTSIMVTHDLDTaFAIADRIAVLYDGKIVAEGTPEEL 224
|
...
gi 442622995 710 LKT 712
Cdd:cd03261 225 RAS 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
499-704 |
5.21e-26 |
|
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: 107.11 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLS 565
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNI-LFGQPMDSQRYEevvkkcALErdfdllplrdntiVGERGATLSGGQKARISLARSVYRKASI 644
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 645 YLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03369 147 LVLDEATASID-YATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
517-699 |
2.02e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.86 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSytsqeSWLFSGTVRQNILF-GQpmdsqryee 595
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----AKLPLEELRRRIGYvPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 596 vvkkcalerdfdllplrdntivgergatLSGGQKARISLARSVYRKASIYLLDDPLSAVDAsVARHLFDQCVRGHL-RGS 674
Cdd:cd00267 81 ----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP-ASRERLLELLRELAeEGR 131
|
170 180
....*....|....*....|....*.
gi 442622995 675 TVVLVTHQEQFL-PHVDQIVILANGQ 699
Cdd:cd00267 132 TVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
496-702 |
2.93e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.71 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWDPNSPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------SLSY 566
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 567 TSQES----WLfsgTVRQNILFG---QPMDSQRYEEVVKKcALER----DF-DLLPlrdntivgergATLSGGQKARISL 634
Cdd:COG1116 85 VFQEPallpWL---TVLDNVALGlelRGVPKAERRERARE-LLELvglaGFeDAYP-----------HQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 635 ARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR-GSTVVLVTH--QEQ-FLphVDQIVILAN--GQIKA 702
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHdvDEAvFL--ADRVVVLSArpGRIVE 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1117-1340 |
2.94e-25 |
|
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: 106.43 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLeRPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPvlfsgtmRYNLDPF---DEYSDEKLW--GCLEEVK-----LKEVvsDLPDGLASKISEggtNFSVGQRQLVCL 1265
Cdd:COG1124 82 QMVFQDP-------YASLHPRhtvDRILAEPLRihGLPDREEriaelLEQV--GLPPSFLDRYPH---QLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 ARAILRENRILVMDEATANVDPqtdgLIQATI-------RSKfRDCTVLTIAHRLHtIID--SDKVMVMDAGRVVEFGSP 1336
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQAEIlnllkdlREE-RGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTV 223
|
....
gi 442622995 1337 YELM 1340
Cdd:COG1124 224 ADLL 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
499-712 |
8.85e-25 |
|
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: 104.34 E-value: 8.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDpnspDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-----------LSYT 567
Cdd:cd03299 1 LKVENLSKDWK----EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 568 SQESWLFSG-TVRQNILFG---QPMDSQRYEEVVKKCALERDFDLLPLRDNtivgergATLSGGQKARISLARSVYRKAS 643
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGlkkRKVDKKEIERKVLEIAEMLGIDHLLNRKP-------ETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 644 IYLLDDPLSAVDASVARHLFDQCVR-GHLRGSTVVLVTH-QEQFLPHVDQIVILANGQIKALGDYESLLKT 712
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKiRKEFGVTVLHVTHdFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
499-704 |
1.09e-24 |
|
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: 103.74 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------SLSY 566
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 567 TSQESWLFSG-TVRQNILF-----GQPmDSQRYEEVVKkcaLERDFDLLPLRDNTIVgergaTLSGGQKARISLARSVYR 640
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLP-KSEIKEEVEL---LLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 641 KASIYLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTH--QE-QFLphVDQIVILANGQIKALG 704
Cdd:cd03263 151 GPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTHsmDEaEAL--CDRIAIMSDGKLRCIG 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1135-1347 |
1.51e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 103.74 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDL---RRQISIIPQEPVLFSGT-- 1208
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLlRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLFQSGALFDSLtv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 -------MRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:cd03261 95 fenvafpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1282 TANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSDSKV 1347
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPLV 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
513-710 |
3.04e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 513 PDYTLSgINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS----------QESWLFSG-TVRQ 580
Cdd:COG3840 12 GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsmlfQENNLFPHlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 581 NILFG-------QPMDSQRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:COG3840 91 NIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 654 VDASVAR---HLFDQCVRGhlRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:COG3840 160 LDPALRQemlDLVDELCRE--RGLTVLMVTHDpEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1056-1312 |
3.25e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1056 VITQAMGLIDMVQ----WGVRQTAELENTMTAVERVVE-YESIEpegMLEAPDDKKPPKTWPEQGEIIFKELNLRyTPNA 1130
Cdd:COG4178 300 GLMQAASAFGQVQgalsWFVDNYQSLAEWRATVDRLAGfEEALE---AADALPEAASRIETSEDGALALEDLTLR-TPDG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1131 KAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLidtrdtrqmgLHDLRRqISIIPQEPVLFSGTM 1209
Cdd:COG4178 376 RP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIA----------RPAGAR-VLFLPQRPYLPLGTL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 R----YNLDPfDEYSDEKLWGCLEEVKLKEVVSDLPDGLA-SKIseggtnFSVGQRQLVCLARAILRENRILVMDEATAN 1284
Cdd:COG4178 443 ReallYPATA-EAFSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
250 260
....*....|....*....|....*...
gi 442622995 1285 VDPQTDGLIQATIRSKFRDCTVLTIAHR 1312
Cdd:COG4178 516 LDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
517-704 |
4.15e-24 |
|
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: 102.80 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNILF 584
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHYALFRHmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMD--SQRYEEVVKKcalERDFDLLPLRDNTIVGER-GATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARH 661
Cdd:cd03296 98 GLRVKprSERPPEAEIR---AKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 662 LfdqcvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03296 175 L-----RRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
167-437 |
4.27e-24 |
|
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: 103.49 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 167 LGFPGLAIFVVELGLrTLQPIFLVKLISYFS--GEPDAANAGFYYAVAQIVISALTVMILTpTTFGIHHVCFKMRVAMGS 244
Cdd:pfam00664 1 LILAILLAILSGAIS-PAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFL-QSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 245 MIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGIS-AVFGVLFMLLFMPIQ 323
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 324 MYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVA 403
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 442622995 404 IFLSLV--GYVILGKVFTPEIAFMITAYYNVLLAAM 437
Cdd:pfam00664 239 YALALWfgAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1135-1343 |
4.46e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 108.65 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYN- 1212
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRhFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 -LDPFDEYSDEklwgcLEEV-KLKEVVSD---LPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:PRK10789 410 aLGRPDATQQE-----IEHVaRLASVHDDilrLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1288 QTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKS 1343
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1117-1355 |
6.91e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.77 E-value: 6.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSL---INALFRlsYTDGSVLIDTRDTRQM---GLHD 1190
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER--PTSGSVLVDGVDLTALserELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEPVLFSG-TMRYN----LdpfdeysdeKLWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLV 1263
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSrTVAENvalpL---------EIAG-VPKAEIRKRVAELLElvGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQTDG----LIQaTIRSKFrDCTVLTIAHRLHTI--IdSDKVMVMDAGRVVEFGSPY 1337
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRsildLLK-DINREL-GLTIVLITHEMDVVrrI-CDRVAVLENGRIVEQGPVL 226
|
250
....*....|....*...
gi 442622995 1338 ELMTKSDSKVFHNLVNQS 1355
Cdd:COG1135 227 DVFANPQSELTRRFLPTV 244
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1117-1341 |
7.06e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.09 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTpnakAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDtrqmgLHDLRRQI 1195
Cdd:COG1121 7 IELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlPPTSGTVRLFGKP-----PRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEP------------VLFSGTMRYN--LDPFDEYSDEKLWGCLEEVKLkevvsdlpDGLASK-ISEggtnFSVGQR 1260
Cdd:COG1121 78 GYVPQRAevdwdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGL--------EDLADRpIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1261 QLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDaGRVVEFGSPYE 1338
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEE 224
|
...
gi 442622995 1339 LMT 1341
Cdd:COG1121 225 VLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
517-700 |
7.09e-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: 99.78 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGslsytsQESWLFSGTVRQNILFgQPMDSQRYEEv 596
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-LPEEPSLYEN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 vkkcalerdfdlLPLRDNtivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTV 676
Cdd:cd03230 88 ------------LTVREN-------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI 148
|
170 180
....*....|....*....|....*
gi 442622995 677 VLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:cd03230 149 LLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
515-704 |
1.32e-23 |
|
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: 100.41 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNI 582
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNYALYPHmTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFG-----QPMDS--QRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:cd03301 94 AFGlklrkVPKDEidERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 656 ASVARHLFDQCVRGHLR-GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03301 163 AKLRVQMRAELKRLQQRlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
498-712 |
1.56e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 100.82 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS-------- 568
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSekelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 -------QESWLFSG-TVRQNILFgqPM-------DSQRYEEVVKKCA---LERDFDLLPlrdntivgergATLSGGQKA 630
Cdd:COG1127 82 rrigmlfQGGALFDSlTVFENVAF--PLrehtdlsEAEIRELVLEKLElvgLPGAADKMP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 631 RISLARSVYRKASIYLLDDPLSAVDAsVARHLFDQCVRgHLR---GSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDY 706
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIR-ELRdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
|
....*.
gi 442622995 707 ESLLKT 712
Cdd:COG1127 227 EELLAS 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
398-713 |
1.62e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.97 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 398 VLSRVAIFLSLVGYVILGKVFTPE--------IAFMitAYYNVLLAAMSiyvpsaiiQTAQFLTSI----RRVEQFMQSE 465
Cdd:PRK13657 244 VLNRAASTITMLAILVLGAALVQKgqlrvgevVAFV--GFATLLIGRLD--------QVVAFINQVfmaaPKLEEFFEVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 466 elgssdksegpskDTVPG-NPPSNNNEADLLKSAISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLI 544
Cdd:PRK13657 314 -------------DAVPDvRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 545 QAILGELKANSGQLQVNG----SLSYTS---------QESWLFSGTVRQNILFGQPMDSQryEEVVKkcALER----DFD 607
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGtdirTVTRASlrrniavvfQDAGLFNRSIEDNIRVGRPDATD--EEMRA--AAERaqahDFI 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 608 LL-PLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFD--QCVRghlRGSTVVLVTHQEQ 684
Cdd:PRK13657 455 ERkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAalDELM---KGRTTFIIAHRLS 531
|
330 340
....*....|....*....|....*....
gi 442622995 685 FLPHVDQIVILANGQIKALGDYESLLKTG 713
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELVARG 560
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
517-695 |
2.05e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--SLSYTSQES---WLFSGTVRQNILFG------ 585
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMGrwarrg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 --QPMDSQRYEEVVKkcALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLF 663
Cdd:NF040873 88 lwRRLTRDDRAAVDD--ALER-VGLADLAGRQL-----GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|..
gi 442622995 664 DQCVRGHLRGSTVVLVTHQEQFLPHVDQIVIL 695
Cdd:NF040873 160 ALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
517-697 |
2.94e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.48 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN---SGQLQVNGS-----------LSYTSQESWLFSG-TVRQN 581
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRrltalpaeqrrIGILFQDDLLFPHlSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQPMD---SQRYEEVVKkcALErDFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:COG4136 97 LAFALPPTigrAQRRARVEQ--ALE-EAGLAGFADRDP-----ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442622995 659 aRHLFDQCVRGHLR--GSTVVLVTHQEQFLPHVDQIVILAN 697
Cdd:COG4136 169 -RAQFREFVFEQIRqrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
497-700 |
7.86e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWDPnspDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL------------ 564
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 565 ----SYTsqeswLF-SGTVRQNILFG---QPMDSQRYEEVVKKcALERdFDLLPLRDNtivgeRGATLSGGQKARISLAR 636
Cdd:COG3839 79 mvfqSYA-----LYpHMTVYENIAFPlklRKVPKAEIDRRVRE-AAEL-LGLEDLLDR-----KPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 637 SVYRKASIYLLDDPLSAVDAsvarHLFDQcVRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQI 700
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDA----KLRVE-MRAEIKrlhrrlGTTTIYVTHdQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
516-701 |
9.18e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 97.71 E-value: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 516 TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----------SLSYTSQES--WLFSGTVRQNIL 583
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQ---PMDSQRYEEVVKKCALERDFDLLPLrdntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDA---- 656
Cdd:cd03226 95 LGLkelDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYknme 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 657 SVARhLFDQCVRghlRGSTVVLVTHQEQFLPHV-DQIVILANGQIK 701
Cdd:cd03226 164 RVGE-LIRELAA---QGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
840-1325 |
1.31e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 105.88 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 840 VYKYTLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVM 919
Cdd:PTZ00265 100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 920 QIALWLAGIIIVIANVNPLLlvpTLMLSVIF---YHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQR 996
Cdd:PTZ00265 180 TYASAFLGLYIWSLFKNARL---TLCITCVFpliYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 997 VLEKEFDSYQDAHSS----AFFM----------YISTSQAFGYCMNcicviyISIITLSFFAFPPGNGADVGLVITQAMG 1062
Cdd:PTZ00265 257 TILKKFNLSEKLYSKyilkANFMeslhigmingFILASYAFGFWYG------TRIIISDLSNQQPNNDFHGGSVISILLG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1063 -LIDMVQWgvrqTAELENT---MTAVERVVE-YESIEPEGMLEAPDDKKppkTWPEQGEIIFKELNLRYTPNAKAEnVLK 1137
Cdd:PTZ00265 331 vLISMFML----TIILPNIteyMKSLEATNSlYEIINRKPLVENNDDGK---KLKDIKKIQFKNVRFHYDTRKDVE-IYK 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1138 SLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLI-DTRDTRQMGLHDLRRQISIIPQEPVLFSGTMR----- 1210
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLyDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKnniky 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1211 --------------YNLDPFDEYSDE--------KLWGCL-------------------------------EEVKLKEVV 1237
Cdd:PTZ00265 483 slyslkdlealsnyYNEDGNDSQENKnkrnscraKCAGDLndmsnttdsneliemrknyqtikdsevvdvsKKVLIHDFV 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1238 SDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLT--IAHRLHT 1315
Cdd:PTZ00265 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAHRLST 642
|
570
....*....|
gi 442622995 1316 IIDSDKVMVM 1325
Cdd:PTZ00265 643 IRYANTIFVL 652
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
499-700 |
1.61e-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: 97.56 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------------- 562
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 --SLSYTSQESWLFSG-TVRQNILFGQPMDSQRYEEVVKKC--ALERdFDLlPLRDNTIVGErgatLSGGQKARISLARS 637
Cdd:cd03255 81 rrHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAeeLLER-VGL-GDRLNHYPSE----LSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 638 VYRKASIYLLDDPLSAVDASVARH----LFDQCvrgHLRGSTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEvmelLRELN---KEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
509-710 |
2.15e-22 |
|
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: 103.75 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 509 DPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSYTS---------QESWLFS 575
Cdd:COG5265 368 DPERP--ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirDVTQASlraaigivpQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNILFGQPMDSQryEEVVK--KCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:COG5265 446 DTIAYNIAYGRPDASE--EEVEAaaRAAQIHDFiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 653 AVD-----------ASVARH---LfdqcVRGHlRGSTVVlvthqeqflpHVDQIVILANGQIKALGDYESLL 710
Cdd:COG5265 524 ALDsrteraiqaalREVARGrttL----VIAH-RLSTIV----------DADEILVLEAGRIVERGTHAELL 580
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
499-700 |
2.71e-22 |
|
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: 96.44 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNspdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESW------ 572
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 ---------LFSG-TVRQNILFGqPMDSQRyeeVVKKCALERDFDLLplrdnTIVG------ERGATLSGGQKARISLAR 636
Cdd:cd03262 78 vgmvfqqfnLFPHlTVLENITLA-PIKVKG---MSKAEAEERALELL-----EKVGladkadAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 637 SVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
517-705 |
3.93e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLsytsqeSWLF---SG-----TVRQNILFG--- 585
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 -----QPMDsQRYEEVVKKCALERDFDlLPLRdntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV-- 658
Cdd:COG1134 116 lglsrKEID-EKFDEIVEFAELGDFID-QPVK----------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFqk 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442622995 659 -ARHLFDQCVRghlRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGD 705
Cdd:COG1134 184 kCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1117-1330 |
4.28e-22 |
|
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: 94.77 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAkaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQmGLHDLRRQI 1195
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILgLLKPDSGEIKVLGKDIKK-EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYNLDpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnFSVGQRQLVCLARAILRENR 1274
Cdd:cd03230 76 GYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1275 ILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRV 1330
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
517-699 |
7.09e-22 |
|
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: 94.18 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG---------------SLSYTSQESWLFSG-TVRQ 580
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 581 NILFGqpmdsqryeevvkkcalerdfdllplrdntivgergatLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442622995 661 HLFDQCVRGHLR-GSTVVLVTHQEQFLPHV-DQIVILANGQ 699
Cdd:cd03229 138 EVRALLKSLQAQlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1120-1339 |
1.06e-21 |
|
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: 97.82 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL----SYTDGSVLIDTRDTRQMGLHDLR--- 1192
Cdd:COG0444 5 RNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpppGITSGEILFDGEDLLKLSEKELRkir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 -RQISIIPQEPvlfsgtmrYN-LDP--------------FDEYSDEKLWGC----LEEVKL---KEVVSDLPdglaskiS 1249
Cdd:COG0444 85 gREIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEARERaielLERVGLpdpERRLDRYP-------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1250 EggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPqtdgLIQATI-------RSKFrDCTVLTIAHRLHTI--IdSD 1320
Cdd:COG0444 150 E----LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVVaeI-AD 219
|
250
....*....|....*....
gi 442622995 1321 KVMVMDAGRVVEFGSPYEL 1339
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
522-704 |
1.46e-21 |
|
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: 94.48 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 522 LEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNILFG---- 585
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFAHlTVEQNVGLGlspg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 ---QPMDSQRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHL 662
Cdd:cd03298 99 lklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442622995 663 FDQCVRGHL-RGSTVVLVTHQEQFLPHVDQIVI-LANGQIKALG 704
Cdd:cd03298 168 LDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
499-704 |
1.56e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.63 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSP--DYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVnGSLSYTSQ------- 569
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 -------------ESWLFSGTVRQNILFGqPMDSQRYEEVVKKCALERdFDLLPLrDNTIVGERGATLSGGQKARISLAR 636
Cdd:PRK13634 82 plrkkvgivfqfpEHQLFEETVEKDICFG-PMNFGVSEEDAKQKAREM-IELVGL-PEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 637 SVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHL-RGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALG 704
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmEDAARYADQIVVMHKGTVFLQG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1117-1332 |
1.66e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 94.73 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQM---GLHDLR 1192
Cdd:COG2884 2 IRFENVSKRYPGGREA---LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGQDLSRLkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQ-----------EPVLFSgtMRYNLDPFDEYSD--EKLwgcLEEVKLKEVVSDLPDGLaskiseggtnfSVGQ 1259
Cdd:COG2884 79 RRIGVVFQdfrllpdrtvyENVALP--LRVTGKSRKEIRRrvREV---LDLVGLSDKAKALPHEL-----------SGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1260 RQLVCLARAILRENRILVMDEATANVDPQT-DGLIQATIRSKFRDCTVLtIA-HRLHtIIDS--DKVMVMDAGRVVE 1332
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsWEIMELLEEINRRGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
517-710 |
2.17e-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: 94.42 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTSQESWLFSG-TVRQN 581
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGqpmdSQRYEEVVKKCALERDFDLLP-LRDntIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:cd03224 96 LLLG----AYARRRAKRKARLERVYELFPrLKE--RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 661 HLFDQCVRGHLRGSTVVLVthqEQF----LPHVDQIVILANGQIKALGDYESLL 710
Cdd:cd03224 170 EIFEAIRELRDEGVTILLV---EQNarfaLEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1117-1333 |
2.51e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 94.09 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDL---- 1191
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 RRQISIIPQE---------------PVLFSGTmrynldpFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfS 1256
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGV-------PKKERRERAEELLERVGLGDRLNHYPSEL-----------S 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1257 VGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHrlhtiidsDKVMVMDAGRVVEF 1333
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH--------DPELAEYADRIIEL 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
517-700 |
2.53e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS---------------QESWLFSG-TVR 579
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSRLKrreipylrrrigvvfQDFRLLPDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILF-----GQPMDS--QRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 653 AVDASVAR---HLFDQCvrgHLRGSTVVLVTHQEQFLPHVDQIVI-LANGQI 700
Cdd:COG2884 167 NLDPETSWeimELLEEI---NRRGTTVLIATHDLELVDRMPKRVLeLEDGRL 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
517-704 |
3.00e-21 |
|
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: 93.75 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLsytsqeSWLF---SG-----TVRQNILFG--- 585
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------SSLLglgGGfnpelTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 ----QPMDSQRYEEVVKKCALERDFDlLPLRdntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS---- 657
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqek 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442622995 658 VARHLFDQCvrghLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:cd03220 181 CQRRLRELL----KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
517-705 |
4.80e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.32 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNILF 584
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQDYALFPHlTVAENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 G---QPMDSQRYEEVVKKcALERdFDLLPLrdntivGERG-ATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:COG3842 101 GlrmRGVPKAEIRARVAE-LLEL-VGLEGL------ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLRE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 661 HLfdqcvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALGD 705
Cdd:COG3842 173 EM-----REELRrlqrelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1135-1329 |
6.44e-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: 91.48 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLH--DLRRQISIIPQEPVLFSgtmry 1211
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFDeysdeklwgcleevklkevvsdlpdglasKISEGgtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDG 1291
Cdd:cd03229 90 HLTVLE-----------------------------NIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442622995 1292 LIQATIRSKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGR 1329
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
517-700 |
7.07e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.40 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSYTSQESW------LFSG-------TVR 579
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQLrrqigmIFQQfnlierlSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFG--------QPMDSQRYEEVVKKC--ALERdFDLLPLrdntiVGERGATLSGGQKARISLARSVYRKASIYLLDD 649
Cdd:cd03256 97 ENVLSGrlgrrstwRSLFGLFPKEEKQRAlaALER-VGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 650 PLSAVDASVAR---HLF-DQCVRghlRGSTVVLVTHQEQF-LPHVDQIVILANGQI 700
Cdd:cd03256 171 PVASLDPASSRqvmDLLkRINRE---EGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1135-1334 |
8.50e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.20 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGLHdlRRQISIIPQEPVLF-------- 1205
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 --SGtMRYNLDPFDEYSDEKLWGcLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:cd03259 93 iaFG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1284 NVDPQTDGLIQATIRSKFR--DCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFG 1334
Cdd:cd03259 160 ALDAKLREELREELKELQRelGITTIYVTHdqeealAL-----ADRIAVMNEGRIVQVG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
517-700 |
1.12e-20 |
|
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: 90.18 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGslsytsqeswlfsgtvrQNILFGQPMDSQRyeev 596
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFASPRDARR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 vkkcalerdfdllplrdntivgeRG-AT---LSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR 672
Cdd:cd03216 75 -----------------------AGiAMvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ 131
|
170 180 190
....*....|....*....|....*....|..
gi 442622995 673 GSTVVLVTHqeqFLPHV----DQIVILANGQI 700
Cdd:cd03216 132 GVAVIFISH---RLDEVfeiaDRVTVLRDGRV 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
521-710 |
1.19e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 521 NLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-----------LSYTSQESWLFSG-TVRQNILFG-QP 587
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGlNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 ----MDSQR--YEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVaRH 661
Cdd:PRK10771 99 glklNAAQRekLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL-RQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 662 ----LFDQ-CvrgHLRGSTVVLVTHQeqfLPHVDQI----VILANGQIKALGDYESLL 710
Cdd:PRK10771 167 emltLVSQvC---QERQLTLLMVSHS---LEDAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
515-704 |
1.41e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 91.59 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIK---PGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL-----------------SYTSQESWLF 574
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 575 SG-TVRQNILFGQPMDSQRyeevVKKCALERDFDLLPLrdNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:cd03297 88 PHlNVRENLAFGLKRKRNR----EDRISVDELLDLLGL--DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 654 VDasvaRHLFDQCvRGHLR------GSTVVLVTH--QEQFLPHvDQIVILANGQIKALG 704
Cdd:cd03297 162 LD----RALRLQL-LPELKqikknlNIPVIFVTHdlSEAEYLA-DRIVVMEDGRLQYIG 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
389-699 |
1.65e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 389 RGFDFARRIVlSRVAIFLSLVgyVILGKVFTPEIAF----MITAYYNVLLAAMSIYVpSAIIQTAQFLTSIRRVEQFMQS 464
Cdd:COG4178 266 RNLTFFTTGY-GQLAVIFPIL--VAAPRYFAGEITLgglmQAASAFGQVQGALSWFV-DNYQSLAEWRATVDRLAGFEEA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 465 EELGSSDKSEGPSKDTVPGNppsnnneadllksAISIRDLkakwDPNSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSS 542
Cdd:COG4178 342 LEAADALPEAASRIETSEDG-------------ALALEDL----TLRTPDGRplLEDLSLSLKPGERLLITGPSGSGKST 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 543 LIQAILGELKANSGQLQV--NGSLSYTSQESWLFSGTVRQNILFGQP---MDSQRYEEVVKKCALErdfDLLPLRDntIV 617
Cdd:COG4178 405 LLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVGLG---HLAERLD--EE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 618 GERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQcVRGHLRGSTVVLVTHQEQFLPHVDQIVILAN 697
Cdd:COG4178 480 ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
..
gi 442622995 698 GQ 699
Cdd:COG4178 559 DG 560
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
517-704 |
3.29e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-----------LSYTSQESWLFSG-TVRQNILF 584
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFRHmTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMDSQRYE---EVVKKCALErdfdLLPLRDNTIVGER-GATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:PRK10851 98 GLTVLPRRERpnaAAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 661 HLfdqcvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK10851 174 EL-----RRWLRqlheelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1135-1340 |
6.05e-20 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 90.19 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS-YTDGSVLIDTRDTRQMGLHD-LRRQISIIPQEPVLFSG-TMRY 1211
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLdpfdEYSDEKLWGCLEEVKLKEVVSDLPDgLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDG 1291
Cdd:cd03224 95 NL----LLGAYARRRAKRKARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1292 LIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELM 1340
Cdd:cd03224 170 EIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1119-1334 |
6.91e-20 |
|
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: 89.51 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1119 FKELNLRYTpnakAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMglhdlRRQISI 1197
Cdd:cd03235 2 VEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1198 IPQ------------EPVLFSGTMRYnLDPFDEYSDEKlWGCLEEVkLKEV-VSDLPDglaSKISEggtnFSVGQRQLVC 1264
Cdd:cd03235 73 VPQrrsidrdfpisvRDVVLMGLYGH-KGLFRRLSKAD-KAKVDEA-LERVgLSELAD---RQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1265 LARAILRENRILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIIDS-DKVMVMDaGRVVEFG 1334
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN-RTVVASG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1117-1332 |
8.77e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.72 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLR 1192
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQ-ISIIPQepvlfsgtmRYNLDPF-----------------DEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtn 1254
Cdd:COG1136 85 RRhIGFVFQ---------FFNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1255 fSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVE 1332
Cdd:COG1136 146 -SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
496-735 |
8.77e-20 |
|
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: 94.58 E-value: 8.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN---SGQLQVNG---------- 562
Cdd:COG1123 2 TPLLEVRDLSVRY-PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 ---SLSYTSQE--SWLFSGTVRQNILFG---QPMDS----QRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKA 630
Cdd:COG1123 81 rgrRIGMVFQDpmTQLNPVTVGDQIAEAlenLGLSRaearARVLELLEAVGLERRLDRYP-----------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 631 RISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHL-RGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYES 708
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDlGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260 270
....*....|....*....|....*....|.
gi 442622995 709 LLKTGL----ITGLGSLSKTDKAKTEEQEPL 735
Cdd:COG1123 230 ILAAPQalaaVPRLGAARGRAAPAAAAAEPL 260
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
517-716 |
1.18e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS------------QESWL-FSGTVRQNI 582
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrPLAAWSpwelarrravlpQHSSLaFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFG---QPMDSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLAR-------SVYRKASIYLLDDPLS 652
Cdd:COG4559 97 ALGrapHGSSAAQDRQIVRE-ALAL-VGLAHLAGRSY-----QTLSGGEQQRVQLARvlaqlwePVDGGPRWLFLDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 653 AVD-------ASVARHLFDqcvrghlRGSTVVLVTHQ----EQFlphVDQIVILANGQIKALGDYESLLKTGLIT 716
Cdd:COG4559 170 ALDlahqhavLRLARQLAR-------RGGGVVAVLHDlnlaAQY---ADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1135-1331 |
1.32e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 87.10 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQepvlfsgtmryn 1212
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSgLYKPDSGEILVDGKEVSFASPRDARRAgIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 ldpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDG 1291
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442622995 1292 LIqATIRsKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:cd03216 121 LF-KVIR-RLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
499-700 |
1.66e-19 |
|
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: 89.10 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKaKWDP--NSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFsg 576
Cdd:cd03257 2 LEVKNLS-VSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNI--LFGQPMDS---------------QRYEEVVKKCALER----DFDLLPLrDNTIVGERGATLSGGQKARISLA 635
Cdd:cd03257 79 IRRKEIqmVFQDPMSSlnprmtigeqiaeplRIHGKLSKKEARKEavllLLVGVGL-PEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 636 RSVYRKASIYLLDDPLSAVDASVAR---HLFDQCVRGhlRGSTVVLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAqilDLLKKLQEE--LGLTLLFITHDLGVVAKIaDRVAVMYAGKI 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1114-1339 |
2.01e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.07 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1114 QGEII-FKELNLRYtPNAKAEnVLKSLSFVIQPREKVGIVGRTGAGKSSL---INALFRLsyTDGSVLIDTRDTRQMGLH 1189
Cdd:PRK13635 2 KEEIIrVEHISFRY-PDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLP--EAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1190 DLRRQISIIPQEP-VLFSGT-----MRYNLD----PFDEYSdEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQ 1259
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFVGAtvqddVAFGLEnigvPREEMV-ERVDQALRQVGMEDFLNREPHRL-----------SGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1260 RQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIR--SKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPY 1337
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
..
gi 442622995 1338 EL 1339
Cdd:PRK13635 226 EI 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
517-716 |
2.18e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS------------QESWL-FSGTVRQNI 582
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrPLADWSpaelarrravlpQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQ---PMDSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLAR------SVYRKASIYLLDDPLSA 653
Cdd:PRK13548 98 AMGRaphGLSRAEDDALVAA-ALAQ-VDLAHLAGRDY-----PQLSGGEQQRVQLARvlaqlwEPDGPPRWLLLDEPTSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 654 VD-------ASVARHLFDQcvrghlRGSTVVLVTHQ----EQFlphVDQIVILANGQIKALGDYESLLKTGLIT 716
Cdd:PRK13548 171 LDlahqhhvLRLARQLAHE------RGLAVIVVLHDlnlaARY---ADRIVLLHQGRLVADGTPAEVLTPETLR 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1120-1342 |
3.27e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.94 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNakaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS------YTDGSVLIDTRD--TRQMGLHDL 1191
Cdd:COG1117 15 RNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgaRVEGEILLDGEDiyDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 RRQISIIPQEPVLFSGTM---------------RYNLDPFDEYSDEK--LWgclEEVKlkevvsdlpDglasKISEGGTN 1254
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIydnvayglrlhgiksKSELDEIVEESLRKaaLW---DEVK---------D----RLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1255 FSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAH------RLhtiidSDKVMVMDAG 1328
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLG 229
|
250
....*....|....
gi 442622995 1329 RVVEFGSPYELMTK 1342
Cdd:COG1117 230 ELVEFGPTEQIFTN 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
517-704 |
4.09e-19 |
|
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: 87.71 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILG---ELKANSGQLQVNG----------SLSYTSQESWLFSG-TVRQNI 582
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQPM-------DSQRYEEVVKkcALERDFDLLPLRDNTIVGergatLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:cd03234 103 TYTAILrlprkssDAIRKKRVED--VLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 656 ASVARHLFDQCVRGHLRGSTVVLVTHQ---EQFlPHVDQIVILANGQIKALG 704
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQprsDLF-RLFDRILLLSSGEIVYSG 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1135-1347 |
5.58e-19 |
|
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: 87.49 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQEPVLFSG-TMRY 1211
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISgFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLD---------------PFDEYSD--EKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENR 1274
Cdd:cd03219 95 NVMvaaqartgsglllarARREEREarERAEELLERVGLADLADRPAGEL-----------SYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1275 ILVMDEATANVDPQ-TDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMtkSDSKV 1347
Cdd:cd03219 164 LLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR--NNPRV 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
251-757 |
6.93e-19 |
|
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: 93.44 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 251 LRLTKGALGDTTSGHVVNLISNDIPRLDSA-PYTVHYLwvgpLQVLVITylmyqeIGISAVFGVL----------FMLLF 319
Cdd:TIGR01271 969 LQAPMAVLNTMKAGRILNRFTKDMAIIDDMlPLTLFDF----IQLTLIV------LGAIFVVSVLqpyifiaaipVAVIF 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 320 MPIQMYLgTRTSAiQLKAAErTDNRIRMVNEIISAIQVLkmyaW------EQPFEQMVTHareKEMNTIRQGQY-----I 388
Cdd:TIGR01271 1039 IMLRAYF-LRTSQ-QLKQLE-SEARSPIFSHLITSLKGL----WtirafgRQSYFETLFH---KALNLHTANWFlylstL 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 389 RGFDFARRIVLsrvAIFLSLVGYVILG--KVFTPEIAFMITAYYNVLlAAMSIYVPSAIiQTAQFLTSIRRVEQFM---- 462
Cdd:TIGR01271 1109 RWFQMRIDIIF---VFFFIAVTFIAIGtnQDGEGEVGIILTLAMNIL-STLQWAVNSSI-DVDGLMRSVSRVFKFIdlpq 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 463 QSEELGSSDKSEGPSKDTVPGNP------PSNNNeadllksaISIRDLKAKWDPNSpDYTLSGINLEIKPGSVVAVIGLT 536
Cdd:TIGR01271 1184 EEPRPSGGGGKYQLSTVLVIENPhaqkcwPSGGQ--------MDVQGLTAKYTEAG-RAVLQDLSFSVEGGQRVGLLGRT 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 537 GSGKSSLIQAILgELKANSGQLQVNGsLSYTS--------------QESWLFSGTVRQNILFGQPMDSQRYEEVVKKCAL 602
Cdd:TIGR01271 1255 GSGKSTLLSALL-RLLSTEGEIQIDG-VSWNSvtlqtwrkafgvipQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGL 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 603 ERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQ 682
Cdd:TIGR01271 1333 KSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 683 EQFLPHVDQIVILANGQIKALGDYESLL-KTGLITglGSLSKTDKAKTEEQEPLNLNSPDNKNEVTPIKENSEQTV 757
Cdd:TIGR01271 1412 VEALLECQQFLVIEGSSVKQYDSIQKLLnETSLFK--QAMSAADRLKLFPLHRRNSSKRKPQPKITALREEAEEEV 1485
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
499-711 |
8.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------- 562
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 ---SLSYTSQESWLFSGTVRQNILFGqPMDSQRYEEVVKKcALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVY 639
Cdd:PRK13637 83 kkvGLVFQYPEYQLFEETIEKDIAFG-PINLGLSEEEIEN-RVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 640 RKASIYLLDDPLSAVDASVARHLFDQCVRGHLR-GSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
499-710 |
9.05e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 86.87 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDYT-LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------------- 562
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 -SLSYTSQESWLFSG-TVRQNILFgqPMDSQRYEevvKKCALERDFDLLPLrdntiVG--ERG----ATLSGGQKARISL 634
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVAL--PLEIAGVP---KAEIEERVLELLEL-----VGleDKAdaypAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 635 ARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR-GSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESLL 710
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
517-710 |
9.08e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 87.36 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSG-TVRQNI 582
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 -----LFGQPmdSQRYEEVVKKcALErdfdLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS 657
Cdd:cd03295 97 alvpkLLKWP--KEKIRERADE-LLA----LVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 658 VARHLFDQCVRGHLR-GSTVVLVTH--QEQFLPhVDQIVILANGQIKALGDYESLL 710
Cdd:cd03295 170 TRDQLQEEFKRLQQElGKTIVFVTHdiDEAFRL-ADRIAIMKNGEIVQVGTPDEIL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1117-1338 |
1.02e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.09 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQM---GLHDLR 1192
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSG-TMRYNLD-PFdeysdeKLWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARA 1268
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVAlPL------ELAG-TPKAEIKARVTELLElvGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1269 ILRENRILVMDEATANVDPQTDGLIQATIRSKFRD--CTVLTIAHRLHTI--IdSDKVMVMDAGRVVEFGSPYE 1338
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITHEMDVVkrI-CDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1117-1332 |
1.14e-18 |
|
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: 86.37 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDtrqmgLHDLRRQI 1195
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFS-GTMRYN----LD----PFDEySDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLA 1266
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLElqgvPKAE-ARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATI-----RSKFrdcTVLTIAHRLH-TIIDSDKVMVMDA--GRVVE 1332
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1133-1357 |
1.29e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1133 ENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTR--------DTRQMGLHDLRRQISIIPQEPVL 1204
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRveffnqniYERRVNLNRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 FSGTMRYNLdpfdEYSdEKLWGCLEEVKLKEVV------SDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVM 1278
Cdd:PRK14258 100 FPMSVYDNV----AYG-VKIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1279 DEATANVDPQTDGLIQATIRS-KFR-DCTVLTIAHRLHTIID-SDKVMVMDA-----GRVVEFGspyelMTKsdsKVFHN 1350
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSlRLRsELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG-----LTK---KIFNS 246
|
....*..
gi 442622995 1351 LVNQSGR 1357
Cdd:PRK14258 247 PHDSRTR 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
476-710 |
1.43e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 90.73 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 476 PSKDTVPGNPPSNNNEADLLksaISIRDLKAKWDPNSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKA 553
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPL---LEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 554 NSGQLQVNG-SLSYTSQESW-----------------LFSG-TVRQNILFgqPMDSQRY----------EEVVKKCALER 604
Cdd:COG1123 318 TSGSILFDGkDLTKLSRRSLrelrrrvqmvfqdpyssLNPRmTVGDIIAE--PLRLHGLlsraerrervAELLERVGLPP 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 605 DF-DLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDqcvrgHLR------GSTVV 677
Cdd:COG1123 396 DLaDRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-----LLRdlqrelGLTYL 459
|
250 260 270
....*....|....*....|....*....|....
gi 442622995 678 LVTHQEQFLPHV-DQIVILANGQIKALGDYESLL 710
Cdd:COG1123 460 FISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1117-1351 |
1.54e-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: 86.47 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLR 1192
Cdd:cd03256 1 IEVENLSKTY-PNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvEPTSGSVLIDGTDINKLKgkaLRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEP-----------VLFS-----GTMRYNLDPFDEYSDEKLWGCLEEVklkevvsdlpdGLASKISEGGTNFS 1256
Cdd:cd03256 78 RQIGMIFQQFnlierlsvlenVLSGrlgrrSTWRSLFGLFPKEEKQRALAALERV-----------GLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1257 VGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEF 1333
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFD 226
|
250
....*....|....*...
gi 442622995 1334 GSPYELmtksDSKVFHNL 1351
Cdd:cd03256 227 GPPAEL----TDEVLDEI 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1135-1342 |
1.70e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL------SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSgt 1208
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 mryNLDPFDEYS---------------DEKLWGCLEEVKLKEVVSDLPDGLASKISEGgtnfsvgQRQLVCLARAILREN 1273
Cdd:PRK14247 96 ---NLSIFENVAlglklnrlvkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGG-------QQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1274 RILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
517-710 |
2.10e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG---------SL----SYTSQESWLFSGTVRQNIL 583
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaSLrnqvALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPMDSQRYE-EVVKKCALERDF-DLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARH 661
Cdd:PRK11176 439 YARTEQYSREQiEEAARMAYAMDFiNKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 662 LfdQCVRGHLRGS-TVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PRK11176 519 I--QAALDELQKNrTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1117-1341 |
2.62e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.58 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRLsyTDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:PRK13632 8 IKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKP--QSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEP-VLFSGTmrynldpfdEYSDEKLWG----CLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLA 1266
Cdd:PRK13632 84 KIGIIFQNPdNQFIGA---------TVEDDIAFGlenkKVPPKKMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
517-704 |
2.67e-18 |
|
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: 85.75 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-----------LSYTSQESWLFSG-TVRQNILF 584
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMDSQRYEEVVKKcaLERDFDLLPLRDntIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFD 664
Cdd:cd03300 96 GLRLKKLPKAEIKER--VAEALDLVQLEG--YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 665 QCVRGHLR-GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:cd03300 172 ELKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1117-1339 |
2.73e-18 |
|
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: 85.25 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQmGLHDLRRQI 1195
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgELRPTSGTAYINGYSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYNLdpfdeysdeKLWG---CLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAI 1269
Cdd:cd03263 78 GYCPQFDALFDElTVREHL---------RFYArlkGLPKSEIKEEVELLLRvlGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1270 LRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTI-IDSDKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
517-700 |
2.73e-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: 85.15 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----------------SLSYTSQESWLFSG-TVR 579
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGErgatLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVA 659
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 660 RHLFDQCVRGHLRGSTVVLVTH-QEQFLPHVDQIVILANGQI 700
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
497-700 |
2.95e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.52 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELK--ANSGQLQVNG----------SL 564
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGrpldkrsfrkII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 565 SYTSQESWLFSG-TVRQNILFgqpmdsqryeevVKKCalerdfdllplrdntivgeRGatLSGGQKARISLARSVYRKAS 643
Cdd:cd03213 85 GYVPQDDILHPTlTVRETLMF------------AAKL-------------------RG--LSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 644 IYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ------EQFlphvDQIVILANGQI 700
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpsseifELF----DKLLLLSQGRV 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1123-1334 |
4.28e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.75 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYT----PNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSY--TDGSVLIdtrDTRQMGLHDLRRQI 1195
Cdd:cd03213 8 NLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGlgVSGEVLI---NGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYNLDpfdeYSdeklwgcleeVKLKevvsdlpdGLaskiseggtnfSVGQRQLVCLARAILRENR 1274
Cdd:cd03213 85 GYVPQDDILHPTlTVRETLM----FA----------AKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1275 ILVMDEATANVDPQTDGLIQATIRsKFRD--CTVLTIAHRLHTIIDS--DKVMVMDAGRVVEFG 1334
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
499-700 |
4.29e-18 |
|
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: 84.92 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPnspDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAI--LGELKAN---SGQLQVNGSLSYTS----- 568
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGapdEGEVLLDGKDIYDLdvdvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 ----------QESWLFSGTVRQNILFGQPM----DSQRYEEVVKKcALERDfdllPLRDNtiVGER--GATLSGGQKARI 632
Cdd:cd03260 78 elrrrvgmvfQKPNPFPGSIYDNVAYGLRLhgikLKEELDERVEE-ALRKA----ALWDE--VKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 633 SLARSVYRKASIYLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALD-PISTAKIEELIAELKKEYTIVIVTHNmQQAARVADRTAFLLNGRL 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
499-757 |
5.04e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 85.68 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILgELKANSGQLQVNG-------------SLS 565
Cdd:cd03289 3 MTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQESWLFSGTVRQNI-LFGQPMDSQRYEeVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASI 644
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 645 YLLDDPLSAVDaSVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKalgDYESLLKtgLITGLGSL--- 721
Cdd:cd03289 160 LLLDEPSAHLD-PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR---QYDSIQK--LLNEKSHFkqa 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 442622995 722 -SKTDKAKTEEQEPLNLNSPDNKNEVTPIKENSEQTV 757
Cdd:cd03289 234 iSPSDRLKLFPRRNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1133-1346 |
5.73e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 84.69 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1133 ENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTrqMGLHDLRRQISIIPQEPVLFSgtmry 1211
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDI--TNLPPEKRDISYVPQNYALFP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFD--EYSDEKLWGCLEEV--KLKEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:cd03299 85 HMTVYKniAYGLKKRKVDKKEIerKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1288 QTDGLIQ---ATIRSKFrDCTVLTIAHRLHTI-IDSDKVMVMDAGRVVEFGSPYELMTKSDSK 1346
Cdd:cd03299 163 RTKEKLReelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
517-707 |
8.22e-18 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 84.41 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTSQESWLFSG-TVRQN 581
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 IL----------FGQPMDSQRYEEVVKKC--ALERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDD 649
Cdd:cd03219 96 VMvaaqartgsgLLLARARREEREARERAeeLLER-VGLADLAD-----RPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 650 PLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQF-LPHVDQIVILANGQIKALGDYE 707
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPD 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1117-1332 |
1.06e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.37 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINA---LFRLsyTDGSVLIDTRDtrqmgLHDLRR 1193
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagLEKP--TSGEVLVDGKP-----VTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLF---------------SGTMRynldpfDEYSD--EKLwgcLEEVKLKEVVSDLPDGLaskiseggtnfS 1256
Cdd:COG1116 81 DRGVVFQEPALLpwltvldnvalglelRGVPK------AERREraREL---LELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1257 VGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAH------RLhtiidSDKVMVMDA- 1327
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
....*.
gi 442622995 1328 -GRVVE 1332
Cdd:COG1116 216 pGRIVE 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
517-692 |
1.06e-17 |
|
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: 82.79 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESW----LFSG---------TVRQNIL 583
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPheniLYLGhlpglkpelSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPMdsQRYEEVVKKCALE----RDFDLLPLrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVA 659
Cdd:TIGR01189 96 FWAAI--HGGAQRTIEDALAavglTGFEDLPA----------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|....
gi 442622995 660 RhLFDQCVRGHL-RGSTVVLVTHQEQFLPHVDQI 692
Cdd:TIGR01189 164 A-LLAGLLRAHLaRGGIVLLTTHQDLGLVEAREL 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
517-710 |
1.14e-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: 83.75 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------------SLSYTSQESWLFSG-TVRQN 581
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 I---LFGQPMDSQRYEEVVKkcALERDFDLLPLRDNtivgeRGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:cd03218 96 IlavLEIRGLSKKEREEKLE--ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 659 ARHLfdQCVRGHLRGSTV-VLVT--HQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:cd03218 169 VQDI--QKIIKILKDRGIgVLITdhNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
495-726 |
1.23e-17 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 84.19 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDpNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------ 562
Cdd:cd03288 16 LGGEIKIHDLCVRYE-NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 -SLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRK 641
Cdd:cd03288 95 sRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 642 ASIYLLDDPLSAVDASvARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL--KTGLitgLG 719
Cdd:cd03288 175 SSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV---FA 250
|
....*..
gi 442622995 720 SLSKTDK 726
Cdd:cd03288 251 SLVRTDK 257
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1117-1289 |
1.33e-17 |
|
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: 83.23 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRqmGLHD----- 1190
Cdd:cd03292 1 IEFINVTKTYPNGTAA---LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVS--DLRGraipy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEPVLFsgtmrYNLDPFDE--YSDEklwgcLEEVKLKEV---VSDLPD--GLASKISEGGTNFSVGQRQLV 1263
Cdd:cd03292 76 LRRKIGVVFQDFRLL-----PDRNVYENvaFALE-----VTGVPPREIrkrVPAALElvGLSHKHRALPAELSGGEQQRV 145
|
170 180
....*....|....*....|....*.
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQT 1289
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDT 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1135-1347 |
1.49e-17 |
|
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: 83.93 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDLRRQ--------ISIIPQEPVL- 1204
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITgFYRPTSGRILFDGRDITGLPPHRIARLgiartfqnPRLFPELTVLe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 -------------FSGTMRYNLDPFDEYSD--EKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAI 1269
Cdd:COG0411 99 nvlvaaharlgrgLLAALLRLPRARREEREarERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1270 LRENRILVMDEATANVDPQ-TDGLIQaTIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMtkSDS 1345
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEeTEELAE-LIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVR--ADP 244
|
..
gi 442622995 1346 KV 1347
Cdd:COG0411 245 RV 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
517-712 |
1.90e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGsLSYTS----------------QESWLFSG-TVR 579
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-LKVNDpkvderlirqeagmvfQQFYLFPHlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFGqPMdsqRYEEVVKKCALERDFDLLplrdnTIVG--ERG----ATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PRK09493 96 ENVMFG-PL---RVRGASKEEAEKQARELL-----AKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 654 VDA-------SVARHLFDQcvrghlrGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESLLKT 712
Cdd:PRK09493 167 LDPelrhevlKVMQDLAEE-------GMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1136-1335 |
2.05e-17 |
|
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: 87.43 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVL-----IDTRDTRQMglHDLRRQISIIPQEPvlFSgtmr 1210
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRfdgqdLDGLSRRAL--RPLRRRMQVVFQDP--FG---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1211 yNLDP---------------FDEYS----DEKLWGCLEEVKLKevvsdlPDGLASKISEggtnFSVGQRQLVCLARAILR 1271
Cdd:COG4172 374 -SLSPrmtvgqiiaeglrvhGPGLSaaerRARVAEALEEVGLD------PAARHRYPHE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1272 ENRILVMDEATANVDPQtdglIQATIRSKFRDC------TVLTIAHRLHTI--IdSDKVMVMDAGRVVEFGS 1335
Cdd:COG4172 443 EPKLLVLDEPTSALDVS----VQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGP 509
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1117-1348 |
2.58e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.50 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtpnakaENVLKSLSFVIQPREKVGIVGRTGAGKSSLINAL--FrLSYTDGSVLIDTRDTRQMGLHDlrRQ 1194
Cdd:COG3840 2 LRLDDLTYRY------GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNGQDLTALPPAE--RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSG-TMRYN----LDPFDEYSDE---KLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLA 1266
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1267 RAILRENRILVMDEATANVDPqtdGLIQ------ATIRSKfRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDP---ALRQemldlvDELCRE-RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
....*....
gi 442622995 1340 MTKSDSKVF 1348
Cdd:COG3840 218 LDGEPPPAL 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
499-704 |
4.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSP--DYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVnGSLSYTSQ------- 569
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTskqkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 -------------ESWLFSGTVRQNILFGqPMDSQRYEEVVKKCALERdFDLLPLrDNTIVGERGATLSGGQKARISLAR 636
Cdd:PRK13643 81 pvrkkvgvvfqfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEK-LEMVGL-ADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 637 SVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
489-710 |
4.46e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.70 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 489 NNEADLLKSAISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SL 564
Cdd:PRK10790 331 NDDRPLQSGRIDIDNVSFAYRDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 565 SYTS---------QESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLA 635
Cdd:PRK10790 409 SHSVlrqgvamvqQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 636 RSVYRKASIYLLDDPLSAVDA----SVARHLfdQCVRGHlrgSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSgteqAIQQAL--AAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1117-1341 |
4.73e-17 |
|
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: 82.35 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:cd03295 1 IEFENVTKRYGGGKKA---VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYN--LDPfdeysdeKLWGCLEEvKLKEVVSDL-------PDGLASKISEggtNFSVGQRQLVCL 1265
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENiaLVP-------KLLKWPKE-KIRERADELlalvgldPAEFADRYPH---ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 ARAILRENRILVMDEATANVDPQTDGLIQ---ATIRSKFRDcTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1117-1312 |
6.47e-17 |
|
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: 79.51 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLrYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRdtrqmglhdlrRQI 1195
Cdd:cd03223 1 IELENLSL-ATPDGRV--LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGMPEG-----------EDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSGTmrynldpfdeysdeklwgcleevkLKEVVSdLPdglaskiseGGTNFSVGQRQLVCLARAILRENRI 1275
Cdd:cd03223 67 LFLPQRPYLPLGT------------------------LREQLI-YP---------WDDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 442622995 1276 LVMDEATANVDPQTDGLIQATIRSKFrdCTVLTIAHR 1312
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1117-1338 |
6.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENV-LKSLSFVIQPREKVGIVGRTGAGKSSLI---NALfrLSYTDGSVLIDTRD--TRQMGLHD 1190
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIqhlNGL--LKPTSGKIIIDGVDitDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEP--VLFSGTMR-------YNLDPFDEYSDEKLWGCLEEVKLKevVSDLPDglaskisEGGTNFSVGQRQ 1261
Cdd:PRK13637 81 IRKKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLD--YEDYKD-------KSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1262 LVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYE 1338
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
495-702 |
9.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLsYTSQESW-- 572
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 -------------LFSG-TVRQNILFGQPMDSQRYEEVVkkcalERDFDLLPLRDNTIVGERG-ATLSGGQKARISLARS 637
Cdd:PRK13650 80 rhkigmvfqnpdnQFVGaTVEDDVAFGLENKGIPHEEMK-----ERVNEALELVGMQDFKEREpARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 638 VYRKASIYLLDDPLSAVDASVARHLFdQCVRGhLR---GSTVVLVTHQEQFLPHVDQIVILANGQIKA 702
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELI-KTIKG-IRddyQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1117-1365 |
1.59e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtpNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS-YTDGSVLIDTRDTRQMGLHDLRRQI 1195
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPV-LFSG-TMRY--------NLDPFDEYSdEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCL 1265
Cdd:PRK13648 86 GIVFQNPDnQFVGsIVKYdvafglenHAVPYDEMH-RRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 ARAILRENRILVMDEATANVDPQTDGLIQATIR--SKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKS 1343
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
250 260 270
....*....|....*....|....*....|....
gi 442622995 1344 DS------------KVFHNLVNQSGRASYEGLLK 1365
Cdd:PRK13648 234 EEltrigldlpfpiKINQMLGHQTSFLTYEGLVD 267
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
499-699 |
2.37e-16 |
|
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: 77.10 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNspdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV--NGSLSYTSQeswlfsg 576
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 tvrqnilfgqpmdsqryeevvkkcalerdfdllplrdntivgergatLSGGQKARISLARSVYRKASIYLLDDP-----L 651
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPtnhldL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 652 SAVDAsvarhlfdqcVRGHLRG--STVVLVTHQEQFLPHV-DQIVILANGQ 699
Cdd:cd03221 104 ESIEA----------LEEALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
517-718 |
2.49e-16 |
|
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: 80.13 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQ-LQVNG-------------SLSYTSQE-SWLFSG--TVR 579
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSPAlQLRFPRdeTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNIL---FGQPMDSQRYEEVVKKCALE--RDFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:COG1119 99 DVVLsgfFDSIGLYREPTDEQRERAREllELLGLAHLADRPF-----GTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 655 DAsVARHLFDQCVRG--HLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLKTGLITGL 718
Cdd:COG1119 174 DL-GARELLLALLDKlaAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1135-1332 |
2.51e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQEPVLF------- 1205
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSgVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 ----------SGTMRYNldpfDEYSD-EKLwgcLEEVKL----KEVVSDLpdglaskiseggtnfSVGQRQLVCLARAIL 1270
Cdd:COG1129 99 niflgreprrGGLIDWR----AMRRRaREL---LARLGLdidpDTPVGDL---------------SVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1271 RENRILVMDEATANVDPQ-TDGLIqATIRsKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGRVVE 1332
Cdd:COG1129 157 RDARVLILDEPTASLTEReVERLF-RIIR-RLKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
517-683 |
2.62e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS----LSYTSQESWLfsG---------TVRQNIL 583
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYL--GhrnamkpalTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPMDSQRYEEVVKkcALERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD-ASVArhL 662
Cdd:PRK13539 96 FWAAFLGGEELDIAA--ALEA-VGLAPLAH-----LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDaAAVA--L 165
|
170 180
....*....|....*....|..
gi 442622995 663 FDQCVRGHL-RGSTVVLVTHQE 683
Cdd:PRK13539 166 FAELIRAHLaQGGIVIAATHIP 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
485-704 |
3.15e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 485 PPSNNNEADLLKSAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-S 563
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 564 LSYTSQE---------SW-LFSG-TVRQNILFGQPMDSQRYEEVVkkcalERDFDLLPL-RDNTIVGERGATLSGGQKAR 631
Cdd:PRK09452 78 ITHVPAEnrhvntvfqSYaLFPHmTVFENVAFGLRMQKTPAAEIT-----PRVMEALRMvQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 632 ISLARSVYRKASIYLLDDPLSAVDASVARHLfdQCVRGHLR---GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQM--QNELKALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
520-710 |
4.74e-16 |
|
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: 80.00 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------------SLSYTSQESWLFSG-TVRQN 581
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPHrTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFG---QPMDSQ----RYEEVVKKCALERDFDLLPlrdntivGErgatLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:cd03294 123 VAFGlevQGVPRAereeRAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 655 DASVARHLFDQCVRGHL-RGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:cd03294 192 DPLIRREMQDELLRLQAeLQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1135-1298 |
4.83e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 78.29 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGlHDLRRQISIIPQEPVLFSG-TMRYN 1212
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAgLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 LDpF------DEYSDEKLWGCLEEVKLKEVvSDLPDGlaskiseggtNFSVGQRQLVCLARAILRENRILVMDEATANVD 1286
Cdd:COG4133 96 LR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170
....*....|..
gi 442622995 1287 PQTDGLIQATIR 1298
Cdd:COG4133 164 AAGVALLAELIA 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
479-709 |
5.79e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 479 DTVPgNPPSNNNEAdlLKSAISIRDLKAKWDPNspdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQL 558
Cdd:PRK11607 3 DAIP-RPQAKTRKA--LTPLLEIRNLTKSFDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 559 QVNG-SLSYTS----------QESWLFSG-TVRQNILFGQPMDSQRYEEVVKKcaLERDFDLLPLRDntIVGERGATLSG 626
Cdd:PRK11607 77 MLDGvDLSHVPpyqrpinmmfQSYALFPHmTVEQNIAFGLKQDKLPKAEIASR--VNEMLGLVHMQE--FAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 627 GQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR-GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 442622995 705 DYESL 709
Cdd:PRK11607 233 EPEEI 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
511-697 |
6.65e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 511 NSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV---NGSLsYTSQESWLFSGTVRQNILFg 585
Cdd:cd03223 9 ATPDGRvlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLL-FLPQRPYLPLGTLREQLIY- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 qpmdsqryeevvkkcalerdfdllPLRDntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQ 665
Cdd:cd03223 87 ------------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|..
gi 442622995 666 CvrgHLRGSTVVLVTHQEQFLPHVDQIVILAN 697
Cdd:cd03223 134 L---KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
518-693 |
7.02e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 518 SGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL------SYTSQESWL--FSG-----TVRQNILF 584
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLghQPGiktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMdSQRYEEVVKKCALERdfdllplrdntiVGERG------ATLSGGQKARISLARSVYRKASIYLLDDPLSAVD-AS 657
Cdd:PRK13538 98 YQRL-HGPGDDEALWEALAQ------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkQG 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 442622995 658 VAR--HLFDQcvrgHL-RGSTVVLVTHQEqfLPHVDQIV 693
Cdd:PRK13538 165 VARleALLAQ----HAeQGGMVILTTHQD--LPVASDKV 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1151-1328 |
7.04e-16 |
|
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: 78.14 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1151 IVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDL----RRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLW 1225
Cdd:cd03290 32 IVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1226 GCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDGLIQATIRSKFRD- 1303
Cdd:cd03290 112 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDd 191
|
170 180
....*....|....*....|....*.
gi 442622995 1304 -CTVLTIAHRLHTIIDSDKVMVMDAG 1328
Cdd:cd03290 192 kRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1117-1351 |
7.34e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENV-LKSLSFVIQPREKVGIVGRTGAGKSSLI---NALfrLSYTDGSVLID----TRDTRQMGL 1188
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMqhfNAL--LKPSSGTITIAgyhiTPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1189 HDLRRQISIIPQ--EPVLFSGTM-------RYNLDPFDEYSDEKLWGCLEEVKLKEVVsdlpdglaskISEGGTNFSVGQ 1259
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVlkdvefgPKNFGFSEDEAKEKALKWLKKVGLSEDL----------ISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1260 RQLVCLARAILRENRILVMDEATANVDPQTdgliQATIRSKFRDC-----TVLTIAHRLHTIID-SDKVMVMDAGRVVEF 1333
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKH 226
|
250
....*....|....*...
gi 442622995 1334 GSPYELMTKSDSKVFHNL 1351
Cdd:PRK13641 227 ASPKEIFSDKEWLKKHYL 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
517-700 |
7.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.40 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSlSYTSQ--------------------ESWLFSG 576
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDT-LITSTsknkdikqirkkvglvfqfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGqPMDSQRYEEVVKKCALERdFDLLPLRDNtIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDA 656
Cdd:PRK13649 102 TVLKDVAFG-PQNFGVSQEEAEALAREK-LALVGISES-LFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442622995 657 SVARHLFDQCVRGHLRGSTVVLVTH-QEQFLPHVDQIVILANGQI 700
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
497-703 |
1.03e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.64 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV-----NGSLSYTSQES 571
Cdd:PRK11264 2 SAIEVKNLVKKFHGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 572 ----------WLFSG-------TVRQNILFG------QPMDS--QRYEEVVKKCALERDFDLLPLRdntivgergatLSG 626
Cdd:PRK11264 79 lirqlrqhvgFVFQNfnlfphrTVLENIIEGpvivkgEPKEEatARARELLAKVGLAGKETSYPRR-----------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 627 GQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-------DQIVILANGQ 699
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVadraifmDQGRIVEQGP 227
|
....
gi 442622995 700 IKAL 703
Cdd:PRK11264 228 AKAL 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
517-717 |
1.07e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSYTS---------QESWL-FSGTVRQNI 582
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveALSARAasrrvasvpQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQPMDSQRY-------EEVVKKcALER-DFDLLPLRDNTivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:PRK09536 99 EMGRTPHRSRFdtwtetdRAAVER-AMERtGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 655 DAS-------VARHLFDQcvrghlrGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLKTGLITG 717
Cdd:PRK09536 171 DINhqvrtleLVRRLVDD-------GKTAVAAIHDlDLAARYCDELVLLADGRVRAAGPPADVLTADTLRA 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1136-1341 |
1.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSL---INALFRLSytDGSVLIDTRDTRQMG-LHDLRRQISIIPQEP-VLFSG-TM 1209
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ--KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFVGrTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 RYNLdpfdEYSDEKLwgCLEEVKLKEVVS-DLPD-GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:PRK13644 96 EEDL----AFGPENL--CLPPIEIRKRVDrALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1288 QTDGLIQATIRSKFRDC-TVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1140-1340 |
1.25e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.78 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLRRQISIIPQEPvlFSgtmryNLDP 1215
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLeEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YA-----SLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1216 -----------FDEYSDEKLWGCLEEVK-LKEVVsdlpdGLASKIS-----EggtnFSVGQRQLVCLARAILRENRILVM 1278
Cdd:COG4608 111 rmtvgdiiaepLRIHGLASKAERRERVAeLLELV-----GLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1279 DEATANVDPQtdglIQATIRSKFRD------CTVLTIAHRL----HTiidSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLsvvrHI---SDRVAVMYLGKIVEIAPRDELY 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1135-1341 |
1.26e-15 |
|
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: 78.20 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDG-SVLIDTRDTRQMGLHDLRRQISII---------PQEPV 1203
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGnDVRLFGERRGGEDVWELRKRIGLVspalqlrfpRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 L------FSGTmrynLDPFDEYSDEklwgclEEVKLKEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILV 1277
Cdd:COG1119 98 LdvvlsgFFDS----IGLYREPTDE------QRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1278 MDEATANVDPQTDGLIQATIR--SKFRDCTVLTIAHRLHTIIDS-DKVMVMDAGRVVEFGSPYELMT 1341
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDklAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
498-700 |
1.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKAKWDPNSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------- 562
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 ------SLSYTSQESWLFSGTVRQNILFGqPMDSQRYEEVVKKCALE--RDFDLlplrDNTIVGERGATLSGGQKARISL 634
Cdd:PRK13641 82 klrkkvSLVFQFPEAQLFENTVLKDVEFG-PKNFGFSEDEAKEKALKwlKKVGL----SEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 635 ARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1136-1339 |
1.86e-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: 77.02 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLID----TRDTRqmglhDLRRQISIIPQEPVLFSG-TM 1209
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAghdvVREPR-----EVRRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 RYNLdpfdeYSDEKLWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:cd03265 91 WENL-----YIHARLYG-VPGAERRERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1288 QTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03265 165 QTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
517-707 |
2.13e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV--NGSLSYTSQESWLFSG--TVRQNILFGQPMDSQR 592
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHQEELDPdkTVLDELRDGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 593 Y------------EEVVKKCalerdfdllplrdntivgergATLSGGQKARISLARSVYRKASIYLLDDP--------LS 652
Cdd:COG0488 411 EvrgylgrflfsgDDAFKPV---------------------GVLSGGEKARLALAKLLLSPPNVLLLDEPtnhldietLE 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 653 AVDASVARhlFDqcvrGhlrgsTVVLVTHQEQFLPHV-DQIVILANGQIKA-LGDYE 707
Cdd:COG0488 470 ALEEALDD--FP----G-----TVLLVSHDRYFLDRVaTRILEFEDGGVREyPGGYD 515
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
517-705 |
2.53e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSYTS------------QESWLFSG-TVR 579
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltALSERElraarrkigmifQHFNLLSSrTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFgqPMdsqRYEEVVKKCALERDFDLLPLrdntiVG--ERG----ATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:COG1135 101 ENVAL--PL---EIAGVPKAEIRKRVAELLEL-----VGlsDKAdaypSQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 654 VD----ASVARHLFDqcVRGHLrGSTVVLVTHQeqflPHV-----DQIVILANGQIKALGD 705
Cdd:COG1135 171 LDpettRSILDLLKD--INREL-GLTIVLITHE----MDVvrricDRVAVLENGRIVEQGP 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
517-682 |
2.61e-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: 75.99 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESW----LFSG---------TVRQNIL 583
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIarglLYLGhapgikttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPM-DSQRYEEVVKKCALeRDFDLLPLrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVD-ASVARh 661
Cdd:cd03231 96 FWHADhSDEQVEEALARVGL-NGFEDRPV----------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkAGVAR- 163
|
170 180
....*....|....*....|..
gi 442622995 662 lFDQCVRGHL-RGSTVVLVTHQ 682
Cdd:cd03231 164 -FAEAMAGHCaRGGMVVLTTHQ 184
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
848-1090 |
2.80e-15 |
|
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: 78.03 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 848 ILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAG 927
Cdd:cd18559 49 ILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 928 IIIVIANVNPLLLVpTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQD 1007
Cdd:cd18559 129 LYLLILLAGPMAAV-GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1008 aHSSAFFMYISTSQAFGYCMNCICVIYISIITLSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERV 1087
Cdd:cd18559 208 -NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVS 286
|
...
gi 442622995 1088 VEY 1090
Cdd:cd18559 287 LER 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
517-708 |
2.89e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--SLSYTSQESWLFSG-TVRQNILFG-QPMDS-- 590
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGdAELRAle 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 591 QRYEEVVKKCA-----------LERDFDL------------------LPLRD-NTIVGErgatLSGGQKARISLARSVYR 640
Cdd:COG0488 94 AELEELEAKLAepdedlerlaeLQEEFEAlggweaearaeeilsglgFPEEDlDRPVSE----LSGGWRRRVALARALLS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 641 KASIYLLDDP---LsavDA-SVARhlfdqcVRGHLRG--STVVLVTHQEQFLPHV-DQIVILANGQIKA-LGDYES 708
Cdd:COG0488 170 EPDLLLLDEPtnhL---DLeSIEW------LEEFLKNypGTVLVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSA 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1117-1334 |
3.23e-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: 76.25 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRLSytDGSVLIDTRDTRQMGLhDLRR 1193
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTtlrMLAGLLEPD--AGFATVDGFDVVKEPA-EARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLFSG-TMRYNLDPFdeysdEKLWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAIL 1270
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEYF-----AGLYG-LKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1271 RENRILVMDEATANVD-PQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFG 1334
Cdd:cd03266 153 HDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1140-1341 |
3.45e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.54 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLIN--ALFrLSYTDGSVLIDTRDTRQMGlhDLRRQISIIPQEPVLFSG-TMRYN---- 1212
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTTP--PSRRPVSMLFQENNLFSHlTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 LDP---FDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDP-- 1287
Cdd:PRK10771 96 LNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1288 --QTDGLIQATIRSkfRDCTVLTIAHRLHtiiDSDKV----MVMDAGRVVEFGSPYELMT 1341
Cdd:PRK10771 165 rqEMLTLVSQVCQE--RQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1122-1332 |
3.47e-15 |
|
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: 76.32 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1122 LNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQM---GLHDLRRQ-IS 1196
Cdd:COG4181 14 LTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGQDLFALdedARARLRARhVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1197 IIPQ-EPVLFSGTMRYNL----------DPFDEYSDEklwgcLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCL 1265
Cdd:COG4181 94 FVFQsFQLLPTLTALENVmlplelagrrDARARARAL-----LERVGLGHRLDHYPAQL-----------SGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1266 ARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRD--CTVLTIAHRLHTIIDSDKVMVMDAGRVVE 1332
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
499-709 |
3.59e-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: 76.25 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------SLSY 566
Cdd:cd03265 1 IEVENLVKKYGDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 567 TSQESWLFSG-TVRQNI-----LFGQPMD--SQRYEEVVKKcalerdFDLLPLRDntivgERGATLSGGQKARISLARSV 638
Cdd:cd03265 78 VFQDLSVDDElTGWENLyiharLYGVPGAerRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 639 YRKASIYLLDDPLSAVDASVARHLFD---QCVRGHlrGSTVVLVTH----QEQFlphVDQIVILANGQIKALGDYESL 709
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEyieKLKEEF--GMTILLTTHymeeAEQL---CDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1105-1344 |
4.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1105 KKPPKtwPEQGEIIFKELNLRYTPNAKAENVLKSL---SFVIQPREKVGIVGRTGAGKSSLI---NALFRLSYTD---GS 1175
Cdd:PRK13631 10 LKVPN--PLSDDIILRVKNLYCVFDEKQENELVALnniSYTFEKNKIYFIIGNSGSGKSTLVthfNGLIKSKYGTiqvGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1176 VLI--DTRDTRQMGLHD---------LRRQISIIPQEP--VLFSGTMR-------YNLDPFDEYSDEKLWGCLEEVKLKE 1235
Cdd:PRK13631 88 IYIgdKKNNHELITNPYskkiknfkeLRRRVSMVFQFPeyQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1236 VVSDL-PDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDG-LIQATIRSKFRDCTVLTIAHRL 1313
Cdd:PRK13631 168 SYLERsPFGL-----------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTM 236
|
250 260 270
....*....|....*....|....*....|..
gi 442622995 1314 HTIID-SDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:PRK13631 237 EHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1140-1331 |
4.80e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLINALFRLsY--TDGSVLIDTRDTRQMGLHD-LRRQISIIPQEPVLF----------- 1205
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGL-YqpDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVpnltvaenivl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 --SGTMRYNLDP------FDEYSDE-KLwgcleEVKLKEVVSDLpdglaskiseggtnfSVGQRQLVCLARAILRENRIL 1276
Cdd:COG3845 104 glEPTKGGRLDRkaararIRELSERyGL-----DVDPDAKVEDL---------------SVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1277 VMDEATANVDPQ-TDGLIqATIRsKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:COG3845 164 ILDEPTAVLTPQeADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1117-1344 |
4.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNaKAENVLKSLSFVIQPREKVGIVGRTGAGKSS---LINALfrLSYTDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:PRK13650 5 IEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGL--LEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEP-VLFSGTMrynldpfdeYSDEKLWGcLEE--VKLKEVVSDLPDGLASKiseGGTNF--------SVGQRQL 1262
Cdd:PRK13650 82 KIGMVFQNPdNQFVGAT---------VEDDVAFG-LENkgIPHEEMKERVNEALELV---GMQDFkereparlSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1263 VCLARAILRENRILVMDEATANVDPQTD-GLIQA--TIRSKFrDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYEL 1339
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
....*
gi 442622995 1340 MTKSD 1344
Cdd:PRK13650 228 FSRGN 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
499-700 |
7.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.65 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWdpnsPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-LSYTSQ------ 569
Cdd:PRK13639 2 LETRDLKYSY----PDGTeaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYDKKsllevr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 570 ----------ESWLFSGTVRQNILFGqPMD--------SQRYEEVVKKCALErDFDLLPLRDntivgergatLSGGQKAR 631
Cdd:PRK13639 78 ktvgivfqnpDDQLFAPTVEEDVAFG-PLNlglskeevEKRVKEALKAVGME-GFENKPPHH----------LSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 632 ISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLP-HVDQIVILANGQI 700
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1147-1331 |
9.27e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.84 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1147 EKVGIVGRTGAGKSSLIN--ALFRLSyTDGSVLIDTRDTRQMGLHDlrRQISIIPQEPVLFSG-TMRYNLD----P---F 1216
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNliAGFETP-QSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGlglsPglkL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1217 DEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDP-QTDGLIQ- 1294
Cdd:cd03298 102 TAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPaLRAEMLDl 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 442622995 1295 -ATIRSKfRDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:cd03298 171 vLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1115-1339 |
1.01e-14 |
|
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: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYtpnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRD-TrqmGLHDLR 1192
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLeDPTSGEILIGGRDvT---DLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLF-SGTMRYNL--------DPFDEYsDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLV 1263
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIafplklrkVPKAEI-DRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQtdglIQATIRSKFRdctvltiahRLH-----TII----D-------SDKVMVMDA 1327
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIK---------RLHrrlgtTTIyvthDqveamtlADRIAVMND 209
|
250
....*....|..
gi 442622995 1328 GRVVEFGSPYEL 1339
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1117-1342 |
1.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAEN--VLKSLSFVIQPREKVGIVGRTGAGKSSL---INALfrLSYTDGSVLIDTRDTRQMG-LHD 1190
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL--LIPSEGKVYVDGLDTSDEEnLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEP------------VLFsGTMRYNLDPfdEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVG 1258
Cdd:PRK13633 83 IRNKAGMVFQNPdnqivativeedVAF-GPENLGIPP--EEIRERVDESLKKVGMYEYRRHAPHLL-----------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1259 QRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIR--SKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSP 1336
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
....*.
gi 442622995 1337 YELMTK 1342
Cdd:PRK13633 229 KEIFKE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1140-1344 |
1.23e-14 |
|
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: 77.06 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLINAL----------FRLsytDGSVLIDTRDTRQMGLHdlRRQISIIPQEPVLFSG-T 1208
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdsgrIRL---GGEVLQDSARGIFLPPH--RRRIGYVFQEARLFPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 MRYNLdpfdEYSDEKLWGCLEEVKLKEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1288
Cdd:COG4148 94 VRGNL----LYGRKRAPRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1289 TDGLIQ---ATIRSKFrDCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:COG4148 168 RKAEILpylERLRDEL-DIPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
520-708 |
1.40e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL-----------------SYTSQESWLFSG-TVRQN 581
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFPHyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFG-QPMDSQRYEEVVKKCALERDFDLLPLrdntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:PRK11144 97 LRYGmAKSMVAQFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 661 HL--FDQCVRGHLRgSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYES 708
Cdd:PRK11144 166 ELlpYLERLAREIN-IPILYVSHSlDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1135-1346 |
1.61e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 74.50 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHD-LRRQISIIPQEPVLFSG-TMRY 1211
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDsGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFDE--YSDEKLWgcleEVKLKEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1289
Cdd:cd03218 95 NILAVLEirGLSKKER----EEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1290 DGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSDSK 1346
Cdd:cd03218 169 VQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
496-713 |
1.84e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGsLSYTSQESW--- 572
Cdd:PRK13635 3 EEIIRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 ------------LFSG-TVRQNILF-----GQPMDS--QRYEEVVKKCALERDFDLLPLRdntivgergatLSGGQKARI 632
Cdd:PRK13635 81 rqvgmvfqnpdnQFVGaTVQDDVAFgleniGVPREEmvERVDQALRQVGMEDFLNREPHR-----------LSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 633 SLARSVYRKASIYLLDDPLSAVDA-------SVARHLFDQcvrghlRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGD 705
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPrgrrevlETVRQLKEQ------KGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
....*...
gi 442622995 706 YESLLKTG 713
Cdd:PRK13635 224 PEEIFKSG 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1113-1340 |
1.84e-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: 77.92 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1113 EQGEIIFKELNLRYTPNAKAENVLK---SLSFVIQPREKVGIVGRTGAGKSSLINAL------------FRL-----SYT 1172
Cdd:TIGR03269 274 EVGEPIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsgevnVRVgdewvDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1173 DGSVLIDTRDTRQMGLhdLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCL-----EEVKLKEVVSDLPDGLask 1247
Cdd:TIGR03269 354 KPGPDGRGRAKRYIGI--LHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLkmvgfDEEKAEEILDKYPDEL--- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1248 iseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATI---RSKFRDcTVLTIAHRLHTIID-SDKVM 1323
Cdd:TIGR03269 429 --------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAA 499
|
250
....*....|....*..
gi 442622995 1324 VMDAGRVVEFGSPYELM 1340
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEIV 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
517-700 |
2.19e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS-------------QESWLFSG-TVRQN 581
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGePVRFRSprdaqaagiaiihQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQP------MDSQRYEEVVKKcALER-DFDLLPlrdNTIVGErgatLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:COG1129 100 IFLGREprrgglIDWRAMRRRARE-LLARlGLDIDP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 655 DASVARHLFDQcVRgHLR--GSTVVLVTHqeqFLPHV----DQIVILANGQI 700
Cdd:COG1129 172 TEREVERLFRI-IR-RLKaqGVAIIYISH---RLDEVfeiaDRVTVLRDGRL 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
498-715 |
2.32e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.16 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKAKWdpnsPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESW--- 572
Cdd:PRK13647 4 IIEVEDLHFRY----KDGTkaLKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 ------------LFSGTVRQNILFG---QPMDSQRYEEVVKKcALeRDFDLLPLRDNTivgerGATLSGGQKARISLARS 637
Cdd:PRK13647 80 kvglvfqdpddqVFSSTVWDDVAFGpvnMGLDKDEVERRVEE-AL-KAVRMWDFRDKP-----PYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 638 VYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQF-LPHVDQIVILANGQIKALGDYESLLKTGLI 715
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1132-1341 |
2.60e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1132 AENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS------YTDGSVLIDTRDT-RQMGLHDLRRQISIIPQEPVL 1204
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgyRYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 F---------SGTMRYNLDPFDEYSDeklwgcLEEVKLKEVvsDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRI 1275
Cdd:PRK14271 113 FpmsimdnvlAGVRAHKLVPRKEFRG------VAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1276 LVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1120-1339 |
3.44e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYtpNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS------YTDGSVLIDTRD--TRQMGLHDL 1191
Cdd:PRK14239 9 SDLSVYY--NKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpevTITGSIVYNGHNiySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 RRQISIIPQEPVLFsgtmrynldPFDEYSDE----KLWGCLEEVKLKEVV------SDLPDGLASKISEGGTNFSVGQRQ 1261
Cdd:PRK14239 85 RKEIGMVFQQPNPF---------PMSIYENVvyglRLKGIKDKQVLDEAVekslkgASIWDEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1262 LVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
517-704 |
3.52e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.08 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS---------LSYTSQESWLFSGTVRQNIL--FG 585
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLYPKMKVIDQLvyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 QPMDSQRYEevVKKCA---LERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAsVARHL 662
Cdd:cd03269 96 QLKGLKKEE--ARRRIdewLER-LELSEYAN-----KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442622995 663 FDQCVRGHLR-GSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:cd03269 167 LKDVIRELARaGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1132-1332 |
3.65e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1132 AENVLKSLSFVIQPREKVGIVGRTGAGKSSLINAL------------FR---LSYTDGSVLIDTRDTRQMGLHDL----- 1191
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLvglespsqgnvsWRgepLAKLNRAQRKAFRRDIQMVFQDSisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 -RRQISIIPQEPvlfsgtMRYNLDPFDEYSDEKLWGCLEEVklkevvsDLPDGLASKISEggtNFSVGQRQLVCLARAIL 1270
Cdd:PRK10419 104 pRKTVREIIREP------LRHLLSLDKAERLARASEMLRAV-------DLDDSVLDKRPP---QLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1271 RENRILVMDEATANVDPqtdgLIQATI-------RSKFrDCTVLTIAHRLHTIID-SDKVMVMDAGRVVE 1332
Cdd:PRK10419 168 VEPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
517-700 |
3.82e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV-NGSLSYTSQESWLfsgtvrqniLFgqpmdsqryee 595
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgTAPLAEAREDTRL---------MF----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 596 vvkkcaleRDFDLLPLR---DNTIVGERG-----------------------ATLSGGQKARISLARSVYRKASIYLLDD 649
Cdd:PRK11247 88 --------QDARLLPWKkviDNVGLGLKGqwrdaalqalaavgladranewpAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 650 PLSAVDAsVAR----HLFDQCVRGHlrGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:PRK11247 160 PLGALDA-LTRiemqDLIESLWQQH--GFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1116-1344 |
4.72e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1116 EIIFKELNLRYTPNAKAEN-VLKSLSFVIQPREKVGIVGRTGAGKSSLI---NALfrLSYTDGSVLIDTR----DTRQMG 1187
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERrALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlNGL--LQPTSGTVTIGERvitaGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1188 LHDLRRQISIIPQ--EPVLFSGTMR-------YNLDPFDEYSDEKLWGCLEEVKLKEVVSDL-PDGLaskiseggtnfSV 1257
Cdd:PRK13634 80 LKPLRKKVGIVFQfpEHQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLARsPFEL-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1258 GQRQLVCLARAILRENRILVMDEATANVDPQTdgliQATIRSKF------RDCTVLTIAHRLHTIID-SDKVMVMDAGRV 1330
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
250
....*....|....
gi 442622995 1331 VEFGSPYELMTKSD 1344
Cdd:PRK13634 225 FLQGTPREIFADPD 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
517-700 |
5.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.05 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGsLSYTSQ--------------------ESWLFSG 576
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD-ITITHKtkdkyirpvrkrigmvfqfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGqPMDSQRYEEVVKKCALERDFDLLPLRDntIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDA 656
Cdd:PRK13646 102 TVEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 657 SVARHLFDQCVRGHL-RGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:PRK13646 179 QSKRQVMRLLKSLQTdENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1134-1347 |
6.77e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1134 NVLKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRlsYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEP-VLFSGTM 1209
Cdd:PRK13642 21 NQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 RYNLDPFDEYSDeklwGCLEEVKLKEVVSDLpdgLASKISEGGTN----FSVGQRQLVCLARAILRENRILVMDEATANV 1285
Cdd:PRK13642 99 VEDDVAFGMENQ----GIPREEMIKRVDEAL---LAVNMLDFKTReparLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1286 DPQTDGLIQATI---RSKFRdCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDSKV 1347
Cdd:PRK13642 172 DPTGRQEIMRVIheiKEKYQ-LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
517-704 |
9.32e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.84 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGsVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS------------LSYTSQESWLFSG-TVR---- 579
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEFGVYPNfTVRefld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 -QNILFGQPmDSQRYEEVVKkcALERdFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAsV 658
Cdd:cd03264 95 yIAWLKGIP-SKEVKARVDE--VLEL-VNLGDRAK-----KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-E 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 659 ARHLFdqcvRGHLR----GSTVVLVTHQ-EQFLPHVDQIVILANGQIKALG 704
Cdd:cd03264 165 ERIRF----RNLLSelgeDRIVILSTHIvEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1127-1331 |
1.18e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.81 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1127 TPNAKaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINAL---FRLsyTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPV 1203
Cdd:COG1101 15 TVNEK--RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIagsLPP--DSGSILIDGKDVTKLPEYKRAKYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 ------------------------LFSGTMRYNLDPFDEYsdeklwgcLEEVKLkevvsDLPDGLASKISeggtNFSVGQ 1259
Cdd:COG1101 91 mgtapsmtieenlalayrrgkrrgLRRGLTKKRRELFREL--------LATLGL-----GLENRLDTKVG----LLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1260 RQLVCLARAILRENRILVMDEATANVDPQTDGLI-QAT---IRSKfrDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlELTekiVEEN--NLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
499-704 |
1.25e-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: 71.63 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDL-KAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQESW---- 572
Cdd:cd03266 2 ITADALtKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 LFSG--------TVRQNI-----LFGQPMDS--QRYEEVVKKcalerdFDLLPLRDntivgERGATLSGGQKARISLARS 637
Cdd:cd03266 82 FVSDstglydrlTARENLeyfagLYGLKGDEltARLEELADR------LGMEELLD-----RRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 638 VYRKASIYLLDDPLSAVDASVARHLFDqcVRGHLR--GSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALRE--FIRQLRalGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
497-700 |
1.27e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 71.70 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDL-KAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIqAILGEL-KANSGQLQVNG-SLSYTSQE--- 570
Cdd:COG4181 7 PIIELRGLtKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAGLdRPTSGTVRLAGqDLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 571 -------SWLF-------SGTVRQNI-----LFGQPMDSQRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKAR 631
Cdd:COG4181 86 rlrarhvGFVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYP-----------AQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 632 ISLARSVYRKASIYLLDDPLSAVDASVARH----LFDQCVRghlRGSTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQiidlLFELNRE---RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
517-715 |
1.37e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN--------SGQLQVNGS----------------LSYTSQESW 572
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplaaidaprlarlravLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 LFSgtVRQNILFGQPMDSQRYEEV------VKKCALER-DFDLLPLRDNTivgergaTLSGGQKARISLARSV------- 638
Cdd:PRK13547 97 AFS--AREIVLLGRYPHARRAGALthrdgeIAWQALALaGATALVGRDVT-------TLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 639 --YRKASIYLLDDPLSAVDASVARHLFDQcVRGHLRGST--VVLVTHQEQFLP-HVDQIVILANGQIKALGDYESLLKTG 713
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDT-VRRLARDWNlgVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLTPA 246
|
..
gi 442622995 714 LI 715
Cdd:PRK13547 247 HI 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
511-719 |
1.44e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.71 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 511 NSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----------------SLSYTSQESW 572
Cdd:PRK13644 10 SYPDGTpaLENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgirklvGIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 LFSGTVRQNILFGQ------PMD-SQRYEEVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIY 645
Cdd:PRK13644 90 FVGRTVEEDLAFGPenlclpPIEiRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 646 LLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTGLITGLG 719
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
499-707 |
2.20e-13 |
|
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: 70.25 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGelkaNSGQLQVNGSLsytsqeswLFSGtv 578
Cdd:cd03217 1 LEIKDLHVSVGGKE---ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEI--------LFKG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 rQNILFGQP---------MDSQRYEEV--VKKcaleRDFdllpLRDntiVGErgaTLSGGQKARISLARSVYRKASIYLL 647
Cdd:cd03217 64 -EDITDLPPeerarlgifLAFQYPPEIpgVKN----ADF----LRY---VNE---GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 648 DDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV--DQIVILANGQIKALGDYE 707
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
496-681 |
2.20e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWdpNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS----------LS 565
Cdd:PRK15056 4 QAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 566 YTSQES---WLFSGTVRQNILFGQ-----------PMDSQRYEEvvkkcALERdFDLLPLRDNTIvGErgatLSGGQKAR 631
Cdd:PRK15056 82 YVPQSEevdWSFPVLVEDVVMMGRyghmgwlrrakKRDRQIVTA-----ALAR-VDMVEFRHRQI-GE----LSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 632 ISLARSVYRKASIYLLDDPLSAVDASVARHLFDqcVRGHLR--GSTVVLVTH 681
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIIS--LLRELRdeGKTMLVSTH 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
517-700 |
2.21e-13 |
|
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: 70.37 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANsgqLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEV 596
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN---VSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 VKKCAlerDFDLLpLRDNTIVgeRGatLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHlFDQCVR--GHLRGS 674
Cdd:cd03233 100 VRETL---DFALR-CKGNEFV--RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE-ILKCIRtmADVLKT 170
|
170 180 190
....*....|....*....|....*....|..
gi 442622995 675 TVVLVTHQ------EQFlphvDQIVILANGQI 700
Cdd:cd03233 171 TTFVSLYQasdeiyDLF----DKVLVLYEGRQ 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
495-700 |
2.71e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILG------------ELKANSgqLQVNG 562
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ---ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshiELLGRT--VQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 SLSYTSQESWLFSG------------TVRQNILFGQPMDSQRYEEVVKkcALERDFDLLPLRDNTIVG------ERGATL 624
Cdd:PRK09984 76 RLARDIRKSRANTGyifqqfnlvnrlSVLENVLIGALGSTPFWRTCFS--WFTREQKQRALQALTRVGmvhfahQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 625 SGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQcvrghLR------GSTVVLVTHQEQF-LPHVDQIVILAN 697
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDT-----LRdinqndGITVVVTLHQVDYaLRYCERIVALRQ 228
|
...
gi 442622995 698 GQI 700
Cdd:PRK09984 229 GHV 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1344 |
2.72e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLinalFR-----LSYTDGSVLIDTRDTRQMGLHDLRRQ 1194
Cdd:PRK13652 7 RDLCYSYSGSKEA---LNNINFIAPRNSRIAVIGPNGAGKSTL----FRhfngiLKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEP--VLFSGTMRY-------NLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCL 1265
Cdd:PRK13652 80 VGLVFQNPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 ARAILRENRILVMDEATANVDPQTDGLIQATIR--SKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNdlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
..
gi 442622995 1343 SD 1344
Cdd:PRK13652 229 PD 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
517-704 |
2.83e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQ--------------------LQVNGSLSYTSQESWLFSG 576
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkikevkrLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPlRDntIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDA 656
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP-ED--YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 657 SVAR---HLFDQCVRGHlrGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALG 704
Cdd:PRK13645 184 KGEEdfiNLFERLNKEY--KKRIIMVTHNmDQVLRIADEVIVMHEGKVISIG 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
511-700 |
2.92e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 511 NSPDYT--LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-----------------LSYTSQES 571
Cdd:PRK13636 14 NYSDGThaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresvgMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 572 WLFSGTVRQNILFGqPMDSQRYEEVVKK---CALERDfDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLD 648
Cdd:PRK13636 94 QLFSASVYQDVSFG-AVNLKLPEDEVRKrvdNALKRT-GIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 649 DPLSAVD---ASVARHLFDQCVRGhlRGSTVVLVTHQEQFLP-HVDQIVILANGQI 700
Cdd:PRK13636 167 EPTAGLDpmgVSEIMKLLVEMQKE--LGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1135-1335 |
3.15e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLID-----TRDTRQMglHDLRRQISIIPQEP------- 1202
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDgqplhNLNRRQL--LPVRHRIQVVFQDPnsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1203 -----VLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKevvsdlPDGLASKISEggtnFSVGQRQLVCLARAILRENRILV 1277
Cdd:PRK15134 379 lnvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1278 MDEATANVDPQTDGLIQATIRS---KFRdCTVLTIAHRLHtIIDS--DKVMVMDAGRVVEFGS 1335
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSlqqKHQ-LAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGD 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
498-700 |
3.16e-13 |
|
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: 69.38 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKAKwdpnspdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGslsytsqeswlfsgt 577
Cdd:cd03215 4 VLEVRGLSVK-------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 578 vrQNILFGQPMDSQRyeevvKKCAL---ERD----FDLLPLRDNTIVGERgatLSGG--QKarISLARSVYRKASIYLLD 648
Cdd:cd03215 62 --KPVTRRSPRDAIR-----AGIAYvpeDRKreglVLDLSVAENIALSSL---LSGGnqQK--VVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 649 DPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1135-1341 |
3.41e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQ----EPVLfsgTMR 1210
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQfdnlDPDF---TVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1211 YNLDPFDEYsdeklWGcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQ 1288
Cdd:PRK13537 99 ENLLVFGRY-----FG-LSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1289 TDGLIQATIRSKF-RDCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK13537 173 ARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
517-695 |
3.46e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LSYTSQESWLFSGTVRQNIL 583
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPMDSQRYEEVVKKCALERdFDLlplrDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLF 663
Cdd:PRK10247 103 FPWQIRNQQPDPAIFLDDLER-FAL----PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 442622995 664 D---QCVRGHlrGSTVVLVTHQEQFLPHVDQIVIL 695
Cdd:PRK10247 178 EiihRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1135-1339 |
3.91e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.44 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINAL--FrLSYTDGSVLIDTRDtrqmgLHDL---RRQISIIPQEPVLFSgtm 1209
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF-ETPDSGRILLDGRD-----VTGLppeKRNVGMVFQDYALFP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 ryNLDPFD-------------EYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRIL 1276
Cdd:COG3842 91 --HLTVAEnvafglrmrgvpkAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1277 VMDEATANVDPQTDGLIQATIRSKFRDC--TVLTIAHrlhtiiD-------SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
520-704 |
4.42e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-----------SLSYTSQESWLFSG-TVRQNILFGQP 587
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaerGVGMVFQSYALYPHlSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 MDSQRYEEVVKKcaLERDFDLLPLrdNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCV 667
Cdd:PRK11000 102 LAGAKKEEINQR--VNQVAEVLQL--AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 442622995 668 RGHLR-GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK11000 178 RLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-700 |
4.93e-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: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPD--YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQE----- 570
Cdd:COG1101 2 LELKNLSKTFNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 571 -SWLF---------SGTVRQNIL----------FGQPMDSQRYEEVVKKCAlerDFDL-LPLRDNTIVGergaTLSGGQK 629
Cdd:COG1101 82 iGRVFqdpmmgtapSMTIEENLAlayrrgkrrgLRRGLTKKRRELFRELLA---TLGLgLENRLDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 630 ARISLARSVYRKASIYLLDDPLSAVDASVAR---HLFDQCVRGHlrGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAAlvlELTEKIVEEN--NLTTLMVTHNmEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
499-709 |
5.25e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSpdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------- 563
Cdd:PRK13652 4 IETRDLCYSYSGSK--EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 564 LSYTSQESWLFSGTVRQNILFGqPMD--------SQRYEEVVKKCALERDFDLLPLRdntivgergatLSGGQKARISLA 635
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 636 RSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR-GSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESL 709
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
499-707 |
6.47e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPD--YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQV----NG---------- 562
Cdd:PRK13631 22 LRVKNLYCVFDEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 -----------------SLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCA--LER---DFDLLplrdntivgER 620
Cdd:PRK13631 102 npyskkiknfkelrrrvSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKfyLNKmglDDSYL---------ER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 621 GA-TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANG 698
Cdd:PRK13631 173 SPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKG 252
|
250
....*....|
gi 442622995 699 QIKALGD-YE 707
Cdd:PRK13631 253 KILKTGTpYE 262
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
517-699 |
7.36e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANS--GQLQVNGS---------LSYTSQESWLFSG-TVRQNILF 584
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqilkrTGFVTQDDILYPHlTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMDSQR-YEEVVKKCALERDFDLLPLR--DNTIVGE---RGatLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:PLN03211 164 CSLLRLPKsLTKQEKILVAESVISELGLTkcENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442622995 659 ARHLFDQCVRGHLRGSTVVLVTHQ--EQFLPHVDQIVILANGQ 699
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGR 284
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1140-1342 |
7.94e-13 |
|
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: 70.37 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLRRQ-ISIIPQEPVLFSG-TMRYNL 1213
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1214 dpfdEYSDEkLWGCLEEVKLK---EVVS--DLPDGLASKISEggtnFSVGQRQLVCLARAILRENRILVMDEATANVDPq 1288
Cdd:cd03294 124 ----AFGLE-VQGVPRAEREEraaEALElvGLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP- 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1289 tdgLIQATIRSKFRDC------TVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:cd03294 194 ---LIRREMQDELLRLqaelqkTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
845-1087 |
7.98e-13 |
|
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: 70.66 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:cd07346 47 LLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVNP----LLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAInrspVYSHLAASLNGLTTIRALDAQRVLEK 1000
Cdd:cd07346 127 LIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVRESLAE----LSAFLQESLSGIRVVKAFAAEEREIE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1001 EFDSYQDAHSSAFFMYISTSQAFGYCMNCICVIyISIITLSFFAFPPGNGA-DVGlVITQAMGLIDMVQWGVRQTAELEN 1079
Cdd:cd07346 203 RFREANRDLRDANLRAARLSALFSPLIGLLTAL-GTALVLLYGGYLVLQGSlTIG-ELVAFLAYLGMLFGPIQRLANLYN 280
|
250
....*....|..
gi 442622995 1080 T----MTAVERV 1087
Cdd:cd07346 281 QlqqaLASLERI 292
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
515-710 |
8.52e-13 |
|
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: 72.66 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQ--LQVNGSLSYTSQESWL-FSGTVRQNILFG---QPM 588
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarPQPGIKVGYLPQEPQLdPTKTVRENVEEGvaeIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 589 DSQRYEEVVKKCALE-RDFDLLPLR----------------DNTIvgERGA-------------TLSGGQKARISLARSV 638
Cdd:TIGR03719 99 ALDRFNEISAKYAEPdADFDKLAAEqaelqeiidaadawdlDSQL--EIAMdalrcppwdadvtKLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 639 YRKASIYLLDDPLSAVDA-SVA---RHLFDqcvrghLRGsTVVLVTHQEQFLPHVDQ-IVILANGQ-IKALGDYESLL 710
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAeSVAwleRHLQE------YPG-TVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSWL 247
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1116-1339 |
9.66e-13 |
|
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: 69.29 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1116 EIIFKELNLRYtPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDlrRQ 1194
Cdd:cd03296 2 SIEVRNVSKRF-GDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPVQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1195 ISIIPQEPVLFSG-TMRYNL-----------DPFDEYSDEKLWGCLEEVKLkevvsdlpDGLASKISeggTNFSVGQRQL 1262
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQL--------DWLADRYP---AQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1263 VCLARAILRENRILVMDEATANVDPQTDGLIQATIRsKFRD---CTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYE 1338
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLR-RLHDelhVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDE 223
|
.
gi 442622995 1339 L 1339
Cdd:cd03296 224 V 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1344 |
1.06e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTR--DTRQMGLHDLRRQIS 1196
Cdd:PRK13636 9 EELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1197 IIPQEP--VLFSGTMrynldpFDEYSDEKLWGCLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAILRE 1272
Cdd:PRK13636 86 MVFQDPdnQLFSASV------YQDVSFGAVNLKLPEDEVRKRVDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1273 NRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTI-IDSDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
517-700 |
1.27e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQaILGEL-KANSGQLQVNG---------SLSYTSQESWLF---------SGT 577
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGqdvatldadALAQLRREHFGFifqryhllsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 578 VRQNILFgqpmdSQRYEEVVKKCALERDFDLLP---LRDNtiVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:PRK10535 103 AAQNVEV-----PAVYAGLERKQRLLRAQELLQrlgLEDR--VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 655 DA----SVARHLFDQCVRGHlrgsTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:PRK10535 176 DShsgeEVMAILHQLRDRGH----TVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
517-710 |
1.47e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.23 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------------------LSYTSQE 570
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadknqlrllrtrLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 571 SWLFSG-TVRQNILfGQPMDSQRYEEVVKKCALERDFDLLPLrDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDD 649
Cdd:PRK10619 101 FNLWSHmTVLENVM-EAPIQVLGLSKQEARERAVKYLAKVGI-DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 650 PLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVI-LANGQIKALGDYESLL 710
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIfLHQGKIEEEGAPEQLF 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1132-1341 |
1.61e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1132 AENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSG-TM 1209
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 R----YNLDPFDeysdeKLWGCLEEVKLKEVVSDLP----DGLASKISeggTNFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:PRK11231 94 RelvaYGRSPWL-----SLWGRLSAEDNARVNQAMEqtriNHLADRRL---TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1282 TANVDPQTdgliQATIRSKFRDC-----TVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK11231 166 TTYLDINH----QVELMRLMRELntqgkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1117-1342 |
2.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRLSYTDGSVL-IDTRDTRQMGLHDLR 1192
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKItVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEP-VLFSGTMrynldpfdeYSDEKLWGcLE-----EVKLKEVVSD-LPD-GLASKISEGGTNFSVGQRQLVC 1264
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGAT---------VGDDVAFG-LEnravpRPEMIKIVRDvLADvGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1265 LARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTK 1342
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
517-743 |
2.53e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTSQESWLFSG-TVRQN 581
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQP---MDSQRYEEVVKKCALERDFDLLplrdntivgerGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:PRK15439 107 ILFGLPkrqASMQKMKQLLAALGCQLDLDSS-----------AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 659 ARHLFDQcVRGHL-RGSTVVLVTHQeqfLPHV----DQIVILANGQIKALGDYESLLKTGLITGLGSLSKTDKAkTEEQE 733
Cdd:PRK15439 176 TERLFSR-IRELLaQGVGIVFISHK---LPEIrqlaDRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKSL-SASQK 250
|
250
....*....|
gi 442622995 734 pLNLNSPDNK 743
Cdd:PRK15439 251 -LWLELPGNR 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1135-1342 |
2.88e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINAL--------------FRLSYTD--GSVLIDTRDTRQMGL---------- 1188
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHVALCEkcGYVERPSKVGEPCPVcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1189 ----------HDLRRQISIIPQEPVLFSGTMRYnLD------PFDEYSDEKLWGclEEVKLKEVVSdlpdgLASKISEGG 1252
Cdd:TIGR03269 95 dfwnlsdklrRRIRKRIAIMLQRTFALYGDDTV-LDnvlealEEIGYEGKEAVG--RAVDLIEMVQ-----LSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1253 TNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--KFRDCTVLTIAHRLHTIID-SDKVMVMDAGR 1329
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|...
gi 442622995 1330 VVEFGSPYELMTK 1342
Cdd:TIGR03269 247 IKEEGTPDEVVAV 259
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1113-1352 |
2.93e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1113 EQGEIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS-------YTDGSVLIDTRDTRQ 1185
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKA--ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1186 MGLHDLRRQISIIPQEPVLFSgtmryNLDPFDEYSDE-KLWGCLEEVKLKEVVSD------LPDGLASKISEGGTNFSVG 1258
Cdd:PRK14246 83 IDAIKLRKEVGMVFQQPNPFP-----HLSIYDNIAYPlKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1259 QRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPY 1337
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*
gi 442622995 1338 ELMTKSDSKVFHNLV 1352
Cdd:PRK14246 238 EIFTSPKNELTEKYV 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
517-700 |
3.22e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------------SLSYTSQESWLFSG-TVRQN 581
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQPM-DSQRYEEvvkkcALERDFDLLP-LRDNTIvgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVA 659
Cdd:PRK11614 101 LAMGGFFaERDQFQE-----RIKWVYELFPrLHERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 660 RHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQI 700
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNaNQALKLADRGYVLENGHV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1134-1341 |
3.25e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1134 NVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLiDTRDTRQMGLHDLRRQ---ISIIPQEPVLFSG-TM 1209
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-EIGGNPCARLTPAKAHqlgIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 RYNLD---PFDEYSDEKLwgcleEVKLKEVVSDL-PDGLASKISeggtnfsVGQRQLVCLARAILRENRILVMDEATANV 1285
Cdd:PRK15439 104 KENILfglPKRQASMQKM-----KQLLAALGCQLdLDSSAGSLE-------VADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1286 DP-QTDGLIQaTIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK15439 172 TPaETERLFS-RIRElLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1135-1311 |
3.90e-12 |
|
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: 67.46 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRlSY--TDGSVLIDTRDT---------RQMglHDLRRQ--------I 1195
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYlpDSGSILVRHDGGwvdlaqaspREI--LALRRRtigyvsqfL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQ--------EPVLFSGTM-------------RYNLdpfdeysDEKLWgcleevklkevvsDLPDglaskiseggTN 1254
Cdd:COG4778 103 RVIPRvsaldvvaEPLLERGVDreearararellaRLNL-------PERLW-------------DLPP----------AT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1255 FSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAH 1311
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEaKARGTAIIGIFH 210
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1120-1335 |
4.08e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRY-TPNAKAENVlKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL----SYTDGSVLIDTRDTRQMGLHDLRR- 1193
Cdd:PRK09473 16 KDLRVTFsTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaanGRIGGSATFNGREILNLPEKELNKl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 ---QISIIPQEPVLfsgtmryNLDPFDEYSDE------------KLWGCLEEVKLKEVVSdLPDglASK-ISEGGTNFSV 1257
Cdd:PRK09473 95 raeQISMIFQDPMT-------SLNPYMRVGEQlmevlmlhkgmsKAEAFEESVRMLDAVK-MPE--ARKrMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1258 GQRQLVCLARAILRENRILVMDEATANVDPQtdglIQATI-------RSKFrDCTVLTIAHRLHTIIDS-DKVMVMDAGR 1329
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQImtllnelKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGR 239
|
....*.
gi 442622995 1330 VVEFGS 1335
Cdd:PRK09473 240 TMEYGN 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
517-704 |
4.60e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN---SGQLQVNG---------SLSYTSQESWLFSG--TVRQNI 582
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemrAISAYVQQDDLFIPtlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQPMDSQR-YEEVVKKCALERDFDLLPLRD--NTIVGERGAT--LSGGQKARISLARSVYRKASIYLLDDPLSAVDAS 657
Cdd:TIGR00955 121 MFQAHLRMPRrVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 658 VARHLFdQCVRG-HLRGSTVVLVTHQ------EQFlphvDQIVILANGQIKALG 704
Cdd:TIGR00955 201 MAYSVV-QVLKGlAQKGKTIICTIHQpsselfELF----DKIILMAEGRVAYLG 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1131-1346 |
5.24e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1131 KAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHD-LRRQISIIPQEPVLFSGT 1208
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 MRYN-----LDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskisegGTNFSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:PRK10895 94 SVYDnlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1284 NVDPQTDGLIQATIRsKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSDSK 1346
Cdd:PRK10895 167 GVDPISVIDIKRIIE-HLRDsgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1135-1341 |
5.33e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.49 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINAL-FRLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVL---FSGTM- 1209
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAInGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 --------RYNLDPFDEYSDEKLWGCLEEVklkevvsdlpdGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:PRK09536 98 vemgrtphRSRFDTWTETDRAAVERAMERT-----------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1282 TANVD----PQTDGLIQATIRSkfrDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK09536 167 TASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
515-699 |
6.06e-12 |
|
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: 67.43 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGS-----VVAVIGLTGSGKSSLIQAILGELKANSGQLQV-NGSLSYTSQE-SWLFSGTVRQ---NILF 584
Cdd:cd03237 8 KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQYiKADYEGTVRDllsSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 585 GQPMDSQRYEEVVKkcalerdfdllPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD-------AS 657
Cdd:cd03237 88 DFYTHPYFKTEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 658 VARHLFDQcvrghlRGSTVVLVTHQEQFLPHVDQIVILANGQ 699
Cdd:cd03237 157 VIRRFAEN------NEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1117-1330 |
6.42e-12 |
|
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: 66.40 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAkaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLID----TRDTRQmgLHDL 1191
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIIIDglklTDDKKN--INEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 RRQISIIPQEPVLFS----------GTMRYNLDPFDEySDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQ 1261
Cdd:cd03262 75 RQKVGMVFQQFNLFPhltvlenitlAPIKVKGMSKAE-AEERALELLEKVGLADKADAYPAQL-----------SGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1262 LVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRD-CTVLTIAHRLHTIID-SDKVMVMDAGRV 1330
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
517-715 |
6.46e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-------------SLSYTSQESWLFSG-TVRQNI 582
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQ-PMD------SQRYEEVVKKcALERdfdllpLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:PRK11231 98 AYGRsPWLslwgrlSAEDNARVNQ-AMEQ------TRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 656 ASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLKTGLI 715
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTVLHDlNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1131-1341 |
6.84e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1131 KAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD------GSVLIDTRD--TRQMGL-HDLRRQISIIPQE 1201
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDTARslSQQKGLiRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 pvlfsgtmrYNLDPFDEYSDEKLWGCL--------EEVKL-KEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILRE 1272
Cdd:PRK11264 94 ---------FNLFPHRTVLENIIEGPVivkgepkeEATARaRELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1273 NRILVMDEATANVDPQTDGLIQATIRSKFRDC-TVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
517-700 |
7.72e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----SLSytSQE---------------SWLFSGT 577
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltALS--EKElrkarrqigmifqhfNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 578 VRQNILFGQPMDSQRYEEVVKKCAlerdfDLLPLrdntiVG--ERG----ATLSGGQKARISLARSVYRKASIYLLDDPL 651
Cdd:PRK11153 99 VFDNVALPLELAGTPKAEIKARVT-----ELLEL-----VGlsDKAdrypAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 652 SAVDASVARHLFDQcvrghLR------GSTVVLVTHQEQFLPHV-DQIVILANGQI 700
Cdd:PRK11153 169 SALDPATTRSILEL-----LKdinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRL 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1136-1340 |
8.72e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.12 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTrQMGLHDLRRQ-ISIIPQEPV---------- 1203
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAgMIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 -LFSGTMRYNLDPFDEYSDEKLWGCLEEVKLK-EVVSDLPDGLASkiseggtnfsvGQRQLVCLARAILRENRILVMDEA 1281
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1282 TANVDpqtdgliqATIRSKFRDCTV-LTIAHRLHTII----------DSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:PRK15112 177 LASLD--------MSMRSQLINLMLeLQEKQGISYIYvtqhlgmmkhISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1135-1340 |
1.03e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSV-LIDTRDTRQMGLhdLRRQISIIPQEPVL-FSGTMRY 1211
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDaGKItVLGVPVPARARL--ARARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFDEYSDeklwgcLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1289
Cdd:PRK13536 134 NLLVFGRYFG------MSTREIEAVIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1290 DGLIQATIRSKF-RDCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFGSPYELM 1340
Cdd:PRK13536 208 RHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1129-1330 |
1.25e-11 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 64.76 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1129 NAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQepvlfs 1206
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLrPPASGEITLDGKPVTRRSPRDAIRAgIAYVPE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1207 gtmrynldpfdeysDEKLWGCLEEVKLKEVVSdLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVD 1286
Cdd:cd03215 83 --------------DRKREGLVLDLSVAENIA-LSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442622995 1287 PQTDGLIQATIRsKFRD--CTVLTIAHRLHTIID-SDKVMVMDAGRV 1330
Cdd:cd03215 137 VGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
517-681 |
1.35e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 65.82 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLfsgtVRQNILFGQ---------P 587
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL----RRIGVVFGQktqlwwdlpV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 MDS------------QRYEEVVKKCAlerdfDLLPLRDntIVGERGATLSGGQKARISLARSVYRKASIYLLDDP---LS 652
Cdd:cd03267 113 IDSfyllaaiydlppARFKKRLDELS-----ELLDLEE--LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPtigLD 185
|
170 180
....*....|....*....|....*....
gi 442622995 653 AVDASVARHLFDQCVRghLRGSTVVLVTH 681
Cdd:cd03267 186 VVAQENIRNFLKEYNR--ERGTTVLLTSH 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1115-1341 |
1.37e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1115 GEIIFKELNLRYTPNAKAE-NVLKSLSFVIQPREKVGIVGRTGAGKSSLINalfrlsYTDGSVLIDTRDT---------- 1183
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEfKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQ------LTNGLIISETGQTivgdyaipan 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1184 --RQMGLHDLRRQISIIPQEP--VLFSGTMRYNL--DPFDEYSDEklwgclEEV--KLKEVVS--DLPDGLASKiseGGT 1253
Cdd:PRK13645 79 lkKIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENK------QEAykKVPELLKlvQLPEDYVKR---SPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1254 NFSVGQRQLVCLARAILRENRILVMDEATANVDPQ-TDGLIQATIR-SKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRV 1330
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKV 229
|
250
....*....|.
gi 442622995 1331 VEFGSPYELMT 1341
Cdd:PRK13645 230 ISIGSPFEIFS 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1122-1335 |
2.05e-11 |
|
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: 68.17 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1122 LNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-----SYTDGSVLIDTRDTRQMGLHDLRR--- 1193
Cdd:COG4172 12 LSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 -QISIIPQEPvlfsgtMRyNLDPF--------------DEYSDEKLWG----CLEEVKLKEVvsdlpdglASKISEGGTN 1254
Cdd:COG4172 92 nRIAMIFQEP------MT-SLNPLhtigkqiaevlrlhRGLSGAAARAraleLLERVGIPDP--------ERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1255 FSVGQRQLVCLARAILRENRILVMDEatanvdPQT--DGLIQATIRSKFRDCT------VLTIAHRLHTIID-SDKVMVM 1325
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADE------PTTalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRRfADRVAVM 230
|
250
....*....|
gi 442622995 1326 DAGRVVEFGS 1335
Cdd:COG4172 231 RQGEIVEQGP 240
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
843-1087 |
2.08e-11 |
|
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: 66.26 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 843 YTLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIA 922
Cdd:cd18544 47 YLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 923 LWLAGIIIVIANVNP------LLLVPTLMLSVIFYhlRNLYLKTSRDL-KRVEAINrspvySHLAASLNGLTTIRALDAQ 995
Cdd:cd18544 127 LLLIGILIAMFLLNWrlalisLLVLPLLLLATYLF--RKKSRKAYREVrEKLSRLN-----AFLQESISGMSVIQLFNRE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 996 RVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCICVIYISIItLSFFAFPPGNGA-DVGLVITQAMgLIDMVQWGVRQT 1074
Cdd:cd18544 200 KREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALV-LWYGGGQVLSGAvTLGVLYAFIQ-YIQRFFRPIRDL 277
|
250
....*....|....*..
gi 442622995 1075 AE----LENTMTAVERV 1087
Cdd:cd18544 278 AEkfniLQSAMASAERI 294
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1121-1356 |
2.68e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1121 ELNLRYtpnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSL-INALFRLSYTDGSVLIDTR--DTRQMGLHDLRRQISI 1197
Cdd:PRK13638 6 DLWFRY----QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1198 IPQEP---VLFSgtmryNLDPFDEYSDEKLwGCLEEvklkEVVSDLPDGLASKISEGGTN-----FSVGQRQLVCLARAI 1269
Cdd:PRK13638 82 VFQDPeqqIFYT-----DIDSDIAFSLRNL-GVPEA----EITRRVDEALTLVDAQHFRHqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1270 LRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTI-AHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSDskv 1347
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE--- 228
|
....*....
gi 442622995 1348 fhnLVNQSG 1356
Cdd:PRK13638 229 ---AMEQAG 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
517-705 |
3.02e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.90 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-LSYTSQ--------ESWLFSG-TVRQNIL-FG 585
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpLDPEDRrrigylpeERGLYPKmKVGEQLVyLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 586 Q--PMDSQRYEEVVKKcALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAsVARHLF 663
Cdd:COG4152 97 RlkGLSKAEAKRRADE-WLER-LGLGDRANKKV-----EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442622995 664 DQCVRGH-LRGSTVVLVTHQeqfLPHV----DQIVILANGQIKALGD 705
Cdd:COG4152 169 KDVIRELaAKGTTVIFSSHQ---MELVeelcDRIVIINKGRKVLSGS 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1123-1336 |
3.76e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 63.70 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSY--TDGSVLIDTRDTRQMGLHD-LRRQISII 1198
Cdd:cd03217 5 DLHVSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYevTEGEILFKGEDITDLPPEErARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1199 PQEPVLFSGtmrynldpfdeysdeklwgcleeVKLKEVVSDLPDGlaskiseggtnFSVGQRQLVCLARAILRENRILVM 1278
Cdd:cd03217 83 FQYPPEIPG-----------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1279 DEATANVDPQTDGLIQATIRS-KFRDCTVLTIAH--RLHTIIDSDKVMVMDAGRVVEFGSP 1336
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1122-1350 |
3.82e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1122 LNLRYTPNakaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL------SYTDGSVLIDTRD--TRQMGLHDLRR 1193
Cdd:PRK14267 10 LRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneeARVEGEVRLFGRNiySPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEPVLFSGTMRY----------NLDPFDEYSDEKLWGCLEEVKLKEVVSDlpdglasKISEGGTNFSVGQRQLV 1263
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYdnvaigvklnGLVKSKKELDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHR-LHTIIDSDKVMVMDAGRVVEFGsPYElmtk 1342
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG-PTR---- 233
|
....*...
gi 442622995 1343 sdsKVFHN 1350
Cdd:PRK14267 234 ---KVFEN 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
517-711 |
4.10e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS------------LSYTSQESWL-FSGTVRQNIL 583
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDNLdLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 -FGQ--PMDSQRYEEVVKKCAlerDFDLLPLRDNTivgeRGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASvAR 660
Cdd:PRK13536 137 vFGRyfGMSTREIEAVIPSLL---EFARLESKADA----RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 661 HLFDQCVRGHL-RGSTVVLVTH-QEQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHfMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1117-1344 |
4.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLI---NALFRLSytDGSVLIDTRDTRQMGLHDLRR 1193
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLPQ--RGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEP--VLFSGTMR-------YNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVC 1264
Cdd:PRK13647 80 KVGLVFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1265 LARAILRENRILVMDEATANVDPQ-TDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPyELMTK 1342
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRgQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
..
gi 442622995 1343 SD 1344
Cdd:PRK13647 228 ED 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1136-1340 |
4.60e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLRRQ--------ISIIPQEPV 1203
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 LFSGTMRYNLDPFD-EYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEAT 1282
Cdd:PRK10070 124 LDNTAFGMELAGINaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1283 ANVDPQTDGLIQ---ATIRSKFRDcTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELM 1340
Cdd:PRK10070 193 SALDPLIRTEMQdelVKLQAKHQR-TIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
523-681 |
4.60e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 523 EIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQE-SWLFSGTVRQnILFGQP---MDSQRYEEVVK 598
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYiKPDYDGTVED-LLRSITddlGSSYYKSEIIK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 599 KCALERDFDlLPLRDntivgergatLSGGQKARISLARSVYRKASIYLLDDPLSAVD-------ASVARHLFDQcvrghl 671
Cdd:PRK13409 440 PLQLERLLD-KNVKD----------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------ 502
|
170
....*....|
gi 442622995 672 RGSTVVLVTH 681
Cdd:PRK13409 503 REATALVVDH 512
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1129-1349 |
4.79e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1129 NAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTRDTRQMGLHDLRR-------QISIIPQE 1201
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARhraylsqQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 PVlFSGTMRYNLDPFDEYSDEKLwgcleevkLKEVVSDLpdGLASKISEGGTNFSVGQRQLVCLARAILR-------ENR 1274
Cdd:PRK03695 85 PV-FQYLTLHQPDKTRTEAVASA--------LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1275 ILVMDEATANVDPQTDGLIQATIRskfRDC----TVLTIAHRL-HTIIDSDKVMVMDAGRVVEFGSPYELMTKSD-SKVF 1348
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPENlAQVF 230
|
.
gi 442622995 1349 H 1349
Cdd:PRK03695 231 G 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1135-1334 |
5.13e-11 |
|
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: 63.81 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDlrRQISIIPQEPVLFS-----GT 1208
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPhmtvyDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 MRYNLD----PFDEYsDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATAN 1284
Cdd:cd03301 93 IAFGLKlrkvPKDEI-DERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1285 VDpqtdgliqATIRSKFRdcTVLTIAHRLH--TII----D-------SDKVMVMDAGRVVEFG 1334
Cdd:cd03301 161 LD--------AKLRVQMR--AELKRLQQRLgtTTIyvthDqveamtmADRIAVMNDGQIQQIG 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
523-653 |
5.58e-11 |
|
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: 67.12 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 523 EIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQE-SWLFSGTVRQNI--LFGQPMDSQRYE-EVVK 598
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFGSSYYKtEIIK 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 599 KCALERDFDlLPLRDntivgergatLSGGQKARISLARSVYRKASIYLLDDPlSA 653
Cdd:COG1245 442 PLGLEKLLD-KNVKD----------LSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
845-1332 |
6.29e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.75 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADM-HFFSINKHgSILNRFTKDM---SQVDEVLPVVLVDVMQ 920
Cdd:COG4615 56 GLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLeRLERIGAA-RLLAALTEDVrtiSQAFVRLPELLQSVAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 921 IAlwlaGIIIVIANVNPLLLVPT---LMLSVIFYHLrnLYLKTSRDLKRV-EAINRspVYSHLAASLNGLTTIRaLDAQR 996
Cdd:COG4615 135 VL----GCLAYLAWLSPPLFLLTlvlLGLGVAGYRL--LVRRARRHLRRArEAEDR--LFKHFRALLEGFKELK-LNRRR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 997 ---VLEKEF----DSYQDaHSSAFFMYISTSQAFGYCMncicvIYIsIITLSFFAFP---PGNGADVG---LVITQAMGL 1063
Cdd:COG4615 206 rraFFDEDLqptaERYRD-LRIRADTIFALANNWGNLL-----FFA-LIGLILFLLPalgWADPAVLSgfvLVLLFLRGP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1064 IDMVqwgVRQTAELENTMTAVERVVEYESIEPEGMLEAPDDKKPPktWPEQgeiiFKEL---NLRYT-PNAKAEN--VLK 1137
Cdd:COG4615 279 LSQL---VGALPTLSRANVALRKIEELELALAAAEPAAADAAAPP--APAD----FQTLelrGVTYRyPGEDGDEgfTLG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1138 SLSFVIQPREKVGIVGRTGAGKSSLINALFRLsYT--DGSVLID----TRDTRQmglhDLRRQISIIPQEPVLFsgtmRY 1211
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGL-YRpeSGEILLDgqpvTADNRE----AYRQLFSAVFSDFHLF----DR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFDEYSDEKLWGCLEEVKLKEVVSdlpdglaskISEGG---TNFSVGQRQLVCLARAILrENR-ILVMDEATANVDP 1287
Cdd:COG4615 421 LLGLDGEADPARARELLERLELDHKVS---------VEDGRfstTDLSQGQRKRLALLVALL-EDRpILVFDEWAADQDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1288 QtdgliqatirskFRDC--------------TVLTIAHrlhtiiD------SDKVMVMDAGRVVE 1332
Cdd:COG4615 491 E------------FRRVfytellpelkargkTVIAISH------DdryfdlADRVLKMDYGKLVE 537
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
520-705 |
6.86e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAI-LGELkANSGQLQVNGS---LSYTSQES----------WLFSG-------TV 578
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEM-PRSGTLNIAGNhfdFSKTPSDKairelrrnvgMVFQQynlwphlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 RQNiLFGQPMdsqRYEEVVKKCALERDFDLLP-LRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS 657
Cdd:PRK11124 100 QQN-LIEAPC---RVLGLSKDQALARAEKLLErLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442622995 658 VARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGD 705
Cdd:PRK11124 176 ITAQIVSIIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGD 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1117-1372 |
7.47e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAK-AENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSV----LIDTRDTRQMGLHD 1190
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNgLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 LRRQISIIPQEP--VLFSGTMRYnldpfDEYSDEKLWGCLEEVKLKEVVSDLPD-GLASKISEGGT-NFSVGQRQLVCLA 1266
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLK-----DVAFGPQNFGIPKEKAEKIAAEKLEMvGLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDC-TVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVD 236
|
250 260
....*....|....*....|....*...
gi 442622995 1345 SKVFHNLVNQSGRASYEGLLKIAQETFE 1372
Cdd:PRK13643 237 FLKAHELGVPKATHFADQLQKTGAVTFE 264
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
499-711 |
8.05e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.72 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSPDY--TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQ----------------- 559
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 560 ----VNGSLSYTSQ------------------ESWLFSGTVRQNILFGqPMDSQryeeVVKKCALERDFDLLPLrdntiV 617
Cdd:PRK13651 83 vlekLVIQKTRFKKikkikeirrrvgvvfqfaEYQLFEQTIEKDIIFG-PVSMG----VSKEEAKKRAAKYIEL-----V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 618 G------ERGA-TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHV 689
Cdd:PRK13651 153 GldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWT 232
|
250 260
....*....|....*....|..
gi 442622995 690 DQIVILANGQIKALGDYESLLK 711
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILS 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1123-1349 |
1.03e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1123 NLRYTPNAKAenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQE 1201
Cdd:PRK13548 7 NLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 PVL-FSGT----MRYNLDPFDEYSDEKlwGCLEEVKLKEVvsDLpDGLASKiseggtNF---SVGQRQLVCLARAILR-- 1271
Cdd:PRK13548 85 SSLsFPFTveevVAMGRAPHGLSRAED--DALVAAALAQV--DL-AHLAGR------DYpqlSGGEQQRVQLARVLAQlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1272 ----ENRILVMDEATANVDP--QTDGLIQATIRSKFRDCTVLTIAHRLH-TIIDSDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLahQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
....*.
gi 442622995 1345 -SKVFH 1349
Cdd:PRK13548 234 lRRVYG 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
517-699 |
1.04e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQESWLFSG--------------TVRQN 581
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQ-PM-----DSQRYEEVVKKCALERDFDLLPlrdntivGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:PRK10982 94 MWLGRyPTkgmfvDQDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442622995 656 ASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQ 699
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
520-712 |
1.07e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-LSYTS----------QESWLFSG-TVRQNILFGQP 587
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdVTHRSiqqrdicmvfQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 MDSQRYEEVVK--KCALERdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLfdq 665
Cdd:PRK11432 105 MLGVPKEERKQrvKEALEL-VDLAGFEDRYV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM--- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 666 cvRGHLR------GSTVVLVTH-QEQFLPHVDQIVILANGQIKALGDYESLLKT 712
Cdd:PRK11432 176 --REKIRelqqqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
496-711 |
1.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWDPNSPdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLsyTSQESWL-- 573
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--ISKENLKei 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 574 --------------FSG-TVRQNILFG--------QPMDsQRYEEVVKKCALERDFDLLPLrdntivgergaTLSGGQKA 630
Cdd:PRK13632 82 rkkigiifqnpdnqFIGaTVEDDIAFGlenkkvppKKMK-DIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 631 RISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGS-TVVLVTHQEQFLPHVDQIVILANGQIKALGDYESL 709
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
..
gi 442622995 710 LK 711
Cdd:PRK13632 230 LN 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1109-1339 |
1.10e-10 |
|
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: 64.11 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1109 KTWPEQGEIIFKELNLRYTPnakaenVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVlidtrdtRQMG 1187
Cdd:cd03291 32 KHSSDDNNLFFSNLCLVGAP------VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKI-------KHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1188 lhdlrrQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLAR 1267
Cdd:cd03291 99 ------RISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLAR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1268 AILRENRILVMDEATANVDPQTDGLIqatirskFRDCTVLTIAHRLHTIIDS--------DKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLDVFTEKEI-------FESCVCKLMANKTRILVTSkmehlkkaDKILILHEGSSYFYGTFSEL 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1134-1334 |
1.16e-10 |
|
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: 62.68 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1134 NVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIdtrDTRQMGLHDlRRQISIIPQEPVLfsgtmryn 1212
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDsGEVLF---DGKPLDIAA-RNRIGYLPEERGL-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1213 ldpfdeYSDEKL------WGCLEEVKLKEVVSDLPD-----GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:cd03269 82 ------YPKMKVidqlvyLAQLKGLKKEEARRRIDEwlerlELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 1282 TANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFG 1334
Cdd:cd03269 156 FSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1120-1334 |
1.16e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1120 KELNLRYTPNAKAENVlkslSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTRQMGLHD-------- 1190
Cdd:PRK11701 10 RGLTKLYGPRKGCRDV----SFDLYPGEVLGIVGESGSGKTTLLNALSaRLAPDAGEVHYRMRDGQLRDLYAlseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1191 ----------------LRRQIS----IipQEPVLFSGTMRYNlDPFDEYSDeklWgcLEEVKLKEV-VSDLPdglaskis 1249
Cdd:PRK11701 86 llrtewgfvhqhprdgLRMQVSaggnI--GERLMAVGARHYG-DIRATAGD---W--LERVEIDAArIDDLP-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1250 eggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQtdglIQAT----IRSKFRD--CTVLTIAH-----RLHtiid 1318
Cdd:PRK11701 150 ---TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARlldlLRGLVRElgLAVVIVTHdlavaRLL---- 218
|
250
....*....|....*.
gi 442622995 1319 SDKVMVMDAGRVVEFG 1334
Cdd:PRK11701 219 AHRLLVMKQGRVVESG 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1135-1339 |
1.19e-10 |
|
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: 63.02 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHdlRRQISIIPQEPVLFSgtmryNL 1213
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTsGEILLDGKDITNLPPH--KRPVNTVFQNYALFP-----HL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1214 DPFDEYS-------------DEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDE 1280
Cdd:cd03300 88 TVFENIAfglrlkklpkaeiKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1281 ATANVDPQTDGLIQATIRsKFRDCTVLTIAHRLH----TIIDSDKVMVMDAGRVVEFGSPYEL 1339
Cdd:cd03300 157 PLGALDLKLRKDMQLELK-RLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1135-1282 |
1.28e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDtRDTRqmglhdlrrqISIIPQEPVLFSGT----- 1208
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIP-KGLR----------IGYLPQEPPLDDDLtvldt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 ------------MRYN-----LDPFDEYSDE--KLWGCLE-------EVKLKEVVSDL---PDGLASKISEggtnFSVGQ 1259
Cdd:COG0488 82 vldgdaelraleAELEeleakLAEPDEDLERlaELQEEFEalggweaEARAEEILSGLgfpEEDLDRPVSE----LSGGW 157
|
170 180
....*....|....*....|...
gi 442622995 1260 RQLVCLARAILRENRILVMDEAT 1282
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
516-684 |
1.28e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 516 TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAI--LGELKAN---SGQLQVNGSLSYTS---------------QESWLFS 575
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPrtdtvdlrkeigmvfQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNILFGQPM----DSQRYEEVVKKcalerdfdllPLRDNTI---VGER----GATLSGGQKARISLARSVYRKASI 644
Cdd:PRK14239 100 MSIYENVVYGLRLkgikDKQVLDEAVEK----------SLKGASIwdeVKDRlhdsALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442622995 645 YLLDDPLSAVDASVARHLfDQCVRGHLRGSTVVLVTHQEQ 684
Cdd:PRK14239 170 ILLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1147-1350 |
1.29e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1147 EKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMG---LHDLRRQISIIPQEPvLFSGTMRYNL-----DPFD 1217
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLvKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMTIgeiiaEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1218 EYSDEKlwgCLEEVK--LKEV---VSDLPDglasKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQtdgl 1292
Cdd:PRK15079 127 TYHPKL---SRQEVKdrVKAMmlkVGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS---- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1293 IQATIRSKFRDC------TVLTIAHRLHTI--IdSDKVMVMDAGRVVEFGspyelmtkSDSKVFHN 1350
Cdd:PRK15079 196 IQAQVVNLLQQLqremglSLIFIAHDLAVVkhI-SDRVLVMYLGHAVELG--------TYDEVYHN 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
495-700 |
1.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSlSYTSQESW-- 572
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 --------------LFSGTVRQNILFGQPMDSQRYEEVVKKCalerDFDLLPLRDNTIVGERGATLSGGQKARISLARSV 638
Cdd:PRK13642 80 rrkigmvfqnpdnqFVGATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 639 YRKASIYLLDDPLSAVD----ASVARHLFDQCVRGHLrgsTVVLVTHQEQFLPHVDQIVILANGQI 700
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL---TVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
517-701 |
2.54e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQE---------------SWLFSGTV-- 578
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEaraklrakhvgfvfqSFMLIPTLna 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 RQNI-----LFGQPMDSQRYE--EVVKKCALERDFDLLPlrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPL 651
Cdd:PRK10584 106 LENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 652 SAVDAS----VARHLFDQcvrGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIK 701
Cdd:PRK10584 175 GNLDRQtgdkIADLLFSL---NREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
491-709 |
3.91e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.19 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 491 EADLLKSAISIRDLKA-KWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS 568
Cdd:PRK15079 10 EVADLKVHFDIKDGKQwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 QESWLfsgTVRQNI--LFGQP------------------------MDSQRYEEVVKkcALERDFDLLPLRDNTIVGErga 622
Cdd:PRK15079 90 DDEWR---AVRSDIqmIFQDPlaslnprmtigeiiaeplrtyhpkLSRQEVKDRVK--AMMLKVGLLPNLINRYPHE--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 623 tLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFD--QCVRGHLrGSTVVLVTHQEQFLPHV-DQIVILANGQ 699
Cdd:PRK15079 162 -FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHIsDRVLVMYLGH 239
|
250
....*....|
gi 442622995 700 IKALGDYESL 709
Cdd:PRK15079 240 AVELGTYDEV 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
517-689 |
4.22e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSG--QLQVNGSLSYTSQESWL-FSGTVRQNIL--FGQPMDSQ 591
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeaRPAPGIKVGYLPQEPQLdPEKTVRENVEegVAEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 592 -RYEEVVKKCALE-RDFDLLPLR----------------DNTIvgERGA-------------TLSGGQKARISLARSVYR 640
Cdd:PRK11819 103 dRFNEIYAAYAEPdADFDALAAEqgelqeiidaadawdlDSQL--EIAMdalrcppwdakvtKLSGGERRRVALCRLLLE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 641 KASIYLLDDPLSAVDA-SVA---RHLFDqcvrghLRGsTVVLVTHQEQFLPHV 689
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAeSVAwleQFLHD------YPG-TVVAVTHDRYFLDNV 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-692 |
4.61e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAiLGELKANSGQLQVNGSLSYTSQESW-- 572
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 -------------------LFSGTVRQNILFGQPMDSQR----YEEVVKKCAleRDFDLLPLRDNTIvGERGATLSGGQK 629
Cdd:PRK14258 80 rvnlnrlrrqvsmvhpkpnLFPMSVYDNVAYGVKIVGWRpkleIDDIVESAL--KDADLWDEIKHKI-HKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 630 ARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGS-TVVLVTHQeqfLPHVDQI 692
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN---LHQVSRL 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1136-1334 |
5.78e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVL------IDTRDTRQmgLHDLRRQISIIPQEPVLfsgtm 1209
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqrIDTLSPGK--LQALRRDIQFIFQDPYA----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 ryNLDPFDEYSDE-----KLWGCLEEVKLKEVVSDLPDGLASKISEGGT---NFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:PRK10261 413 --SLDPRQTVGDSimeplRVHGLLPGKAAAARVAWLLERVGLLPEHAWRyphEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1282 TANVDPQTDGLIQATIRSKFRDCTV--LTIAHRLHTIID-SDKVMVMDAGRVVEFG 1334
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
515-686 |
6.09e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESwlfsgTVRQNILFGQPMDSQRye 594
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREA-----SLIDAIGRKGDFKDAV-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 595 EVVKKCALErdfdllplrDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS----VARHLFDQCVRgh 670
Cdd:COG2401 117 ELLNAVGLS---------DAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrVARNLQKLARR-- 185
|
170
....*....|....*.
gi 442622995 671 lRGSTVVLVTHQEQFL 686
Cdd:COG2401 186 -AGITLVVATHHYDVI 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
497-719 |
9.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSS---LIQAILGELKANSGQLQVNGsLSYTSQESW- 572
Cdd:PRK13640 4 NIVEFKHVSFTY-PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 573 --------------LFSG-TVRQNILFG---QPMDSQRYEEVVKKcALErDFDLLPLRDNtivgeRGATLSGGQKARISL 634
Cdd:PRK13640 82 irekvgivfqnpdnQFVGaTVGDDVAFGlenRAVPRPEMIKIVRD-VLA-DVGMLDYIDS-----EPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 635 ARSVYRKASIYLLDDPLSAVDAS-------VARHLFDQcvrghlRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYE 707
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAgkeqilkLIRKLKKK------NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
250
....*....|...
gi 442622995 708 SLL-KTGLITGLG 719
Cdd:PRK13640 229 EIFsKVEMLKEIG 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
517-699 |
1.41e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.87 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILgelkANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGqpmdsqryeev 596
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFSRNKLIFIDQLQFLIDVG----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 597 vkkcalerdFDLLPLrdntivGERGATLSGGQKARISLARSVYR--KASIYLLDDPLSAVDASVARHLFDQCVRGHLRGS 674
Cdd:cd03238 76 ---------LGYLTL------GQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN 140
|
170 180
....*....|....*....|....*
gi 442622995 675 TVVLVTHQEQFLPHVDQIVILANGQ 699
Cdd:cd03238 141 TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1135-1334 |
1.61e-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: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLhdlrrQISIIPQ----EPVLFSGTM 1209
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDsGTVTVRGRVSSLLGL-----GGGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 rYNLDPfdEYSDEKlwgcLEEVklkEVVSDLPDGLASKISeggtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1289
Cdd:cd03220 112 -LGLSR--KEIDEK----IDEI---IEFSELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442622995 1290 DGLIQATIRSKFRDC-TVLTIAHRLHTIID-SDKVMVMDAGRVVEFG 1334
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
497-681 |
1.70e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQESWLFS 575
Cdd:PRK13537 6 APIDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 G------------TVRQNIL-FGQ--PMDSQRYEEVVKKCaLErdFDLLPLRDNTIVGErgatLSGGQKARISLARSVYR 640
Cdd:PRK13537 83 GvvpqfdnldpdfTVRENLLvFGRyfGLSAAAARALVPPL-LE--FAKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 641 KASIYLLDDPLSAVDASvARHLFDQCVRGHL-RGSTVVLVTH 681
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLaRGKTILLTTH 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
520-680 |
1.76e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRqniLFGQPMDSQRYEEVVKK 599
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGH---LPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 600 CALE-RDFDLLPLRDNTIVGERGAT------LSGGQKARISLARSVYRKASIYLLDDPLSAVDASvARHLFDQCVRGHLR 672
Cdd:PRK13543 107 CGLHgRRAKQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAHLR 185
|
....*...
gi 442622995 673 GSTVVLVT 680
Cdd:PRK13543 186 GGGAALVT 193
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1108-1332 |
2.25e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1108 PKTWPEQGEIIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSS---LINALFRLSytDGSVLIDTRDTR 1184
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFS---VGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQPQ--SGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1185 QMGLHDLRRQISIIPQEPVLFSGTmrynLDPFDEYSDEKL---WgcLEEVKLKEVVSdLPDGlasKISEggTNFSVGQRQ 1261
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALvekW--LERLKMAHKLE-LEDG---RISN--LKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1262 LVCLARAILRENRILVMDEATANVDPQ------TDGLIQATIRSKfrdcTVLTIAHRLHTIIDSDKVMVMDAGRVVE 1332
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPLLQEMGK----TIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
517-699 |
2.40e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.98 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGqlqvngSLSYTSQESW--LFSGTVRQnILfgqpmDSQRYE 594
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG------SILVRHDGGWvdLAQASPRE-IL-----ALRRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 595 -----------------EVV----------KKCALERDFDLLpLRDNtiVGER-----GATLSGGQKARISLARSVYRKA 642
Cdd:COG4778 95 igyvsqflrviprvsalDVVaepllergvdREEARARARELL-ARLN--LPERlwdlpPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 643 SIYLLDDPLSAVDA---SVARHLFDQCVRghlRGSTVVLVTHQEQFLPHV-DQIVILANGQ 699
Cdd:COG4778 172 PLLLLDEPTASLDAanrAVVVELIEEAKA---RGTAIIGIFHDEEVREAVaDRVVDVTPFS 229
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
520-682 |
2.45e-09 |
|
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: 61.69 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLiQAILGEL-KANSGQLQV--NGSLSYTSQESWLFSGTVRQNILFgqPMDS-QRYEE 595
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSL-FRILGELwPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIY--PDSSeDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 596 VVKKCALERDFDLLPLRDntIVGERGA---------TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQC 666
Cdd:TIGR00954 548 GLSDKDLEQILDNVQLTH--ILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
170
....*....|....*.
gi 442622995 667 VRghlRGSTVVLVTHQ 682
Cdd:TIGR00954 626 RE---FGITLFSVSHR 638
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1136-1362 |
2.53e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.80 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLS------YTDGSVLIDTRDTRQMGLH--DLRRQISIIPQEPVLFSG 1207
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1208 TMRYNL------DPFDEYSDEklwgcLEEVKLKEVVsdLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:PRK14243 106 SIYDNIaygariNGYKGDMDE-----LVERSLRQAA--LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1282 TANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAgRVVEFGSPYELMTKSDS--KVFHNLVNQSGRA 1358
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARvSDMTAFFNV-ELTEGGGRYGYLVEFDRteKIFNSPQQQATRD 257
|
....
gi 442622995 1359 SYEG 1362
Cdd:PRK14243 258 YVSG 261
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
515-825 |
2.56e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWL---FSGTvrQNI-LFGQPM-- 588
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLngqLTGI--ENIeLKGLMMgl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 589 DSQRYEEVVKKCALERDFdllplrdNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVR 668
Cdd:PRK13545 116 TKEKIKEIIPEIIEFADI-------GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 669 GHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGD-------YESLLKtglitGLGSLSKTDKAKTEEQEPLNLNSP 740
Cdd:PRK13545 189 FKEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKEYGDikevvdhYDEFLK-----KYNQMSVEERKDFREEQISQFQHG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 741 DNKNEVTPIKENSEQTVGGSSSGKEhvERQESGGISLALYRKYFQAGGGLVAFLVMLSSSVLAQVAVTGGDYFLTYWVKK 820
Cdd:PRK13545 264 LLQEDQTGRERKRKKGKKTSRKFKK--KRVLITGVCIALLTGIISTGYYYKNLLPFNSENKYAEKVASKENVTESKQMVK 341
|
....*
gi 442622995 821 ESTAA 825
Cdd:PRK13545 342 KEKGA 346
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
517-681 |
3.04e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL---------SYTSQESWLFSGTVRQNILFGQp 587
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaergVVFQNEGLLPWRNVQDNVAFGL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 mdsqRYEEVVKKCALERDFDLLPLrdntiVGERGA------TLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARH 661
Cdd:PRK11248 96 ----QLAGVEKMQRLEIAHQMLKK-----VGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|.
gi 442622995 662 LFDQCVR-GHLRGSTVVLVTH 681
Cdd:PRK11248 167 MQTLLLKlWQETGKQVLLITH 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
518-709 |
3.29e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 518 SGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFgqpmdsqryeevv 597
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLF------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 598 KKCALERDFDLL-----PLRDNT----------------IVGERGAT------LSGGQKARISLARSVYRKASIYLLDDP 650
Cdd:PRK11831 91 QSGALFTDMNVFdnvayPLREHTqlpapllhstvmmkleAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 651 LSAVDA---SVARHLFDQCvrGHLRGSTVVLVTHQeqfLPHV----DQIVILANGQIKALGDYESL 709
Cdd:PRK11831 171 FVGQDPitmGVLVKLISEL--NSALGVTCVVVSHD---VPEVlsiaDHAYIVADKKIVAHGSAQAL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1072-1374 |
3.58e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1072 RQTAELENTMTAVERVVEYEsiEPEGMLEAPDDKKPPKTWPEqgeIIFKELNLRYTPNAKAenVLKSLSFVIQPREKVGI 1151
Cdd:TIGR01257 889 REERALEKTEPLTEEMEDPE--HPEGINDSFFERELPGLVPG---VCVKNLVKIFEPSGRP--AVDRLNITFYENQITAF 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1152 VGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTrQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWgclEE 1230
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTgLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---EE 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1231 VKLkEVVSDLPD-GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRsKFRD--CTVL 1307
Cdd:TIGR01257 1038 AQL-EMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL-KYRSgrTIIM 1115
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1308 TIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDSKVFHNLVN-----QSGRASYEGLLKIAQETFESS 1374
Cdd:TIGR01257 1116 STHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRkmkniQSQRGGCEGTCSCTSKGFSTR 1187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1131-1335 |
4.01e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.98 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1131 KAENVLKSL---SFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQ---MGLHDLRRQISIIPQEPv 1203
Cdd:PRK11308 23 KPERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIeTPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 lfsgtmrY-NLDPFDEYSD------------------EKLWGCLEEVKLK-EVVSDLPDglaskiseggtNFSVGQRQLV 1263
Cdd:PRK11308 102 -------YgSLNPRKKVGQileepllintslsaaerrEKALAMMAKVGLRpEHYDRYPH-----------MFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQtdglIQATIRSKFRD------CTVLTIAHRL----HTiidSDKVMVMDAGRVVEF 1333
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLsvveHI---ADEVMVMYLGRCVEK 236
|
..
gi 442622995 1334 GS 1335
Cdd:PRK11308 237 GT 238
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
520-703 |
4.37e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-LSYTSQESW--LFSGTVRQNILF-------GQPMD 589
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYrkLFSAVFTDFHLFdqllgpeGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 590 SQRYEEVVKKCALErdfDLLPLRDNTIVGERgatLSGGQKARISLARSVYRKASIYLLD------DPlsavdasVARHLF 663
Cdd:PRK10522 422 PALVEKWLERLKMA---HKLELEDGRISNLK---LSKGQKKRLALLLALAEERDILLLDewaadqDP-------HFRREF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 664 DQCVRGHLR--GSTVVLVTHQEQFLPHVDQIVILANGQIKAL 703
Cdd:PRK10522 489 YQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
520-704 |
4.54e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.57 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG------------SLSYTSQESWLFSG-TVRQNILFGQ 586
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 587 PMDSQRYEEV-VKKCALERDFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQ 665
Cdd:TIGR01257 1029 QLKGRSWEEAqLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442622995 666 CVRgHLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:TIGR01257 1104 LLK-YRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1135-1299 |
5.22e-09 |
|
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: 57.75 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDtrqmgLHDLRRQisiiPQEPVLFSG------ 1207
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWNGTP-----LAEQRDE----PHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1208 ---TMRYNLD---PFDEYSDEKLWGCLEEVKLkevvSDLPDGLASKISeggtnfsVGQRQLVCLARAILRENRILVMDEA 1281
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGL----TGFEDLPAAQLS-------AGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*...
gi 442622995 1282 TANVDPQTDGLIQATIRS 1299
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRA 172
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1136-1329 |
6.40e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL----SYtDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQEPVL------ 1204
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgTY-EGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 ----FSGT--MRYNLDPFDE-YSDEKLWgcLEEVKLkEVVSDLPDGlaskiseggtNFSVGQRQLVCLARAILRENRILV 1277
Cdd:PRK13549 100 leniFLGNeiTPGGIMDYDAmYLRAQKL--LAQLKL-DINPATPVG----------NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1278 MDEATANVDPQTDGLIQATIRS-KFRDCTVLTIAHRLHTIID-SDKVMVMDAGR 1329
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
517-690 |
6.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSL----SYTSQESWLFSG---------TVRQNIL 583
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdLCTYQKQLCFVGhrsginpylTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 FGQPMDSQRYE--EVVKKCALERDFDLlPLrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARH 661
Cdd:PRK13540 97 YDIHFSPGAVGitELCRLFSLEHLIDY-PC----------GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*....
gi 442622995 662 LFDQCVRGHLRGSTVVLVTHQEQFLPHVD 690
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
517-700 |
6.64e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQESW-LFSGTV-------------RQN 581
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGePLAKLNRAQRkAFRRDIqmvfqdsisavnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 I--LFGQPM----DSQRYEEVVKKCALERDFDLlplrDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:PRK10419 108 VreIIREPLrhllSLDKAERLARASEMLRAVDL----DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 656 asvaRHLFDQCVR-----GHLRGSTVVLVTHQ----EQFLPHVdqiVILANGQI 700
Cdd:PRK10419 184 ----LVLQAGVIRllkklQQQFGTACLFITHDlrlvERFCQRV---MVMDNGQI 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1135-1331 |
6.70e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVlidtrdtRQMGLHDLRRQISIIPQEPVLFS--GTMRY 1211
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEV-------RVAGLVPWKRRKKFLRRIGVVFGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGL--ASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQT 1289
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLdlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442622995 1290 DGLIQATIR--SKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:cd03267 189 QENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1151-1335 |
7.86e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1151 IVGRTGAGKSSLINALFRLSYTD-------GSVLIDTRDTRQMGLHdlRRQISIIPQEPVLF-----SGTMRYNLDPFD- 1217
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQkgrivlnGRVLFDAEKGICLPPE--KRRIGYVFQDARLFphykvRGNLRYGMAKSMv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1218 EYSDE--KLWGcleevkLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVD-PQTDGLIQ 1294
Cdd:PRK11144 107 AQFDKivALLG------IEPLLDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442622995 1295 ATIR-SKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGS 1335
Cdd:PRK11144 170 YLERlAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1136-1339 |
1.07e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINAL-FRL---SYTDGSVLIDTR--DTRQMglhdlrRQISIIPQEPVLFSGTM 1209
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSpkgVKGSGSVLLNGMpiDAKEM------RAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 --RYNLD-------PFDEYSDEKlwgcLEEVklKEVVSDLpdGLAS----KISEGGT--NFSVGQRQLVCLARAILRENR 1274
Cdd:TIGR00955 115 tvREHLMfqahlrmPRRVTKKEK----RERV--DEVLQAL--GLRKcantRIGVPGRvkGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1275 ILVMDEATANVDPQTDGLIQATIRSkfrdctvltIAHRLHTIIDS------------DKVMVMDAGRVVEFGSPYEL 1339
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKG---------LAQKGKTIICTihqpsselfelfDKIILMAEGRVAYLGSPDQA 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
519-658 |
1.14e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 59.31 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 519 GINLEIKPGSVVAVIGLTGSGKSSLIQAILGeLKANSGQLQVNG-SLSYTSQESWL-------------FSG-----TVR 579
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALRplrrrmqvvfqdpFGSlsprmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNIlfGQPM--------DSQRYEEVVKkcALERdfdllplrdntiVGERGATL-------SGGQKARISLARSVYRKASI 644
Cdd:COG4172 383 QII--AEGLrvhgpglsAAERRARVAE--ALEE------------VGLDPAARhryphefSGGQRQRIAIARALILEPKL 446
|
170
....*....|....
gi 442622995 645 YLLDDPLSAVDASV 658
Cdd:COG4172 447 LVLDEPTSALDVSV 460
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
171-458 |
1.24e-08 |
|
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: 57.95 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 171 GLAIFVVELGLRTLQPIFLVKLISYFSGEPDaanagfYYAVAQIVISALTVMILTPTTFGIHHVCF-----KMRVAMGSM 245
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGD------LSLLLWIALLLLLLALLRALLSYLRRYLAarlgqRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 246 IFRKALRLTKGALGDTTSGHVVNLISNDIPRLDS-APYTVHYLWVGPLQVLVITYLMYQeigIS---AVFGVLFMLLFMP 321
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILFY---LNwklTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 322 IQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSR 401
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 402 VAIFLSLV--GYVILGKVFTPEIAFMITAYYNVLLAA----MSIYVpsaIIQTAqfLTSIRRV 458
Cdd:cd07346 235 LGTALVLLygGYLVLQGSLTIGELVAFLAYLGMLFGPiqrlANLYN---QLQQA--LASLERI 292
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
517-716 |
1.44e-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: 59.07 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILG----------------ELKANSGQLQVNGSLSYTSQESWLFSG-TVR 579
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNIRDTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFGQ----PMDSQRYEEVVKKC-ALERDFDLLPLRDNTIVGERGatlsGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:TIGR02633 97 ENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 655 DASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESLLKTGLIT 716
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMSEDDIIT 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1138-1340 |
1.87e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1138 SLSFviqPREKV-GIVGRTGAGKSSLINALFR-LSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQE-PVLFSGTMR---- 1210
Cdd:PRK10575 31 SLTF---PAGKVtGLIGHNGSGKSTLLKMLGRhQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRelva 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1211 ---Y----NLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:PRK10575 108 igrYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1284 NVD--PQTD--GLIQATirSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELM 1340
Cdd:PRK10575 177 ALDiaHQVDvlALVHRL--SQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
843-1087 |
2.59e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 57.10 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 843 YTLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIA 922
Cdd:cd18540 48 YLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 923 LWLAGIIIVIANVNP------LLLVPtlMLSVIFYHLRNLYLKTSRdlkRVEAINrspvySHLAASLN-GLT---TIRAL 992
Cdd:cd18540 128 TYMIGILIVMLILNWklalivLAVVP--VLAVVSIYFQKKILKAYR---KVRKIN-----SRITGAFNeGITgakTTKTL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 993 DAQRVLEKEFD---------SYQDAHSSAFFM-------YISTSQAFGYCMNCICVIYISIITLSFFafppgngadvglv 1056
Cdd:cd18540 198 VREEKNLREFKelteemrraSVRAARLSALFLpivlflgSIATALVLWYGGILVLAGAITIGTLVAF------------- 264
|
250 260 270
....*....|....*....|....*....|.
gi 442622995 1057 ITQAMGLIDMVQWGVRQTAELENTMTAVERV 1087
Cdd:cd18540 265 ISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-705 |
2.70e-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: 58.28 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILG--ELKANSGQLQVNGSL----------------------SYTSQES- 571
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALcekcgyverpskvgepcpvcggTLEPEEVd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 572 -WLFSGTVRQNILFGQPMDSQR----YEE------VVK---------KCALERDFDLLplrDNTIVGER----GATLSGG 627
Cdd:TIGR03269 96 fWNLSDKLRRRIRKRIAIMLQRtfalYGDdtvldnVLEaleeigyegKEAVGRAVDLI---EMVQLSHRithiARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 628 QKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRG-HLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGD 705
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLsDKAIWLENGEIKEEGT 252
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1118-1344 |
3.23e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 56.62 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1118 IFKELNLRYTPNAKAEnVLKSLSFVIQPREKVGIVGRTGAGKSSL---INALfrLSYTDGSVLIDTR--DTRQMGLHDLR 1192
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGI--LKPTSGEVLIKGEpiKYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEP--VLFSGTMR-------YNLDPFDEYSDEKLWGCLEEVKLkevvsdlpDGLASKISEggtNFSVGQRQLV 1263
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGM--------EGFENKPPH---HLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1264 CLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRD-CTVLTIAHRLHTI-IDSDKVMVMDAGRVVEFGSPYELMT 1341
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
...
gi 442622995 1342 KSD 1344
Cdd:PRK13639 227 DIE 229
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
843-1035 |
3.69e-08 |
|
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: 56.71 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 843 YTLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIA 922
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 923 LWLAGIIIVIANVNP------LLLVPTLMLSVIF--YHLRNLYLKTSRdlkrveaiNRSPVYSHLAASLNGLTTIRALDA 994
Cdd:cd18545 126 LTLVGIVIIMFSLNVrlalvtLAVLPLLVLVVFLlrRRARKAWQRVRK--------KISNLNAYLHESISGIRVIQSFAR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442622995 995 QRVLEKEFDSYQDAH----------SSAFFMYISTSQAFGycmncICVIYI 1035
Cdd:cd18545 198 EDENEEIFDELNRENrkanmravrlNALFWPLVELISALG-----TALVYW 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1116-1346 |
4.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1116 EIIFKelNLRYTPNAKAENVLKSL---SFVIQPREKVGIVGRTGAGKSSLI---NALF---------------------- 1167
Cdd:PRK13651 2 QIKVK--NIVKIFNKKLPTELKALdnvSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1168 RLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQ--EPVLFS---------GTMRYNLDPfdEYSDEKLWGCLEEVKLKEv 1236
Cdd:PRK13651 80 KEKVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEqtiekdiifGPVSMGVSK--EEAKKRAAKYIELVGLDE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1237 vsdlpdglaSKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQtdGLIQatirskfrdctVLTIAHRLH-- 1314
Cdd:PRK13651 157 ---------SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GVKE-----------ILEIFDNLNkq 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 442622995 1315 --TII----DSD-------KVMVMDAGRVVEFGSPYELMtkSDSK 1346
Cdd:PRK13651 215 gkTIIlvthDLDnvlewtkRTIFFKDGKIIKDGDTYDIL--SDNK 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1117-1345 |
4.25e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.48 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAkaenVLKSLSFVIQPREKVGIVGRTGAGKSSL---INALFRLsyTDGSVLIDTRDTRqmglhDLRR 1193
Cdd:PRK09493 2 IEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEEI--TSGDLIVDGLKVN-----DPKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1194 QISIIPQEP-VLFSgtmRYNLDPFDEYSDEKLWGCLE-----EVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCL 1265
Cdd:PRK09493 71 DERLIRQEAgMVFQ---QFYLFPHLTALENVMFGPLRvrgasKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 ARAILRENRILVMDEATANVDPQtdgliqatIRSKfrdctVLTIAHRL-----------HTIIDSDKV----MVMDAGRV 1330
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPE--------LRHE-----VLKVMQDLaeegmtmvivtHEIGFAEKVasrlIFIDKGRI 214
|
250
....*....|....*
gi 442622995 1331 VEFGSPYELMTKSDS 1345
Cdd:PRK09493 215 AEDGDPQVLIKNPPS 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1151-1347 |
4.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1151 IVGRTGAGKSSLI---NALfrLSYTDGSVLID----TRDTRQMGLHDLRRQISIIPQ--EPVLFSGTMRYNLdpfdEYSD 1221
Cdd:PRK13646 38 IVGQTGSGKSTLIqniNAL--LKPTTGTVTVDditiTHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVEREI----IFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1222 EKLWGCLEEVKLKEVVSDLPDGLASKI-SEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS- 1299
Cdd:PRK13646 112 KNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSl 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442622995 1300 -KFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMtKSDSKV 1347
Cdd:PRK13646 192 qTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF-KDKKKL 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
515-714 |
4.62e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.91 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS---------------LSYTSQESWLFSGTVR 579
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddnfeklrkhigIVFQNPDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFGQPMDSQRYEEVVKKC--ALErDFDLLPLRDNtivgeRGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS 657
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVseALK-QVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 658 VARHLFDqCVRgHLRGS---TVVLVTHQEQFLPHVDQIVILANGQIKALG-------DYESLLKTGL 714
Cdd:PRK13648 177 ARQNLLD-LVR-KVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGtpteifdHAEELTRIGL 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1136-1331 |
4.74e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGlHDLRRQ--ISIIPQE-PVLFSGTMRY 1211
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1212 NLdPFDEYSDEKLWGC--LEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANV-D 1286
Cdd:PRK09700 100 NL-YIGRHLTKKVCGVniIDWREMRVRAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 1287 PQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1135-1338 |
5.45e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.00 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINAL-FRLSYTDGSVlidtrdtrQMGlHDLRrqISIIPQEpvlfSGTMRYNL 1213
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPDSGTV--------KLG-ETVK--IGYFDQH----QEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1214 DPFDEysdekLWGCLEEVKLKEVVSDL------PDGLASKISeggtNFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:COG0488 395 TVLDE-----LRDGAPGGTEQEVRGYLgrflfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 1288 QT-----DGLIQatirskFrDCTVLTIAH-R--LHTIidSDKVMVMDAGRVVEFGSPYE 1338
Cdd:COG0488 466 ETlealeEALDD------F-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREYPGGYD 515
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
517-681 |
6.52e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQESWLFSG--------------TVRQN 581
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQ-P-----MDSQRYEEVVKKCALERDFDLLPlrdNTIVGErgatLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:PRK11288 100 LYLGQlPhkggiVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180
....*....|....*....|....*...
gi 442622995 656 ASVARHLFDqcVRGHLR--GSTVVLVTH 681
Cdd:PRK11288 173 AREIEQLFR--VIRELRaeGRVILYVSH 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
517-705 |
7.06e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLfsgTVRQNI--LFGQPMDSQRYE 594
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL---ALRQQVatVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 595 EVVKKCAL-------------ERDFDLLPLRDNTIVGERG-ATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:PRK13638 94 DIDSDIAFslrnlgvpeaeitRRVDEALTLVDAQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442622995 661 HLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALGD 705
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGA 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-704 |
7.39e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSG-TVRQNI--LFGQP------ 587
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiKLRKEVgmVFQQPnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 588 --MDSQRY-----------------EEVVKKCALERD-FDLLplrdntivGERGATLSGGQKARISLARSVYRKASIYLL 647
Cdd:PRK14246 106 siYDNIAYplkshgikekreikkivEECLRKVGLWKEvYDRL--------NSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 648 DDPLSAVDAsVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:PRK14246 178 DEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWG 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1130-1325 |
7.40e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1130 AKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGT 1208
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 MRYNLD-PFDEYSDeklwgcleEVKLKEVVSDLPD-GLASKISEGGTN-FSVGQRQLVCLARAILRENRILVMDEATANV 1285
Cdd:PRK10247 97 VYDNLIfPWQIRNQ--------QPDPAIFLDDLERfALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 1286 DPQTDGLIQATIRSKFRD--CTVLTIAHRLHTIIDSDKVMVM 1325
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREqnIAVLWVTHDKDEINHADKVITL 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1117-1311 |
7.42e-08 |
|
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: 52.84 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNakaeNVLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRDTrqmglhdlrrqI 1195
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGSTVK-----------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQepvlFSGtmrynldpfdeysdeklwgcleevklkevvsdlpdglaskiseggtnfsvGQRQLVCLARAILRENRI 1275
Cdd:cd03221 66 GYFEQ----LSG--------------------------------------------------GEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*...
gi 442622995 1276 LVMDEATANVDPQTdglIQATIR--SKFRdCTVLTIAH 1311
Cdd:cd03221 92 LLLDEPTNHLDLES---IEALEEalKEYP-GTVILVSH 125
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1125-1289 |
8.23e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1125 RYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQM---GLHDLR-RQISIIP 1199
Cdd:PRK11629 14 RYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1200 Q---------------EPVLFSGTMRynldpfdEYSDEKLWGCLEEVklkevvsdlpdGLASKISEGGTNFSVGQRQLVC 1264
Cdd:PRK11629 94 QfhhllpdftalenvaMPLLIGKKKP-------AEINSRALEMLAAV-----------GLEHRANHRPSELSGGERQRVA 155
|
170 180
....*....|....*....|....*
gi 442622995 1265 LARAILRENRILVMDEATANVDPQT 1289
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARN 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
517-681 |
8.76e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTS-------------QESWLFSG-TVRQN 581
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkPVRIRSprdaialgigmvhQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQP------MDSQRYEEVVKkcALERDFDlLPLRDNTIVGErgatLSGGQKARISLARSVYRKASIYLLDDPLsavd 655
Cdd:COG3845 101 IVLGLEptkggrLDRKAARARIR--ELSERYG-LDVDPDAKVED----LSVGEQQRVEILKALYRGARILILDEPT---- 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 442622995 656 aSV-----ARHLFDqcvrgHLR-----GSTVVLVTH 681
Cdd:COG3845 170 -AVltpqeADELFE-----ILRrlaaeGKSIIFITH 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
520-701 |
8.91e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTSQESWLFSG-TVRQNIL- 583
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSVYDNLMa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 584 ---FGQPMDSQRYEEVVKKcaLERDFDLLPLRDNTivgerGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD----- 655
Cdd:PRK10895 102 vlqIRDDLSAEQREDRANE--LMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvi 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 656 --ASVARHL---------FDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIK 701
Cdd:PRK10895 175 diKRIIEHLrdsglgvliTDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-704 |
9.38e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 496 KSAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQaILGELKANSGQLQVNGSLSYTSQEswLFS 575
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQD--IFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTV-----RQNILFGQP---------------------MDSQRYEEVVKKCALERDFDLLPLRDNtiVGERGATLSGGQK 629
Cdd:PRK14247 75 MDVielrrRVQMVFQIPnpipnlsifenvalglklnrlVKSKKELQERVRWALEKAQLWDEVKDR--LDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 630 ARISLARSVYRKASIYLLDDP---LSAVDASVARHLFDQCVrghlRGSTVVLVTHQEQFLPHV-DQIVILANGQIKALG 704
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPtanLDPENTAKIESLFLELK----KDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWG 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1135-1330 |
1.06e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLI-------DTR-DTRQMgLHDLRrqisIIPQEPVL-- 1204
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplaEAReDTRLM-FQDAR----LLPWKKVIdn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 ----FSGTMRynldpfdeysdEKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLARAILRENRILVMDE 1280
Cdd:PRK11247 102 vglgLKGQWR-----------DAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1281 ATANVDPQTDGLIQATIRSKFRD--CTVLTIAHRL-HTIIDSDKVMVMDAGRV 1330
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1135-1332 |
1.12e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL------SYTDGSVLIDTRDTRQMGLHDLRR----QISIIPQEPVL 1204
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1205 fsgtmryNLDPFdeYSDEK--------------------LWGCLEEVKLKEV---VSDLPDGLaskiseggtnfSVGQRQ 1261
Cdd:PRK15134 104 -------SLNPL--HTLEKqlyevlslhrgmrreaargeILNCLDRVGIRQAakrLTDYPHQL-----------SGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1262 LVCLARAILRENRILVMDEATANVDPQtdglIQATIRSKFRDC------TVLTIAHRLHTIID-SDKVMVMDAGRVVE 1332
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRELqqelnmGLLFITHNLSIVRKlADRVAVMQNGRCVE 237
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
845-1028 |
1.21e-07 |
|
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: 55.10 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:cd18547 53 GLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVNPLL------LVPtLMLSVIFY---HLRNLYLKTSRDLKRVEAinrspvysHLAASLNGLTTIRALDAQ 995
Cdd:cd18547 133 IVGTLIMMLYISPLLtlivlvTVP-LSLLVTKFiakRSQKYFRKQQKALGELNG--------YIEEMISGQKVVKAFNRE 203
|
170 180 190
....*....|....*....|....*....|...
gi 442622995 996 RVLEKEFDSYQDAHSSAFFmyisTSQAFGYCMN 1028
Cdd:cd18547 204 EEAIEEFDEINEELYKASF----KAQFYSGLLM 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
526-686 |
1.29e-07 |
|
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: 52.38 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 526 PGSVVAVIGLTGSGKSSLIQAILGELKANSGQlqvngslsytsqeswlfsgtvrqnilfgqpmdsqryeevVKKCALERD 605
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG---------------------------------------VIYIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 606 FDLLPL-RDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHL------RGSTVVL 678
Cdd:smart00382 42 LEEVLDqLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseKNLTVIL 121
|
....*...
gi 442622995 679 VTHQEQFL 686
Cdd:smart00382 122 TTNDEKDL 129
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
840-1003 |
1.55e-07 |
|
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: 54.73 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 840 VYKYTLIIILSVI--------MNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEvl 911
Cdd:cd18554 41 VYKLFTIIGIMFFiflilrppVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 912 pVVLVDVMQIALWLAGIIIVIANV---NPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTT 988
Cdd:cd18554 119 -FITTGLMNIWLDMITIIIAICIMlvlNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSV 197
|
170
....*....|....*
gi 442622995 989 IRALDAQRVLEKEFD 1003
Cdd:cd18554 198 IKSFALEKHEQKQFD 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1151-1339 |
1.71e-07 |
|
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: 54.81 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1151 IVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHdlRRQISIIPQEPVLF---------SGTMRYNLDPFDEYs 1220
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDsGSIMLDGEDVTNVPPH--LRHINMVFQSYALFphmtveenvAFGLKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1221 DEKLWGCLEEVKLKEVVSDLPdglaskiseggTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSK 1300
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 442622995 1301 FRD--CTVLTIAH-RLHTIIDSDKVMVMDAGRVVEFGSPYEL 1339
Cdd:TIGR01187 147 QEQlgITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1117-1312 |
1.77e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLrYTPNAkaENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLidTRDTRQmglhdlrrQIS 1196
Cdd:TIGR00954 452 IKFENIPL-VTPNG--DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL--TKPAKG--------KLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1197 IIPQEPVLFSGTMR----YNLDPFD----EYSDEKLWGCLEEVKLKEVVSDlpDGLASKISEGGTNFSVGQRQLVCLARA 1268
Cdd:TIGR00954 519 YVPQRPYMTLGTLRdqiiYPDSSEDmkrrGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442622995 1269 ILRENRILVMDEATANVDPQTDGLIqatirskFRDC-----TVLTIAHR 1312
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1119-1338 |
1.77e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1119 FKELNLRYTPNAKAE-NVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDT----RQMGLH-DL 1191
Cdd:COG1134 24 LKELLLRRRRTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEpTSGRVEVNGRVSalleLGAGFHpEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1192 --RrqisiipqEPVLFSGTMrYNLDPfdeysdeklwgclEEV--KLKEVV--SDLPDGLASKISeggtNFSVGQRqlvcl 1265
Cdd:COG1134 104 tgR--------ENIYLNGRL-LGLSR-------------KEIdeKFDEIVefAELGDFIDQPVK----TYSSGMR----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1266 AR-----AILRENRILVMDEATAnVdpqTDGLIQATIRSKFRD-----CTVLTIAHRLHTIID-SDKVMVMDAGRVVEFG 1334
Cdd:COG1134 153 ARlafavATAVDPDILLVDEVLA-V---GDAAFQKKCLARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDG 228
|
....
gi 442622995 1335 SPYE 1338
Cdd:COG1134 229 DPEE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1113-1330 |
2.11e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1113 EQGEIIFKELNLR-YTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRlSYT---DGSVLIDTR--DTRQM 1186
Cdd:TIGR02633 252 EIGDVILEARNLTcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPgkfEGNVFINGKpvDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1187 gLHDLRRQISIIPQE-------PVL-------------FSGTMRYNldpfDEYSDEKLWGCLEEVKLKEVVSDLPDGlas 1246
Cdd:TIGR02633 331 -AQAIRAGIAMVPEDrkrhgivPILgvgknitlsvlksFCFKMRID----AAAELQIIGSAIQRLKVKTASPFLPIG--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1247 kiseggtNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRD-CTVLTIAHRLHTIID-SDKVMV 1324
Cdd:TIGR02633 403 -------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGlSDRVLV 475
|
....*.
gi 442622995 1325 MDAGRV 1330
Cdd:TIGR02633 476 IGEGKL 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1135-1287 |
2.37e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLSYTDGSVLIDTRD-TRQMGLHDLRRQISIIPQEPVLFSG-TMRY 1211
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1212 NLDPFDEYSDEKLWgcleEVKLKEVVSDLPDGLASKISEGGTnFSVGQRQLVCLARAILRENRILVMDEATANVDP 1287
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
521-710 |
2.52e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 521 NLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGslsytsqeswlfsgtvrqnILFGQPMDSQRYEEVVKKC 600
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 601 ALE-RDFDLLP---LRDNTIVGERGA-----------------------------TLSGGQKARISLARSVYRKASIYLL 647
Cdd:PRK10070 109 AMVfQSFALMPhmtVLDNTAFGMELAginaeerrekaldalrqvglenyahsypdELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 648 DDPLSAVDASVARHLFDQCVR---GHLRgsTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLL 710
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKlqaKHQR--TIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
517-650 |
3.01e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTS---QESWLFSG-TV 578
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrKGEGLVLDlSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 RQNILF--------GQPMDSQRYEEVVKKCAleRDFDLLPLRDNTIVGergaTLSGG--QKarISLARSVYRKASIYLLD 648
Cdd:COG1129 348 RENITLasldrlsrGGLLDRRRERALAEEYI--KRLRIKTPSPEQPVG----NLSGGnqQK--VVLAKWLATDPKVLILD 419
|
..
gi 442622995 649 DP 650
Cdd:COG1129 420 EP 421
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
517-745 |
3.27e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--SLSYTSQESWLFsgtVRQNILFGQPMDSQRYE 594
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEF---LRADESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 595 EVVKKcalerdfdllpLRD--------NTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQC 666
Cdd:PRK10636 405 ELEQK-----------LRDylggfgfqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 667 VrgHLRGSTVVlVTHQEQFL-PHVDQIVILANGQIKA----LGDYESLLKtglitglgSLSKTDKAKTEEQEPLNLNSPD 741
Cdd:PRK10636 474 I--DFEGALVV-VSHDRHLLrSTTDDLYLVHDGKVEPfdgdLEDYQQWLS--------DVQKQENQTDEAPKENNANSAQ 542
|
....
gi 442622995 742 NKNE 745
Cdd:PRK10636 543 ARKD 546
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
513-711 |
3.28e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 513 PDYTL-SGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS-------------LSYTSQESWLFSG-T 577
Cdd:PRK10575 22 PGRTLlHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGmT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 578 VRQNILFGQ-----------PMDSQRYEEVVKKCALErdfdllPLRDNTIvgergATLSGGQKARISLARSVYRKASIYL 646
Cdd:PRK10575 102 VRELVAIGRypwhgalgrfgAADREKVEEAISLVGLK------PLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 647 LDDPLSAVDASVARHLFDQCVR-GHLRGSTVVLVTHQEQFLP-HVDQIVILANGQIKALGDYESLLK 711
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRlSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1135-1339 |
3.32e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.96 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVLIDTRDTRQMGLHdlRRQISIIPQEPVLF-----SGT 1208
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFphmslGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1209 MRYNLdpfdeysdeKLWGC-LEEVK--LKEVVS--DLpDGLASKISEggtNFSVGQRQLVCLARAILRENRILVMDEATA 1283
Cdd:PRK11432 99 VGYGL---------KMLGVpKEERKqrVKEALElvDL-AGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 1284 NVDPQtdglIQATIRSKFR------DCTVLTIAH-RLHTIIDSDKVMVMDAGRVVEFGSPYEL 1339
Cdd:PRK11432 166 NLDAN----LRRSMREKIRelqqqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1128-1332 |
3.37e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1128 PNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGLHD-LRRQISIIPQEpvlf 1205
Cdd:PRK11288 15 PGVKA---LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDaGSILIDGQEMRFASTTAaLAAGVAIIYQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 sgtmrYNLDPfdEYS-DEKLW--------GCLEEVKLKEVVSDLPDGLASKISEGG--TNFSVGQRQLVCLARAILRENR 1274
Cdd:PRK11288 88 -----LHLVP--EMTvAENLYlgqlphkgGIVNRRLLNYEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1275 ILVMDEATANVD-PQTDGL--IQATIRSKFRdcTVLTIAHRLHTIID-SDKVMVMDAGRVVE 1332
Cdd:PRK11288 161 VIAFDEPTSSLSaREIEQLfrVIRELRAEGR--VILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
845-1003 |
3.60e-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: 53.58 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLS---SSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQI 921
Cdd:cd18552 44 AIIGLFLLRGLAsylQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 922 ALWLAGIIIVIANVNP------LLLVPTLMLSVIFY--HLRnlylKTSRdlKRVEAINRspVYSHLAASLNGLTTIRALD 993
Cdd:cd18552 124 PLTVIGLLGVLFYLDWkltliaLVVLPLAALPIRRIgkRLR----KISR--RSQESMGD--LTSVLQETLSGIRVVKAFG 195
|
170
....*....|
gi 442622995 994 AQRVLEKEFD 1003
Cdd:cd18552 196 AEDYEIKRFR 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
497-704 |
5.02e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 497 SAISIRDLKAKWDPNSPdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTS-------- 568
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepadrdia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 ---QESWLFSG-TVRQNILFG---QPMDSQRYEEVVKKCA--LErdfdLLPLRDntivgERGATLSGGQKARISLARSVY 639
Cdd:PRK11650 80 mvfQNYALYPHmSVRENMAYGlkiRGMPKAEIEERVAEAAriLE----LEPLLD-----RKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442622995 640 RKASIYLLDDPLSAVDAS--VA-----RHLfdqcvrgHLR-GSTVVLVTH-QEQFLPHVDQIVILANGQIKALG 704
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKlrVQmrleiQRL-------HRRlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIG 217
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
845-1034 |
7.12e-07 |
|
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: 52.56 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSF--LLFNIA-KKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQI 921
Cdd:cd18557 41 ILLAIYLLQSVFTFVryYLFNIAgERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 922 ALWLAGIIIVIANVNP------LLLVPTLMLSVIFY--HLRNLYLKTSRDLKRVeainrspvySHLAA-SLNGLTTIRAL 992
Cdd:cd18557 121 ILQVIGGLIILFILSWkltlvlLLVIPLLLIASKIYgrYIRKLSKEVQDALAKA---------GQVAEeSLSNIRTVRSF 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442622995 993 DAQRVLEKEFD-----SYQDAHSSAFF--MYISTSQAFGYCmnCICVIY 1034
Cdd:cd18557 192 SAEEKEIRRYSealdrSYRLARKKALAnaLFQGITSLLIYL--SLLLVL 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-681 |
7.40e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 495 LKSAISIRDLKAKWDPNspdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAI-----LGELKANSGQLQVNGSLSYTS- 568
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 569 --------QESWLFSG-------TVRQNILFGQPMDS---------QRYEEVVKKCALerdFDLLPLRDNtivgERGATL 624
Cdd:PRK14267 78 vdpievrrEVGMVFQYpnpfphlTIYDNVAIGVKLNGlvkskkeldERVEWALKKAAL---WDEVKDRLN----DYPSNL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 625 SGGQKARISLARSVYRKASIYLLDDPLSAVD----ASVARHLFDqcvrghLRGS-TVVLVTH 681
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDpvgtAKIEELLFE------LKKEyTIVLVTH 206
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
472-712 |
8.44e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 472 KSEGPSKDTVPGNPpsnnneadllksAISIRDLKAKWdPNSPdYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGEL 551
Cdd:PLN03073 494 KFEFPTPDDRPGPP------------IISFSDASFGY-PGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGEL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 552 KANSG--------------QLQVNGsLSYTSQE----SWLFSGTVRQNIL-----FGqpmdsqryeeVVKKCALERDFdl 608
Cdd:PLN03073 560 QPSSGtvfrsakvrmavfsQHHVDG-LDLSSNPllymMRCFPGVPEQKLRahlgsFG----------VTGNLALQPMY-- 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 609 lplrdntivgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVrghLRGSTVVLVTHQEQFLP- 687
Cdd:PLN03073 627 --------------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV---LFQGGVLMVSHDEHLISg 689
|
250 260
....*....|....*....|....*....
gi 442622995 688 HVDQIVILANGQIK----ALGDYESLLKT 712
Cdd:PLN03073 690 SVDELWVVSEGKVTpfhgTFHDYKKTLQS 718
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
517-681 |
9.34e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYtsqeswlfsGTVRQNILFGQ--PMDSQRYE 594
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI---------GYVPQKLYLDTtlPLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 595 EV---VKKCalerdfDLLPLRDNT----IVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDAS--VARH-LFD 664
Cdd:PRK09544 91 RLrpgTKKE------DILPALKRVqaghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNgqVALYdLID 164
|
170
....*....|....*..
gi 442622995 665 QcVRGHLrGSTVVLVTH 681
Cdd:PRK09544 165 Q-LRREL-DCAVLMVSH 179
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
515-702 |
9.42e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.36 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQaILGELKA-NSGQLQVNG-SLSYTSQES-----------------WLFS 575
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGqPMSKLSSAAkaelrnqklgfiyqfhhLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 576 GTVRQNI----LFG--QPMDSQ-RYEEVVKKCALERdfdllplRDNtivgERGATLSGGQKARISLARSVYRKASIYLLD 648
Cdd:PRK11629 102 FTALENVamplLIGkkKPAEINsRALEMLAAVGLEH-------RAN----HRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 649 DPLSAVDASVARHLFDqcVRGHL---RGSTVVLVTHQEQFLPHVDQIVILANGQIKA 702
Cdd:PRK11629 171 EPTGNLDARNADSIFQ--LLGELnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1136-1331 |
9.53e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL----SYtDGSVLIDTRDTRQMGLHDLRRQ-ISIIPQEPVLF----- 1205
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgTW-DGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 -------------SGTMRYNLDpfdEYSDEKLwgcLEEVKLkevvSDLPDglASKISEGGtnfsVGQRQLVCLARAILRE 1272
Cdd:TIGR02633 96 aeniflgneitlpGGRMAYNAM---YLRAKNL---LRELQL----DADNV--TRPVGDYG----GGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 1273 NRILVMDEATANV-DPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:TIGR02633 160 ARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
519-710 |
1.12e-06 |
|
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: 52.88 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 519 GINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGqpMDSQRY----- 593
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAKRYIG--ILHQEYdlyph 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 594 ----EEVVKKCALERDFDLLPLRD--------------NTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVD 655
Cdd:TIGR03269 380 rtvlDNLTEAIGLELPDELARMKAvitlkmvgfdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 656 ASVARHLFDQCVRGHLR-GSTVVLVTHQEQFLPHV-DQIVILANGQIKALGDYESLL 710
Cdd:TIGR03269 460 PITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
524-681 |
1.16e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 524 IKPGSVVAVIGLTGSGKSSLIQAILGELKANSG------------------QLQ------VNGSLS------YTSQESWL 573
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtELQnyfkklYNGEIKvvhkpqYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 574 FSGTVRQniLFGQPMDSQRYEEVVKKcalerdFDLLPLRDNTIvgergATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PRK13409 176 FKGKVRE--LLKKVDERGKLDEVVER------LGLENILDRDI-----SELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|..
gi 442622995 654 VDA----SVARhlfdqCVRGHLRGSTVVLVTH 681
Cdd:PRK13409 243 LDIrqrlNVAR-----LIRELAEGKYVLVVEH 269
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
517-704 |
1.62e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGeLKANSGQLQVNG-SLS------------YTSQE-SWLFSGTVRQNI 582
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqPLEawsaaelarhraYLSQQqTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 583 LFGQPmDSQRYEEVVKkcALERDFDLLPLRD--NTIVGergaTLSGGQKARISLA-------RSVYRKASIYLLDDPLSA 653
Cdd:PRK03695 91 TLHQP-DKTRTEAVAS--ALNEVAEALGLDDklGRSVN----QLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 654 VDasVARH-LFDQCVRGHLR-GSTVVLVTHQ-EQFLPHVDQIVILANGQIKALG 704
Cdd:PRK03695 164 LD--VAQQaALDRLLSELCQqGIAVVMSSHDlNHTLRHADRVWLLKQGKLLASG 215
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
845-963 |
1.71e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 51.26 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:cd18541 48 LLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFL 127
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 442622995 925 LAGIIIVIANVNPLL----LVPTLMLSVIFYHLRNLYLKTSRD 963
Cdd:cd18541 128 GVLVLVMMFTISPKLtliaLLPLPLLALLVYRLGKKIHKRFRK 170
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1140-1339 |
1.98e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1140 SFVIQPREKVGIVGRTGAGKSSLINAL--FrlsY--TDGSVLIDTRDTR--------QMGL-----H-DLRRQISIIPQE 1201
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLtgF---YkpTGGTILLRGQHIEglpghqiaRMGVvrtfqHvRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1202 PV---------LFSGTmrYNLDPFDEYSDEKL-----WgcLEEVKLKEVVSdlpdglaskiSEGGtNFSVGQRQLVCLAR 1267
Cdd:PRK11300 102 LVaqhqqlktgLFSGL--LKTPAFRRAESEALdraatW--LERVGLLEHAN----------RQAG-NLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1268 AILRENRILVMDEATANVDPQ-TDGLIQ--ATIRSKFrDCTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYEL 1339
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKeTKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1103-1331 |
2.65e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1103 DDKKPPKTwPEQGEIIFKELNLRytpnakAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLID-- 1179
Cdd:COG1129 242 EDLFPKRA-AAPGEVVLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADsGEIRLDgk 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1180 ---TRDTRQ-----MGL--HDlRRQISIIPQEPVlfsgtmRYN--LDPFDEYSDeklWGCLEEVKLKEVVSDL------- 1240
Cdd:COG1129 315 pvrIRSPRDairagIAYvpED-RKGEGLVLDLSI------RENitLASLDRLSR---GGLLDRRRERALAEEYikrlrik 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1241 PDGLASKISeggtNFSVGQRQLVCLARAILRENRILVMDEATANVDpqtdgliqatIRSKFrdcTVLTIAHRL----HTI 1316
Cdd:COG1129 385 TPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID----------VGAKA---EIYRLIRELaaegKAV 447
|
250 260
....*....|....*....|....*.
gi 442622995 1317 I----D-------SDKVMVMDAGRVV 1331
Cdd:COG1129 448 IvissElpellglSDRILVMREGRIV 473
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
831-1035 |
2.69e-06 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 50.98 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 831 EDMESKSMDVYKYTLIIILSVI------MNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDM 904
Cdd:cd18573 29 ESGDIEIFGLSLKTFALALLGVfvvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 905 SQVDEVLPVVLVDVMQIALWLAGIIIVIANVNP------LLLVPTLMLSVIFY--HLRNLylktSRDLKrvEAINRSpvy 976
Cdd:cd18573 109 SVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkltlvmLLVVPPIAVGAVFYgrYVRKL----SKQVQ--DALADA--- 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622995 977 SHLAA-SLNGLTTIRALDAQRVLEKEFD---------SYQDAHSSAFFMyiSTSQAFGYCMnCICVIYI 1035
Cdd:cd18573 180 TKVAEeRLSNIRTVRAFAAERKEVERYAkkvdevfdlAKKEALASGLFF--GSTGFSGNLS-LLSVLYY 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
500-562 |
3.00e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 3.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622995 500 SIRDLKAKwdPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG 562
Cdd:COG3845 259 EVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
845-1023 |
3.12e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.52 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTkDMSQVDEVLPVVLVDVMqIALW 924
Cdd:cd18570 50 LLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLF-LDLL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGII-IVIANVNPLL----LVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINrspvYSHLAASLNGLTTIRALDAQ---- 995
Cdd:cd18570 128 MVIISgIILFFYNWKLflitLLIIPLYILIILLFNKPFKKKNREVMESNAEL----NSYLIESLKGIETIKSLNAEeqfl 203
|
170 180
....*....|....*....|....*...
gi 442622995 996 RVLEKEFDSYQdaHSSAFFMYISTSQAF 1023
Cdd:cd18570 204 KKIEKKFSKLL--KKSFKLGKLSNLQSS 229
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
846-1024 |
4.43e-06 |
|
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: 50.27 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 846 IIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFtKDMSQVDEVLP----VVLVDVMQI 921
Cdd:cd18566 51 AILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTgqalLALLDLPFV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 922 ALWLaGIIIVIANvnPLLLVPTLMLSVIF-------YHLRNLYLKTSR-DLKRveainrspvYSHLAASLNGLTTIRALD 993
Cdd:cd18566 130 LIFL-GLIWYLGG--KLVLVPLVLLGLFVlvaillgPILRRALKERSRaDERR---------QNFLIETLTGIHTIKAMA 197
|
170 180 190
....*....|....*....|....*....|....
gi 442622995 994 AQRVLEKEFDSYQDAHSSAFF---MYISTSQAFG 1024
Cdd:cd18566 198 MEPQMLRRYERLQANAAYAGFkvaKINAVAQTLG 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
512-722 |
4.50e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 512 SPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG--------------SLSYTSQE-SWLFSG 576
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQ-PMDS-------------QRYEEVVKKCALERDFDllplrdntivgERGATLSGGQKARISLARSVYRKA 642
Cdd:PRK09700 96 TVLENLYIGRhLTKKvcgvniidwremrVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 643 SIYLLDDPLSAVDASVARHLFdqCVRGHLR--GSTVVLVTHQeqflphvdqiviLAngQIKALGDYESLLKTGLITGLGS 720
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVYISHK------------LA--EIRRICDRYTVMKDGSSVCSGM 228
|
..
gi 442622995 721 LS 722
Cdd:PRK09700 229 VS 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
517-703 |
4.73e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSG--KSSLIQAILG---------------ELKANSGQLQVNGSLSYTSQESwlFSGtvR 579
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*Gpdagrrpwrf*twcaNRRALRRTIG*HRPVR*GRRES--FSG--R 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNI-LFGQPMDSQRYEEVVKKCALERDFDLlplrdNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:NF000106 105 ENLyMIGR*LDLSRKDARARADELLERFSL-----TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442622995 659 ARHLFDQcVRGHLRGSTVVLVTHQ-----EQF---LPHVDQIVILANGQIKAL 703
Cdd:NF000106 180 RNEVWDE-VRSMVRDGATVLLTTQymeeaEQLaheLTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
516-718 |
5.18e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 516 TLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS----LSYTSQ-----ESWL------------- 573
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFShitrLSFEQLqklvsDEWQrnntdmlspgedd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 574 FSGTVRQNILFGQPmDSQRYEEvvkkcaLERDFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PRK10938 98 TGRTTAEIIQDEVK-DPARCEQ------LAQQFGITALLD-----RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 654 VDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPH-VDQIVILANGQIKALGDYESLLKTGLITGL 718
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQALVAQL 231
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1150-1192 |
5.36e-06 |
|
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: 47.33 E-value: 5.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442622995 1150 GIVGRTGAGKSSLINALFRLSYTDGSVLID-TRDTR----QMGLHDLR 1192
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPtTRAAQayvwQTGGDGLV 48
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1135-1326 |
5.57e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIdtrdtRQMGLhdlrrQISIIPQepvlfsgtmRYNLD 1214
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----RNGKL-----RIGYVPQ---------KLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1215 PFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTN-FSVGQRQLVCLARAILRENRILVMDEATANVDpqTDG-- 1291
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD--VNGqv 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442622995 1292 ----LIQaTIRSKFrDCTVLTIAHRLHTII-DSDKVMVMD 1326
Cdd:PRK09544 158 alydLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
501-711 |
5.85e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 501 IRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLfSG--TV 578
Cdd:PRK13546 24 MKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGqlTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 579 RQNILFGQ-PMDSQRYE------EVVKKCALErDFDLLPLRDntivgergatLSGGQKARISLARSVYRKASIYLLDDPL 651
Cdd:PRK13546 103 IENIEFKMlCMGFKRKEikamtpKIIEFSELG-EFIYQPVKK----------YSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 652 SAVDASVARHLFDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKALGDYESLLK 711
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1136-1334 |
5.88e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALF---RLsyTDGSVLIDTRDTRQMGLHDLrrqISIIPQE-------PVLF 1205
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRL--ASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1206 SGTM---RYNLDPFDEYSDEKLWGCLEEVkLKEVvsDLPDGLASKISEggtnFSVGQRQLVCLARAILRENRILVMDEAT 1282
Cdd:PRK15056 98 EDVVmmgRYGHMGWLRRAKKRDRQIVTAA-LARV--DMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442622995 1283 ANVDPQTDGLIQATIRsKFRD--CTVLTIAHRLHTIIDSDKVMVMDAGRVVEFG 1334
Cdd:PRK15056 171 TGVDVKTEARIISLLR-ELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1099-1331 |
6.84e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1099 LEAPDDKKPPKTwpeqGEIIFKELNLRYTPNAKAEnVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL-SYTDGSVL 1177
Cdd:COG3845 242 VLLRVEKAPAEP----GEVVLEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLrPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1178 IDTRDTRQMGLHDLRRQ-ISIIPQEP-----VLfSGTMRYNLDpFDEYSDEKL--WGCLEEVKLKEVVSDL-------PD 1242
Cdd:COG3845 317 LDGEDITGLSPRERRRLgVAYIPEDRlgrglVP-DMSVAENLI-LGRYRRPPFsrGGFLDRKAIRAFAEELieefdvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1243 GLASKISeggtNFSVGQRQLVCLARAILRENRILVMDEATANVDpqtdglIQAT--IRSKFRD-----CTVLTIAHRLHT 1315
Cdd:COG3845 395 GPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD------VGAIefIHQRLLElrdagAAVLLISEDLDE 464
|
250
....*....|....*..
gi 442622995 1316 IID-SDKVMVMDAGRVV 1331
Cdd:COG3845 465 ILAlSDRIAVMYEGRIV 481
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
517-681 |
7.37e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG----------------SLSYTSQES-WLFSGTVR 579
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 580 QNILFGQPMDSQRYEEVVKKCALERD-FDLLPLRDNTIVgergaTLSGGQKARISLARSVYRKASIYLLDDPLSAVDASV 658
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDkVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....*.
gi 442622995 659 AR---HLFDQCVRghlRGSTVVLVTH 681
Cdd:PRK10908 173 SEgilRLFEEFNR---VGVTVLMATH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1117-1331 |
7.44e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYTPNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSY-TDGSVLIDTRDTRQMGLHD---LR 1192
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA---LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDITRLKNREvpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1193 RQISIIPQEPVLFSGTMRYnldpfDEYSDEKLWGCLEEVKLKEVVSDLPD--GLASKISEGGTNFSVGQRQLVCLARAIL 1270
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVY-----DNVAIPLIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 1271 RENRILVMDEATANVDpqtDGLIQATIR--SKFR--DCTVLTIAHRLHTIIDSD-KVMVMDAGRVV 1331
Cdd:PRK10908 154 NKPAVLLADEPTGNLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1149-1168 |
7.99e-06 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 49.38 E-value: 7.99e-06
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
848-991 |
8.06e-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: 49.43 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 848 ILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAG 927
Cdd:cd18563 54 VLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIG 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622995 928 IIIVIANVNP------LLLVPTLMLSVIFY--HLRNLYLKTSRdlkrveaiNRSPVYSHLAASLNGLTTIRA 991
Cdd:cd18563 134 IGVVLFSLNWklallvLIPVPLVVWGSYFFwkKIRRLFHRQWR--------RWSRLNSVLNDTLPGIRVVKA 197
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
844-1014 |
8.18e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.43 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 844 TLIIILSVIMNLSSSFLLFNIAK-KASIRLHNTI--------FNRVTRADMHFFSINKHGSILNRFTkDMSQVDEVLPVV 914
Cdd:cd18555 40 LLNVLGIGILILFLLYGLFSFLRgYIIIKLQTKLdkslmsdfFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 915 LVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDA 994
Cdd:cd18555 119 VISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS 198
|
170 180
....*....|....*....|
gi 442622995 995 QRVLEKEFDSYQDAHSSAFF 1014
Cdd:cd18555 199 EKNIYKKWENLFKKQLKAFK 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
517-684 |
8.67e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAI-----LGELKANSGQLQVNGSLSYTS---------------QESWLFSG 576
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNILFGQPMDSQR--YEEVVKKcALERDFDLLPLRDNtiVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAV 654
Cdd:PRK14243 106 SIYDNIAYGARINGYKgdMDELVER-SLRQAALWDEVKDK--LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|...
gi 442622995 655 DA-SVAR--HLFDQCVRGHlrgsTVVLVTHQEQ 684
Cdd:PRK14243 183 DPiSTLRieELMHELKEQY----TIIIVTHNMQ 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
422-698 |
1.01e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 422 IAFmiTAYYNVLLAAMSIYVPSAIiQTAQFLTSIRRVEQFMQSEELGSSDKSEGPSKDTVPGNPP----SNNNEADLLKS 497
Cdd:TIGR00956 676 IGF--TVFFFFVYILLTEFNKGAK-QKGEILVFRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDltdeSDDVNDEKDME 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 498 AISIRDLKaKWDPNSPDYTLSGINLEI--------KPGSVVAVIGLTGSGKSSLIQAILGELKA---NSGQLQVNG---- 562
Cdd:TIGR00956 753 KESGEDIF-HWRNLTYEVKIKKEKRVIlnnvdgwvKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGrpld 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 563 -----SLSYTSQESW-LFSGTVRQNILFG----QPMDSQRYEevvKKCALERDFDLLPLRD--NTIVGERGATLSGGQKA 630
Cdd:TIGR00956 832 ssfqrSIGYVQQQDLhLPTSTVRESLRFSaylrQPKSVSKSE---KMEYVEEVIKLLEMESyaDAVVGVPGEGLNVEQRK 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 631 RISLA-RSVYRKASIYLLDDPLSAVDASVA-------RHLFDQcvrghlrGSTVVLVTHQ------EQFlphvDQIVILA 696
Cdd:TIGR00956 909 RLTIGvELVAKPKLLLFLDEPTSGLDSQTAwsicklmRKLADH-------GQAILCTIHQpsailfEEF----DRLLLLQ 977
|
..
gi 442622995 697 NG 698
Cdd:TIGR00956 978 KG 979
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
529-693 |
1.09e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 529 VVAVIGLTGSGKSSLIQAIL----GELKANSGQLQVNGSLsytsqeswLFSGTVRQNI------LFGQPMDSQRYEEVVK 598
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKL--------IREGEVRAQVklafenANGKKYTITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 599 KCALERDFDLLPLrdntIVGERGaTLSGGQKA------RISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLR 672
Cdd:cd03240 96 NVIFCHQGESNWP----LLDMRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKS 170
|
170 180
....*....|....*....|...
gi 442622995 673 GST--VVLVTHQEQFLPHVDQIV 693
Cdd:cd03240 171 QKNfqLIVITHDEELVDAADHIY 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1135-1299 |
1.50e-05 |
|
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: 47.49 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1135 VLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLID------TRDTRQMGLHDLRRQISIipqEPVLfsg 1207
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLLNggpldfQRDSIARGLLYLGHAPGI---KTTL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1208 TMRYNLDPF-DEYSDEKLWGCLEEVKLKEVvSDLPDGlaskiseggtNFSVGQRQLVCLARAILRENRILVMDEATANVD 1286
Cdd:cd03231 89 SVLENLRFWhADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|...
gi 442622995 1287 PQTDGLIQATIRS 1299
Cdd:cd03231 158 KAGVARFAEAMAG 170
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
501-700 |
1.52e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 501 IRDLKAKWDPNSPDyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGEL----KANSGQLQVNG------------SL 564
Cdd:TIGR00956 62 FRKLKKFRDTKTFD-ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGitpeeikkhyrgDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 565 SYTSQESWLF-SGTVRQNILFGQPMDS--QRYEEVVKKCALERDFDL------LPLRDNTIVGE---RGatLSGGQKARI 632
Cdd:TIGR00956 141 VYNAETDVHFpHLTVGETLDFAARCKTpqNRPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRG--VSGGERKRV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 633 SLARSVYRKASIYLLDDPLSAVDASVARHlFDQCVR--GHLRGSTVVLVTHQ------EQFlphvDQIVILANGQI 700
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALE-FIRALKtsANILDTTPLVAIYQcsqdayELF----DKVIVLYEGYQ 289
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1127-1369 |
1.56e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.06 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1127 TPNAKAENVLKS---------LSFVIQPREKVGIVGRTGAGKSSLINAL--FRLSyTDGSVLIDTRDTRQMGLHdlRRQI 1195
Cdd:PRK11607 17 TPLLEIRNLTKSfdgqhavddVSLTIYKGEIFALLGASGCGKSTLLRMLagFEQP-TAGQIMLDGVDLSHVPPY--QRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1196 SIIPQEPVLFSG-TMRYNLD--------PFDEYSDeKLWGCLEEVKLKEVVSDLPDGLaskiseggtnfSVGQRQLVCLA 1266
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAfglkqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1267 RAILRENRILVMDEATANVDPQTDGLIQ---ATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSP---YELM 1340
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQlevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPeeiYEHP 241
|
250 260
....*....|....*....|....*....
gi 442622995 1341 TKSDSKVFHNLVNQsgrasYEGLLKIAQE 1369
Cdd:PRK11607 242 TTRYSAEFIGSVNV-----FEGVLKERQE 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
526-686 |
1.66e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 526 PGSVVAVIGLTGSGKSSLIQAILgelkansgqlqvngslsytsqesWLFSGtvRQNILFGQPMDSQRYEEvvkkcalerd 605
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGCIV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 606 fdllPLRDNTIVGERGaTLSGGQKARISLArSVYRKASI-----YLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVT 680
Cdd:cd03227 65 ----AAVSAELIFTRL-QLSGGEKELSALA-LILALASLkprplYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT 138
|
....*.
gi 442622995 681 HQEQFL 686
Cdd:cd03227 139 HLPELA 144
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
845-1024 |
2.11e-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: 48.33 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHG---SILNrftKDMSQVDEVLPVVLVDVMQI 921
Cdd:cd18565 62 AAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGdlmSVLN---NDVNQLERFLDDGANSIIRV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 922 ALWLAGIIIVIANVNPLL-LVPTLMLSVIFY-------HLRNLYLKTsRdlKRVEAINrspvySHLAASLNGLTTIRALD 993
Cdd:cd18565 139 VVTVLGIGAILFYLNWQLaLVALLPVPLIIAgtywfqrRIEPRYRAV-R--EAVGDLN-----ARLENNLSGIAVIKAFT 210
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442622995 994 AQRV----LEKEFDSYQDAH------SSAFF--MYISTSQAFG 1024
Cdd:cd18565 211 AEDFererVADASEEYRDANwrairlRAAFFpvIRLVAGAGFV 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1256-1339 |
2.15e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.49 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1256 SVGQRQLVCLARAILRENRILVMDEATANVDpqtdgliqATIRSKFR----------DCTVLTIAH-RLHTIIDSDKVMV 1324
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD--------AALRVQMRieisrlhkrlGRTMIYVTHdQVEAMTLADKIVV 206
|
90
....*....|....*
gi 442622995 1325 MDAGRVVEFGSPYEL 1339
Cdd:PRK11000 207 LDAGRVAQVGKPLEL 221
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1148-1168 |
3.13e-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: 44.53 E-value: 3.13e-05
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
839-1034 |
4.49e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 47.08 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 839 DVYKYTLII----ILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVL--P 912
Cdd:cd18577 45 DVNKYALYFvylgIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIgeK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 913 VVLVdVMQIALWLAGIII----------VIanvnpLLLVPTLMLSVIFYhlrnlylkTSRDLKRVEAINRSpvYSHLAA- 981
Cdd:cd18577 125 LGLL-IQSLSTFIAGFIIafiyswkltlVL-----LATLPLIAIVGGIM--------GKLLSKYTKKEQEA--YAKAGSi 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 982 ---SLNGLTTIRALDAQRVLEKEFDSY-QDAHSSAFFMYISTSQAFGYCMNCICVIY 1034
Cdd:cd18577 189 aeeALSSIRTVKAFGGEEKEIKRYSKAlEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
517-693 |
4.76e-05 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSL-IQAILGElkansGQLQVNGSLS-YTSQeswlFSG-----------------T 577
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAE-----GQRRYVESLSaYARQ----FLGqmdkpdvdsieglspaiA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 578 VRQNILFGQPMDSqryeeVVKKCALERDFDLLPLRDNTI--------VG------ERGA-TLSGGQKARISLARSVYRKA 642
Cdd:cd03270 82 IDQKTTSRNPRST-----VGTVTEIYDYLRLLFARVGIRerlgflvdVGlgyltlSRSApTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 643 S--IYLLDDPLSAVDASVARHLFDqcVRGHLR--GSTVVLVTHQEQFLPHVDQIV 693
Cdd:cd03270 157 TgvLYVLDEPSIGLHPRDNDRLIE--TLKRLRdlGNTVLVVEHDEDTIRAADHVI 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1117-1334 |
4.81e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1117 IIFKELNLRYtpnaKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRL------------SYTDGSVLIDTRDTR 1184
Cdd:PRK11124 3 IQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLemprsgtlniagNHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1185 QmglhdLRRQISIIPQEpvlfsgtmrYNLDPF------------------DEYSDEKLWGCLEEVKLKEVVSDLPDGLas 1246
Cdd:PRK11124 79 E-----LRRNVGMVFQQ---------YNLWPHltvqqnlieapcrvlglsKDQALARAEKLLERLRLKPYADRFPLHL-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1247 kiseggtnfSVGQRQLVCLARAILRENRILVMDEATANVDPQtdglIQATIRSKFRDCT-------VLT----IAHRLHT 1315
Cdd:PRK11124 143 ---------SGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQIVSIIRELAetgitqvIVTheveVARKTAS 209
|
250
....*....|....*....
gi 442622995 1316 iidsdKVMVMDAGRVVEFG 1334
Cdd:PRK11124 210 -----RVVYMENGHIVEQG 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
499-711 |
5.98e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 499 ISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILG--ELKANSGQLQVNGS--LSYTSQES--- 571
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPEDRage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 572 ---WLFSGTVR----QNILFGQ-------------PMDSQRYEEVvkkcaLERDFDLLPLRDNTIVGERGATLSGGQKAR 631
Cdd:PRK09580 79 gifMAFQYPVEipgvSNQFFLQtalnavrsyrgqePLDRFDFQDL-----MEEKIALLKMPEDLLTRSVNVGFSGGEKKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 632 ISLARSVYRKASIYLLDDPLSAVDASvARHLFDQCVRGHLRGS-TVVLVTHQEQFLPHV--DQIVILANGQIKALGDYeS 708
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDID-ALKIVADGVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDF-T 231
|
...
gi 442622995 709 LLK 711
Cdd:PRK09580 232 LVK 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
517-690 |
6.22e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 517 LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN--SGQLQVNG---------------------SLSYTSQESWL 573
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkqetfarisgyceqndihSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 574 FSGTVRQnilfgqPMDSQRYEEVVKKCALERDFDLLPLRDnTIVGERGAT-LSGGQKARISLARSVYRKASIYLLDDPLS 652
Cdd:PLN03140 976 YSAFLRL------PKEVSKEEKMMFVDEVMELVELDNLKD-AIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|....*....
gi 442622995 653 AVDASVARhLFDQCVRGHL-RGSTVVLVTHQeqflPHVD 690
Cdd:PLN03140 1049 GLDARAAA-IVMRTVRNTVdTGRTVVCTIHQ----PSID 1082
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1152-1344 |
6.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1152 VGRTGAGKSS---LINALfrLSYTDGSVLID----TRDTRQMGLHDLRRQISIIPQ--EPVLFSGT----MRYNLDPFDE 1218
Cdd:PRK13649 39 IGHTGSGKSTimqLLNGL--HVPTQGSVRVDdtliTSTSKNKDIKQIRKKVGLVFQfpESQLFEETvlkdVAFGPQNFGV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1219 YSDEKLWGCLEEVKLKEVVSDLPDglaskisEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIR 1298
Cdd:PRK13649 117 SQEEAEALAREKLALVGISESLFE-------KNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442622995 1299 SKFRD-CTVLTIAHRLHTIID-SDKVMVMDAGRVVEFGSPYELMTKSD 1344
Cdd:PRK13649 190 KLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQDVD 237
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
876-1009 |
6.84e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 46.33 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 876 IFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLL-------LVPTLMLSV 948
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLalvalaaLPPLALATR 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442622995 949 IFYHL-RNLYLKTsRDlkRVEAINrspvySHLAASLNGLTTIRALDAQRVLEKEF----DSYQDAH 1009
Cdd:cd18546 158 WFRRRsSRAYRRA-RE--RIAAVN-----ADLQETLAGIRVVQAFRRERRNAERFaelsDDYRDAR 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
523-699 |
7.56e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 523 EIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG-SLSYTSQEswlfsgtvrqnilfgqpmdsqryeevvkkca 601
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 602 lerdfdllplrdntivgergATLSGGQKARISLARSVYRKASIYLLDDPLSAVD-------ASVARHLFDQCVRghlrgs 674
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEEGKK------ 123
|
170 180
....*....|....*....|....*
gi 442622995 675 TVVLVTHQEQFLPHVDQIVILANGQ 699
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
835-911 |
9.94e-05 |
|
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: 45.76 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 835 SKSMDVYKyTLIIILSVImNLSSSFL------LFNIAK-KASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQV 907
Cdd:cd18784 29 EKSQDKFS-RAIIIMGLL-AIASSVAagirggLFTLAMaRLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTM 106
|
....
gi 442622995 908 DEVL 911
Cdd:cd18784 107 SDTV 110
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1128-1328 |
1.48e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1128 PNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLI--------DTRDTRQMGlhdlrrqISII 1198
Cdd:PRK10762 15 PGVKA---LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSILYlgkevtfnGPKSSQEAG-------IGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1199 PQEPVLFSG-TMRYNLDPFDEYSDEklWGCLEEVKLKEVVSDLPDGL----ASKISEGgtNFSVGQRQLVCLARAILREN 1273
Cdd:PRK10762 85 HQELNLIPQlTIAENIFLGREFVNR--FGRIDWKKMYAEADKLLARLnlrfSSDKLVG--ELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442622995 1274 RILVMDEAT-ANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAG 1328
Cdd:PRK10762 161 KVIIMDEPTdALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-562 |
2.27e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 2.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 512 SPDYT----LSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNG 562
Cdd:COG4586 29 RREYReveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
844-949 |
2.49e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 44.73 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 844 TLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIAL 923
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100
....*....|....*....|....*.
gi 442622995 924 WLAGIIIVIANVNPLLLVptLMLSVI 949
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTL--VTLAVV 146
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
845-991 |
2.54e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.78 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLF---NIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQI 921
Cdd:cd18575 41 LLLAVALVLALASALRFYlvsWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRN 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 922 ALWLAGIIIVIANVNP------LLLVPTLMLSVIFY--HLRNLYlKTSRDlkRVEAINrspvySHLAASLNGLTTIRA 991
Cdd:cd18575 121 LLLLIGGLVMLFITSPkltllvLLVIPLVVLPIILFgrRVRRLS-RASQD--RLADLS-----AFAEETLSAIKTVQA 190
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1258-1341 |
3.12e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1258 GQRQLVCLARAILRENRILVMDEATANVDPQTdgliQATIrskFR---------DCTVLTIAHRLHTIID-SDKVMVMDA 1327
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQI---FRlltrlnqnnNTTILLISHDLQMLSQwADKINVLYC 234
|
90
....*....|....
gi 442622995 1328 GRVVEFGSPYELMT 1341
Cdd:PRK15093 235 GQTVETAPSKELVT 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1139-1322 |
3.57e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 43.25 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1139 LSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTRQMGlHDLRRQISII-----------PQEPVLFS 1206
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDaGEVLWQGEPIRRQR-DEYHQDLLYLghqpgikteltALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1207 GTMRynldpfDEYSDEKLWGCLEEVKLKEvVSDLPDGlaskiseggtNFSVGQRQLVCLARAILRENRILVMDEA-TAnV 1285
Cdd:PRK13538 99 QRLH------GPGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPfTA-I 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 442622995 1286 DPQTDGLIQATIRSKFRD--CTVLTIAHRLHtiIDSDKV 1322
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQggMVILTTHQDLP--VASDKV 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
515-658 |
3.74e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 515 YTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILgELKANSGQLQVNGS----------LSYTSQESWLFSG-------- 576
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQplhnlnrrqlLPVRHRIQVVFQDpnsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 -TVRQNILFG----QPMDS--QRYEEVVKkcALERdfdllplrdntiVGERGAT-------LSGGQKARISLARSVYRKA 642
Cdd:PRK15134 379 lNVLQIIEEGlrvhQPTLSaaQREQQVIA--VMEE------------VGLDPETrhrypaeFSGGQRQRIAIARALILKP 444
|
170
....*....|....*.
gi 442622995 643 SIYLLDDPLSAVDASV 658
Cdd:PRK15134 445 SLIILDEPTSSLDKTV 460
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1139-1352 |
4.19e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.53 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1139 LSFVIQPREKVGIVGRTGAGKSSLINALFRL-----SYTDGSVLIDTRdtrQMGLHDLR-RQISIIPQEP-VLFSG--TM 1209
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagvRQTAGRVLLDGK---PVAPCALRgRKIATIMQNPrSAFNPlhTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 RYN-----LDPFDEYSDEKLWGCLEEVKLKEVvSDLPDGLASKISEGgtnfsVGQRQLVCLAraILRENRILVMDEATAN 1284
Cdd:PRK10418 99 HTHaretcLALGKPADDATLTAALEAVGLENA-ARVLKLYPFEMSGG-----MLQRMMIALA--LLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1285 VDpqtdGLIQATIRS------KFRDCTVLTIAH------RLhtiidSDKVMVMDAGRVVEFGSPYELMTKSDSKVFHNLV 1352
Cdd:PRK10418 171 LD----VVAQARILDllesivQKRALGMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
501-563 |
4.50e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 4.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 501 IRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGE--LKANSGQLQVNGS 563
Cdd:CHL00131 10 IKNLHASVNENE---ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGE 71
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1145-1336 |
5.38e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1145 PREKVGIVGRTGAGKSSLINALFRLSYTDGS--VLIDTRDTRQMGLHDLRRQIsiipqepvlfsgtmrynldpfdeysde 1222
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1223 klwgcleevklkevvsdlpdglaskISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRS--- 1299
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442622995 1300 ----KFRDCTVLTIAHRLHTIIdsDKVMVMDAGRVVEFGSP 1336
Cdd:smart00382 109 lllkSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1128-1331 |
5.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1128 PNAKAenvLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTD-GSVLIDTRDTR-QMGLHDLRRQISIIPQE--PV 1203
Cdd:PRK10982 9 PGVKA---LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDsGSILFQGKEIDfKSSKEALENGISMVHQElnLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1204 LFSGTM------RYNLDPFdeYSDEKlwgcleevKLKEVVSDLPDGLASKIS--EGGTNFSVGQRQLVCLARAILRENRI 1275
Cdd:PRK10982 86 LQRSVMdnmwlgRYPTKGM--FVDQD--------KMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442622995 1276 LVMDEATANV-DPQTDGLIQATIRSKFRDCTVLTIAHRLHTIID-SDKVMVMDAGRVV 1331
Cdd:PRK10982 156 VIMDEPTSSLtEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1141-1289 |
5.85e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1141 FVIQPREKVGIVGRTGAGKSSLINALfrlsytDGSVLIDtrDTRQMGLHDLRrqISIIPQEP---VlfSGTM-------- 1209
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLD--DGRIIYEQDLI--VARLQQDPprnV--EGTVydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1210 --------RYN---LDPFDEYSD------EKLWGCLE-------EVKLKEVVSDL---PDGLASKISeGGTnfsvgQRQl 1262
Cdd:PRK11147 92 eeqaeylkRYHdisHLVETDPSEknlnelAKLQEQLDhhnlwqlENRINEVLAQLgldPDAALSSLS-GGW-----LRK- 164
|
170 180
....*....|....*....|....*..
gi 442622995 1263 VCLARAILRENRILVMDEATANVDPQT 1289
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
577-663 |
6.79e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 577 TVRQNI-----LFGQPMDS--QRYEEVVkkcaleRDFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDD 649
Cdd:NF033858 355 TVRQNLelharLFHLPAAEiaARVAEML------ERFDLADVAD-----ALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
90
....*....|....
gi 442622995 650 PLSAVDaSVARHLF 663
Cdd:NF033858 424 PTSGVD-PVARDMF 436
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
1150-1198 |
7.15e-04 |
|
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: 41.67 E-value: 7.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 442622995 1150 GIVGRTGAGKSSLINALFRLSYTDGSVLIDT---RDTRQMGLHDLRRQISII 1198
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTtrdPDVYVKELDKGKVKLVLV 52
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1244-1342 |
7.63e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1244 LASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRD-CTVLTIAHRLHTIID-SDK 1321
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHE 213
|
90 100
....*....|....*....|.
gi 442622995 1322 VMVMDAGRVVEFGSPYELMTK 1342
Cdd:NF000106 214 LTVIDRGRVIADGKVDELKTK 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1113-1334 |
7.83e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1113 EQGEIIFKELNLRYTPNAKAEN--VLKSLSFVIQPREKVGIVGRTGAGKSSLINALF-RLS---YTDGSVL-----IDTR 1181
Cdd:TIGR00956 754 ESGEDIFHWRNLTYEVKIKKEKrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTtgvITGGDRLvngrpLDSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1182 DTRQMGL---HDLRRQISIIpQEPVLFSGTMR----YNLDPFDEYSDE--KLwgcLEEVKLKEVVSDLPdglaskisegG 1252
Cdd:TIGR00956 834 FQRSIGYvqqQDLHLPTSTV-RESLRFSAYLRqpksVSKSEKMEYVEEviKL---LEMESYADAVVGVP----------G 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1253 TNFSVGQRQLVCLARAILRENRILV-MDEATANVDPQTDGLIQATIRsKFRDC--TVLTIAHRLHTII--DSDKVMVMD- 1326
Cdd:TIGR00956 900 EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSAILfeEFDRLLLLQk 978
|
....*...
gi 442622995 1327 AGRVVEFG 1334
Cdd:TIGR00956 979 GGQTVYFG 986
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
491-571 |
8.38e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 491 EADLLKSAISIRDLKAKWDPNSpdyTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQ--VNGSLSYTS 568
Cdd:PRK15064 312 DKKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYA 388
|
...
gi 442622995 569 QES 571
Cdd:PRK15064 389 QDH 391
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1136-1298 |
9.14e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.69 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1136 LKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGS------VLIDT--------RDTRQMGLHD--LRRQISIIP 1199
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshieLLGRTvqregrlaRDIRKSRANTgyIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 1200 QEPVL---FSGTM------RYNLDPFDEYSDEKLWGCLEEVklkevvsdlpdGLASKISEGGTNFSVGQRQLVCLARAIL 1270
Cdd:PRK09984 100 RLSVLenvLIGALgstpfwRTCFSWFTREQKQRALQALTRV-----------GMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180
....*....|....*....|....*...
gi 442622995 1271 RENRILVMDEATANVDPQTDGLIQATIR 1298
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLR 196
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
845-1004 |
1.28e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.50 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 845 LIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALW 924
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 925 LAGIIIVIANVNPLL----LVPTLMLSVIFYHLRNLYLKTSRDLKRVEainrspvySHLAA----SLNGLTTIRALDAQR 996
Cdd:cd18564 142 LVGMLGVMFWLDWQLaliaLAVAPLLLLAARRFSRRIKEASREQRRRE--------GALASvaqeSLSAIRVVQAFGREE 213
|
....*...
gi 442622995 997 VLEKEFDS 1004
Cdd:cd18564 214 HEERRFAR 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
624-712 |
1.90e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 624 LSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLfDQCVRGHLRGSTVVLVTHQ-EQFLPHVDQIVILANGQIKA 702
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNlAQAARISDRAALFFDGRLVE 242
|
90
....*....|
gi 442622995 703 LGDYESLLKT 712
Cdd:PRK14271 243 EGPTEQLFSS 252
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
1150-1168 |
2.14e-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: 40.31 E-value: 2.14e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
619-711 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 619 ERGA-TLSGGQKARISLARSVYRKAS--IYLLDDPlsavdaSVARHLFD-----QCVRgHLR--GSTVVLVTHQEQFLPH 688
Cdd:TIGR00630 483 SRAAgTLSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnrrliNTLK-RLRdlGNTLIVVEHDEDTIRA 555
|
90 100
....*....|....*....|....*....
gi 442622995 689 VDQIVILA------NGQIKALGDYESLLK 711
Cdd:TIGR00630 556 ADYVIDIGpgagehGGEVVASGTPEEILA 584
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
529-550 |
2.75e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.68 E-value: 2.75e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
622-693 |
3.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 622 ATLSGGQKARISLARSVYRKAS--IYLLDDP---LSAVDA----SVARHLFDQcvrghlrGSTVVLVTHQEQFLPHVDQI 692
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPsigLHPQDThkliNVIKKLRDQ-------GNTVLLVEHDEQMISLADRI 547
|
.
gi 442622995 693 V 693
Cdd:PRK00635 548 I 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
518-658 |
3.40e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 518 SGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKAN-----SGQLQVNG-SLSYTSQESwlFSGtVRQN---ILFGQPM 588
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGeSLLHASEQT--LRG-VRGNkiaMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 589 DS---------QRYEEVvkkcALERDFDLLPLRDNTI-----VGERGAT---------LSGGQKARISLARSVYRKASIY 645
Cdd:PRK15134 103 VSlnplhtlekQLYEVL----SLHRGMRREAARGEILncldrVGIRQAAkrltdyphqLSGGERQRVMIAMALLTRPELL 178
|
170
....*....|...
gi 442622995 646 LLDDPLSAVDASV 658
Cdd:PRK15134 179 IADEPTTALDVSV 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
590-712 |
3.66e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 590 SQRYEEVVKKCALeRDFDLLPLRDNTIVG----------ERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVA 659
Cdd:PLN03073 302 SQRLEEIYKRLEL-IDAYTAEARAASILAglsftpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAV 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 660 RHLFDQCVRGhlrGSTVVLVTHQEQFLPHVDQIVILANGQ--IKALGDYESLLKT 712
Cdd:PLN03073 381 LWLETYLLKW---PKTFIVVSHAREFLNTVVTDILHLHGQklVTYKGDYDTFERT 432
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
787-930 |
4.72e-03 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 40.72 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 787 GGGLVAFLVMLSSSVlaQVAVTGGDYFLTYWVKKESTAAGHGEMEDMESKSMDVYkYTLIIILSVIMNLSSSFLLFNIAK 866
Cdd:cd18558 12 GGLLPAFMVIFGDMT--DSFTNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYY-YLIIGAIVLITAYIQGSFWGLAAG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442622995 867 KASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQ-IALWLAGIII 930
Cdd:cd18558 89 RQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQnIATFGTGFII 153
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
511-687 |
5.17e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 511 NSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWL----------FSGTVRQ 580
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCtyighnlglkLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 581 NILFGqpmdSQRYEEVVKKCALERDFDLLPLRDntivgERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVAR 660
Cdd:PRK13541 90 NLKFW----SEIYNSAETLYAAIHYFKLHDLLD-----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|....*..
gi 442622995 661 HLFDQCVRGHLRGSTVVLVTHQEQFLP 687
Cdd:PRK13541 161 LLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
520-703 |
5.43e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.92 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 520 INLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGS--------------LSYTSQ---ESWLFSG-TVRQN 581
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrDNGFFPNfSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622995 582 ILFGQPMDSQRY-------EEVVKKCALERDFDLLPLRDNTIvgERGAT-LSGGQKARISLARSVYRKASIYLLDDPLSA 653
Cdd:PRK09700 362 MAISRSLKDGGYkgamglfHEVDEQRTAENQRELLALKCHSV--NQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442622995 654 VDA-------SVARHLFDQcvrghlrGSTVVLVTHQeqfLPHV----DQIVILANGQIKAL 703
Cdd:PRK09700 440 IDVgakaeiyKVMRQLADD-------GKVILMVSSE---LPEIitvcDRIAVFCEGRLTQI 490
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
1148-1168 |
6.52e-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: 39.01 E-value: 6.52e-03
|
| |
