|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-527 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 1215.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYEDFS 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHEELWAVKAERDRIYSLPEMSEADGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 161 KLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 241 MTAAEQARERLLSDNAKKKAQIAELQSFVSRFSANASKAKQATSRARQIDKIQLEEVKPSSRVSPFIRFEQYKKLHRQAV 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHADDFADDMS 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 LFDWMAQWTQGG--EQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLA 478
Cdd:PRK15064 401 LFDWMSQWRQEGddEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489202159 479 LDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDYLRSQGV 527
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-523 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 766.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYEDFSVIDTV 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGHEELWAVKAERDRIYSLPEMSEADGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAVAPGWKLRVL 165
Cdd:COG0488 83 LDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEYMTAAE 245
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 246 QARERLLSDNAKKKAQIAELQSFVSRFSANASKAKQATSRARQIDKIQLEEVKPSSRvSPFIRFEQYKKLHRQAVTVENI 325
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELEGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 326 SKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHaDDFADDMSLFDWM 405
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 406 AQWTQGG-EQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG 484
Cdd:COG0488 401 RDGAPGGtEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 489202159 485 TLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDYLR 523
Cdd:COG0488 481 TVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-520 |
8.17e-103 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 322.29 E-value: 8.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYEDFS 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHEELWAVKAERDRIYSLPEMSEADGM--AVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQhfgPMSAVAP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 239 EYMTAAEQA-R-ERLlsDNA---KKKAQiAEL---QSFVSRFSAN-----ASKA-KQATSRARQID---KIQLEEVKPSS 301
Cdd:PRK11147 240 QYLLEKEEAlRvEEL--QNAefdRKLAQ-EEVwirQGIKARRTRNegrvrALKAlRRERSERREVMgtaKMQVEEASRSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 302 RvspfIRFEqykklhrqavtVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS 381
Cdd:PRK11147 317 K----IVFE-----------MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 382 ADVGYFAQdHADDFADDMSLFDWMAQWTQ-----GGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPN 456
Cdd:PRK11147 382 LEVAYFDQ-HRAELDPEKTVMDNLAEGKQevmvnGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 457 VLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATR--IIElGENGVTDFSGSYDD 520
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFE-GNGKIGRYVGGYHD 525
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-521 |
1.47e-98 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 311.33 E-value: 1.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYeDFS 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPAL-PQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHEELWAVKAErdriysLPEMSEA-DGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYD- 238
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 239 -EYMTAAEQARERLLSDNAKKKaqIAELQSFVSRFSANASKAKQATSRARQIDKIQLeeVKPSSRVSPF-IRFEQYKKLH 316
Cdd:PRK10636 234 fEVQRATRLAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 317 RQAVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHADDFA 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 DDMSLFDWMAQWT-QGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL 475
Cdd:PRK10636 390 ADESPLQHLARLApQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 489202159 476 NLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDY 521
Cdd:PRK10636 470 TEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-521 |
2.49e-88 |
|
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: 282.21 E-value: 2.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYEDFSVIDTVIMGHEELW 93
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 94 AVKAERDRIYSLPEMSEADGMAV----AELEVQFAEFDGYTAESRAGELLLGLGIPLEQhfGPMSAVAPGWKLRVLLAQA 169
Cdd:TIGR03719 98 DALDRFNEISAKYAEPDADFDKLaaeqAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 170 LFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEYMtaaEQARE 249
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL---EQKQK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 250 RLL----SDNAKKKAQIAELQsfvsrFSANASKAKQATSRAR--QIDKIQLEEVKPSSRVSPfIRFEQYKKLHRQAVTVE 323
Cdd:TIGR03719 253 RLEqeekEESARQKTLKRELE-----WVRQSPKGRQAKSKARlaRYEELLSQEFQKRNETAE-IYIPPGPRLGDKVIEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 324 NISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHaDDFADDMSLFD 403
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DALDPNKTVWE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 404 WMAqwtqGGEQLV---------RGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEA 474
Cdd:TIGR03719 406 EIS----GGLDIIklgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489202159 475 LNLALDNYPGTLIFVSHDREFVSSLATRIIEL-GENGVTDFSGSYDDY 521
Cdd:TIGR03719 482 LEEALLNFAGCAVVISHDRWFLDRIATHILAFeGDSHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-521 |
3.34e-82 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 266.21 E-value: 3.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKIL-GNDlEPSAGQVMLEPNVRLGKLRQDQFAYEDFSVIDTVIMGHE 90
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMaGVD-KEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 91 ELWAVKAERDRIYSlpEMSEADG-----MA-VAELEVQFAEFDGYTAESRagelllglgipLEQhfgPMSAV------AP 158
Cdd:PRK11819 97 EVKAALDRFNEIYA--AYAEPDAdfdalAAeQGELQEIIDAADAWDLDSQ-----------LEI---AMDALrcppwdAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 ------GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRL 232
Cdd:PRK11819 161 vtklsgGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 233 FPGNYDEYMtaaEQARERLL----SDNAKKKAQIAELQsFVsRFSAnasKAKQATSRARqidkIQleevkpssrvspfiR 308
Cdd:PRK11819 241 WEGNYSSWL---EQKAKRLAqeekQEAARQKALKRELE-WV-RQSP---KARQAKSKAR----LA--------------R 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 309 FEQ-----YKK--------------LHRQAVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDL 369
Cdd:PRK11819 295 YEEllseeYQKrnetneifippgprLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 370 PVDGGEVKWTDSADVGYFAQDHaDDFADDMSLFDWMAqwtqGGEQLV---------RGTLGRMLFSNDEIKKSVKVISGG 440
Cdd:PRK11819 375 QPDSGTIKIGETVKLAYVDQSR-DALDPNKTVWEEIS----GGLDIIkvgnreipsRAYVGRFNFKGGDQQKKVGVLSGG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRII--ElGENGVTDFSGSY 518
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILafE-GDSQVEWFEGNF 528
|
...
gi 489202159 519 DDY 521
Cdd:PRK11819 529 QEY 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-523 |
1.26e-80 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 266.34 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMK----------------------ILGNDLepSAGQVM 59
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqeVVGDDT--TALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 60 LEPNVRLGKLRQdqfayEDFSVIDTVIMGHEELWAVKAERDRIYSLPEmsEADGMAVAELEVQFAEFDGYTAESRAGELL 139
Cdd:PLN03073 256 LNTDIERTQLLE-----EEAQLVAQQRELEFETETGKGKGANKDGVDK--DAVSQRLEEIYKRLELIDAYTAEARAASIL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 140 LGLGIPLEQHFGPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVC 219
Cdd:PLN03073 329 AGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 220 THMADLDYGELRLFPGNYDEY-MTAAEQARERLLSDNAKKKAQiAELQSFVSRFSANASKAKQATSRARQIDKI------ 292
Cdd:PLN03073 409 TDILHLHGQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLghvdav 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 293 ------QLEEVKPSSRVSPFIrfeqykklhrqaVTVENISKGYDGKP-LFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL 365
Cdd:PLN03073 488 vndpdyKFEFPTPDDRPGPPI------------ISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 366 VGDLPVDGGEVKWTDSADVGYFAQDHADDFADDMSLFDWMAQWTQGG-EQLVRGTLGRMLFSNDEIKKSVKVISGGEQGR 444
Cdd:PLN03073 556 SGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSR 635
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDYLR 523
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-510 |
1.63e-59 |
|
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: 193.43 E-value: 1.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQdhaddfaddm 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 slfdwmaqwtqggeqlvrgtlgrmlfsndeikksvkvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLAL 479
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180 190
....*....|....*....|....*....|.
gi 489202159 480 DNYPGTLIFVSHDREFVSSLATRIIELGENG 510
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-524 |
6.15e-59 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 203.76 E-value: 6.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHadDFADDMSL 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP--PLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 402 FDW---------------------MAQWTQGGEQL------------------VRGTLGRMLFSNDEIKKSVKVISGGEQ 442
Cdd:COG0488 79 LDTvldgdaelraleaeleeleakLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 443 GRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDYL 522
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
..
gi 489202159 523 RS 524
Cdd:COG0488 239 EQ 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-229 |
1.37e-42 |
|
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: 148.75 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQdqfayedfsvidtv 85
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 imgheelwavkaerdriyslpemseadgmavaelevqfaefdgytaesragelllglgipleqhfgpMSavaPGWKLRVL 165
Cdd:cd03221 71 -------------------------------------------------------------------LS---GGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-525 |
1.87e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW------TDSADVGYFAQDHA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 393 DDFADDMSLFD-----------WMAQWTQGGEQLVRGTLGR--MLfsnDEIKKSVKVISGGEQGRMLFGRLILKRPNVLV 459
Cdd:COG1121 86 VDWDFPITVRDvvlmgrygrrgLFRRPSRADREAVDEALERvgLE---DLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 460 MDEPTNHLDMESIEAL-NL--ALDNYPGTLIFVSHDREFVSSLATRIIELGENGVtdFSGSYDDYLRSQ 525
Cdd:COG1121 163 LDEPFAGVDAATEEALyELlrELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTPE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-511 |
5.82e-36 |
|
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: 134.40 E-value: 5.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW--TDSAD---------VGYF 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgRDLASlsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHADDFadDMSLFD-----------WMAQWTQGGEQLVRGTLGRMlfsndEI----KKSVKVISGGEQGRMLFGRLIL 452
Cdd:COG1120 81 PQEPPAPF--GLTVRElvalgryphlgLFGRPSAEDREAVEEALERT-----GLehlaDRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 453 KRPNVLVMDEPTNHLD-------MESIEALNlalDNYPGTLIFVSHDREFVSSLATRIIELGENGV 511
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-508 |
1.03e-34 |
|
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: 129.52 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWT----DSADVGYFAQ----DH 391
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 ADDFADDMSLFDWMAQWTQ-GGEQLVRGTLGRML-------FSNdeikKSVKVISGGEQGRMLFGRLILKRPNVLVMDEP 463
Cdd:COG4133 83 ADGLKPELTVRENLRFWAAlYGLRADREAIDEALeavglagLAD----LPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 464 TNHLDMESIEALNLALDNYP---GTLIFVSHDREFVssLATRIIELGE 508
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
321-510 |
3.27e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA-----------DVGYFAQ 389
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DhADDFAD---DMSLFDWMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:COG4619 82 E-PALWGGtvrDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 467 LDMESIEALNLALDNYP----GTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG4619 161 LDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTL-EAG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-510 |
5.66e-32 |
|
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: 120.97 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK------WTDSAD----VGYFAQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEEvkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 dhaddfadDMSLFDWMaqwtQGGEQLvrgtlgrMLfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM 469
Cdd:cd03230 81 --------EPSLYENL----TVRENL-------KL-------------SGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489202159 470 ESIEALNLALDNY---PGTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:cd03230 129 ESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAIL-NNG 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
8.30e-32 |
|
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: 120.58 E-value: 8.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgklrqdqfayedfsv 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtvIMGHEELWAVKAERDRIYSLPEmseadgmavaelevQFAEFDGYTAEsragELLLglgipleqhfgpMSAvapGWK 161
Cdd:cd03230 59 ----VLGKDIKKEPEEVKRRIGYLPE--------------EPSLYENLTVR----ENLK------------LSG---GMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELlreLKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
320-522 |
1.33e-31 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 128.91 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQD--------- 390
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDpprnvegtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 ------------------HA--DDFADDMS--LFDWMAQW-----TQGGEQL---VRGTLGRMLFSNDeikKSVKVISGG 440
Cdd:PRK11147 84 ydfvaegieeqaeylkryHDisHLVETDPSekNLNELAKLqeqldHHNLWQLenrINEVLAQLGLDPD---AALSSLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDD 520
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQ 240
|
..
gi 489202159 521 YL 522
Cdd:PRK11147 241 YL 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
322-506 |
1.39e-31 |
|
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: 121.10 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK------WTDSADVGYFAQDHADDF 395
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 396 ADDMSLFDW--MAQWTQGG---------EQLVRGTLGRM-LFsnDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEP 463
Cdd:cd03235 82 DFPISVRDVvlMGLYGHKGlfrrlskadKAKVDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 464 TNHLDMESIEAL-----NLALDNYpgTLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03235 160 FAGVDPKTQEDIyellrELRREGM--TILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-512 |
2.83e-31 |
|
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: 119.08 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVgyfAQDHADDFADDMS 400
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-LLDGKDL---ASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 lfdWMAQWTQ--GGEQLvrgtlgrmlfsndeIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD-------MES 471
Cdd:cd03214 77 ---YVPQALEllGLAHL--------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqielLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489202159 472 IEALNlalDNYPGTLIFVSHDREFVSSLATRIIELGENGVT 512
Cdd:cd03214 140 LRRLA---RERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-504 |
4.76e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.47 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF--GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLEPSAGQVmlepnvrLGKLRqdqfayed 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRI-------SGEVL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 fsvidtvIMGHEELWAVKAERDRIYSL----PeMSEADGMAVAElEVQFA----EFDGYTAESRAGELLLGLGIPLEQHF 150
Cdd:COG1123 68 -------LDGRDLLELSEALRGRRIGMvfqdP-MTQLNPVTVGD-QIAEAlenlGLSRAEARARVLELLEAVGLERRLDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 151 GPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLD 226
Cdd:COG1123 139 YP-HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 227 YGELRlfpgnydEYMTAAEqarerLLSDNAKKKAqiaelqsfVSRFSANASKAKQATSRARQIdkIQLEEVKpssrvspf 306
Cdd:COG1123 218 DGRIV-------EDGPPEE-----ILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL--LEVRNLS-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 307 IRFEQYKKLHRQAVtveniskgydgkplfKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KW 378
Cdd:COG1123 268 KRYPVRGKGGVRAV---------------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltKL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 379 TDSA------DVGYFAQDHADDFADDMSLFDWMAQWtqggeQLVRGTLGRmlfsnDEIKKSVKVI--------------- 437
Cdd:COG1123 333 SRRSlrelrrRVQMVFQDPYSSLNPRMTVGDIIAEP-----LRLHGLLSR-----AERRERVAELlervglppdladryp 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 438 ---SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEA--LNLALD---NYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1123 403 helSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqiLNLLRDlqrELGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-508 |
5.69e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.03 E-value: 5.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAdvgyfaqdhaddfaddms 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 lfdwmaqWTQGGEQLVRGTLGrMLFSndeikksvkvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL----- 475
Cdd:cd00267 63 -------IAKLPLEELRRRIG-YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlellr 124
|
170 180 190
....*....|....*....|....*....|...
gi 489202159 476 NLALDNYpgTLIFVSHDREFVSSLATRIIELGE 508
Cdd:cd00267 125 ELAEEGR--TVIIVTHDPELAELAADRVIVLKD 155
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
3.33e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 115.53 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLR---------- 70
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-GRDLASLSrrelarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 --QDQFAYEDFSVIDTVIMG---HEELWAVKAERDRiyslpEMSEAdgmAVAELEVqfAEFdgytAESRAGELllglgip 145
Cdd:COG1120 80 vpQEPPAPFGLTVRELVALGrypHLGLFGRPSAEDR-----EAVEE---ALERTGL--EHL----ADRPVDEL------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 146 leqhfgpmSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDI-NTIRWLEGV--LTA-RNSTMIIISHDrhfLN---SV 218
Cdd:COG1120 139 --------SG---GERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLELLrrLAReRGRTVVMVLHD---LNlaaRY 204
|
250
....*....|..
gi 489202159 219 CTHMADLDYGEL 230
Cdd:COG1120 205 ADRLVLLKDGRI 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
321-520 |
6.80e-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: 114.57 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDSA--DVGYF--- 387
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREArrQIGVLpde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 --------AQDHADDFADDMSLFDwmAQWTQGGEQLVRgtlgRMLFSNDeIKKSVKVISGGEQGRMLFGRLILKRPNVLV 459
Cdd:COG4555 83 rglydrltVRENIRYFAELYGLFD--EELKKRIEELIE----LLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 460 MDEPTNHLDMESIEALN---LALDNYPGTLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDD 520
Cdd:COG4555 156 LDEPTNGLDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALCDRVVIL-HKGKVVAQGSLDE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-231 |
2.43e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 113.03 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdqfAYEDFS 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI----------------LIDGED 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIdtvimgHEELWAvkaeRDRIYSLPEMSEA-DGMAVAELEVQFAEF---DGYTAESRAGELL--LGLGIPLEQHFGPMS 154
Cdd:COG4555 65 VR------KEPREA----RRQIGVLPDERGLyDRLTVRENIRYFAELyglFDEELKKRIEELIelLGLEEFLDRRVGELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 155 AvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA---RNSTMIIISHDRHFLNSVCTHMADLDYGELR 231
Cdd:COG4555 135 T---GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlkkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-504 |
3.25e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 111.84 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV-----KWTDSA----DVGYFAQD 390
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrDVTGVPperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HAddfaddmsLFDWMAQWtqggEQLVRGtLGRMLFSNDEIKKSVKVI-----------------SGGEQGRMLFGRLILK 453
Cdd:cd03259 81 YA--------LFPHLTVA----ENIAFG-LKLRGVPKAEIRARVRELlelvglegllnryphelSGGQQQRVALARALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 454 RPNVLVMDEPTNHLDMESIEALNLALDNYPG----TLIFVSHDREFVSSLATRII 504
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-526 |
9.37e-28 |
|
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: 117.17 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD-----------SADVG 385
Cdd:COG4987 333 SLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDH-------------ADDFADDM---------SLFDWMAQWTQGGEQLVrGTLGRMLfsndeikksvkviSGGEQG 443
Cdd:COG4987 413 VVPQRPhlfdttlrenlrlARPDATDEelwaalervGLGDWLAALPDGLDTWL-GEGGRRL-------------SGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 444 RMLFGRLILKRPNVLVMDEPTNHLDMESIEA-LNLALDNYPG-TLIFVSHDREFVsSLATRIIELgENGVTDFSGSYDDY 521
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGrTVLLITHRLAGL-ERMDRILVL-EDGRIVEQGTHEEL 556
|
....*
gi 489202159 522 LRSQG 526
Cdd:COG4987 557 LAQNG 561
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-256 |
1.72e-27 |
|
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: 116.19 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYEDF-S 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNkT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHEELWAVKAE-RDRIYslpemseadgmavaeleVQFAEFDGYTAESRAGELllglgipleqhfgpmsavAPG 159
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKREiPSRAY-----------------VGRFNFKGSDQQKKVGQL------------------SGG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMadLDY---GELRLFPGN 236
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFegdSHVEWFEGN 525
|
250 260
....*....|....*....|
gi 489202159 237 YDEYmtaaEQARERLLSDNA 256
Cdd:TIGR03719 526 FSEY----EEDKKRRLGEDA 541
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-510 |
2.40e-27 |
|
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: 107.85 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVgyfaqdhaddfaD 397
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDL------------R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMSLFDWMAQ--WTQGGEQLVRGTLgrmlFSNdeikksvkVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL 475
Cdd:cd03228 68 DLDLESLRKNiaYVPQDPFLFSGTI----REN--------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 489202159 476 NLALDNYPG--TLIFVSHDREFVsSLATRIIELgENG 510
Cdd:cd03228 136 LEALRALAKgkTVIVIAHRLSTI-RDADRIIVL-DDG 170
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
2.52e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.77 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML----------EPNVRLGKLRQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 DQFAYEDFSVIDTVimgheELWAvkaerdRIYSLPemseadgmavaelevqfaefdGYTAESRAGELL--LGLGIPLEQH 149
Cdd:COG1131 81 EPALYPDLTVRENL-----RFFA------RLYGLP---------------------RKEARERIDELLelFGLTDAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 150 FGPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADLD 226
Cdd:COG1131 129 VGTLSG---GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELlreLAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
....
gi 489202159 227 YGEL 230
Cdd:COG1131 206 KGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-465 |
4.62e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 106.58 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 335 FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAD-----------VGYFAQDH--------ADDF 395
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkeIGYVFQDPqlfprltvRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 396 ADDMSLFDWMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTN 465
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-504 |
4.64e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.00 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK------WTDSAD----VGYFAQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddFADDMS---LFDWMAQWTQGGEQLVRGTLGRML--FS-NDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEP 463
Cdd:COG1131 81 EPA--LYPDLTvreNLRFFARLYGLPRKEARERIDELLelFGlTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489202159 464 TNHLDMESIEAL-----NLALDNypGTLIFVSHDREFVSSLATRII 504
Cdd:COG1131 159 TSGLDPEARRELwellrELAAEG--KTVLLSTHYLEEAERLCDRVA 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
322-511 |
6.67e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 106.92 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwTDSADVGYFAQDHADDF---- 395
Cdd:cd03246 3 VENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-LDGADISQWDPNELGDHvgyl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 396 ADDMSLFDwmaqwtqggeqlvrGTLgrmlfsNDEIkksvkvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL 475
Cdd:cd03246 82 PQDDELFS--------------GSI------AENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 489202159 476 NLALDNYP---GTLIFVSHDREFVSSlATRIIELgENGV 511
Cdd:cd03246 136 NQAIAALKaagATRIVIAHRPETLAS-ADRILVL-EDGR 172
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-504 |
1.10e-26 |
|
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: 106.50 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS-------------ADVGY 386
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHAddfaddmsLFDWMAqwtqggeqlVRGTLGRMLfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03229 81 VFQDFA--------LFPHLT---------VLENIALGL-------------SGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489202159 467 LDME---SIEALNLAL-DNYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03229 131 LDPItrrEVRALLKSLqAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
1.95e-26 |
|
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: 106.41 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML--EPNVRLGKLRQDQFAYed 78
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngEPIRDAREDYRRRLAY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 fsvidtviMGHeelwavkaeRDRIYslPEMSeadgmaVAELEVQFAEFDGY-TAESRAGELL--LGLGIPLEQHFGPMSA 155
Cdd:COG4133 80 --------LGH---------ADGLK--PELT------VRENLRFWAALYGLrADREAIDEALeaVGLAGLADLPVRQLSA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 156 vapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNS--TMIII-SHDRHFLNSV 218
Cdd:COG4133 135 ---GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArgGAVLLtTHQPLELAAA 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
269-527 |
2.25e-26 |
|
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: 113.39 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 269 VSRFSANASKAKQATSRARQIDKIQLEEVKPSSRVSPFIRFEQykklhRQAVTVENISKGY--DGKPLFKGLSLQVEAGE 346
Cdd:COG2274 428 VAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL-----KGDIELENVSFRYpgDSPPVLDNISLTIKPGE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 347 RVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAQDhaddfaddmSLFDWMAQWTQGGeQLVRGT------L 420
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGIDLRQIDPA---------SLRRQIGVVLQDV-FLFSGTirenitL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 421 GRMLFSNDEIKKSVKV------------------------ISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALN 476
Cdd:COG2274 572 GDPDATDEEIIEAARLaglhdfiealpmgydtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 477 LALDNYPG--TLIFVSHDREFVsSLATRIIELgENGVTDFSGSYDDYLRSQGV 527
Cdd:COG2274 652 ENLRRLLKgrTVIIIAHRLSTI-RLADRIIVL-DKGRIVEDGTHEELLARKGL 702
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
4.97e-26 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 101.50 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 223 ADLDYGELRLFPGNYDEYMTAAEQARERLLSDNAKKKAQIAELQSFVSRFSANASKAKQATSRARQIDKiqLEEVKPSSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEK--MERIEKPER 78
|
....*..
gi 489202159 303 VSPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
322-510 |
8.47e-26 |
|
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: 104.86 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD-----------SADVGYFA 388
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDhaddfADDmslfdwmaqwtqggeQLVRGT--------LGRMLFSNDEIKKSVKVI-----------------SGGEQG 443
Cdd:cd03225 82 QN-----PDD---------------QFFGPTveeevafgLENLGLPEEEIEERVEEAlelvgleglrdrspftlSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 444 RM-LFGRLILkRPNVLVMDEPTNHLDMESIEALN---LALDNYPGTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:cd03225 142 RVaIAGVLAM-DPDILLLDEPTAGLDPAGRRELLellKKLKAEGKTIIIVTHDLDLLLELADRVIVL-EDG 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
321-522 |
9.09e-26 |
|
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: 110.80 E-value: 9.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYD-GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGdlpVD---GGEVKWTDSADVGYFAQD------ 390
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkdfNGEARPQPGIKVGYLPQEpqldpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 ---------------------------HADDFADDMSLFDWMAQW-----TQGGEQLVRgtlgRMLFSNDEIK-----KS 433
Cdd:TIGR03719 83 ktvrenveegvaeikdaldrfneisakYAEPDADFDKLAAEQAELqeiidAADAWDLDS----QLEIAMDALRcppwdAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 434 VKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIEL--GEnGV 511
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELdrGR-GI 237
|
250
....*....|.
gi 489202159 512 TdFSGSYDDYL 522
Cdd:TIGR03719 238 P-WEGNYSSWL 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-510 |
2.08e-25 |
|
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: 104.34 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW----TDSAD-------VGYF 387
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNlrelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDhADDfaddmslfdwmaqwtqggeQLVRGT--------LGRMLFSNDEIKKSVKVI-----------------SGGEQ 442
Cdd:COG1122 81 FQN-PDD-------------------QLFAPTveedvafgPENLGLPREEIRERVEEAlelvglehladrpphelSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 443 GRM-LFGRLILkRPNVLVMDEPTNHLDMESIEALNLALDNYPG---TLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG1122 141 QRVaIAGVLAM-EPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL-DDG 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-494 |
2.53e-25 |
|
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: 104.78 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDL-PVDGGEVKW-------TDSADV----GY 386
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLfgerrggEDVWELrkriGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHADDFADDMSLFD------------WMaQWTQGGEQLVRGTLGRMLFSnDEIKKSVKVISGGEQGRMLFGRLILKR 454
Cdd:COG1119 83 VSPALQLRFPRDETVLDvvlsgffdsiglYR-EPTDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 455 PNVLVMDEPTNHLDMESIEALN-----LALDNYPgTLIFVSHDRE 494
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLalldkLAAEGAP-TLVLVTHHVE 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
2.74e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.40 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGnDLEPSAGQV-MLEPNVRLGKLRqdqFAY-- 76
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILG-LLPPTSGTVrLFGKPPRRARRR---IGYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 ------EDF--SVIDTVIMGheeLWAvkaerdRIYSLPEMSEADGMAVAE-LE-VQFAEFdgytAESRAGELllglgipl 146
Cdd:COG1121 82 qraevdWDFpiTVRDVVLMG---RYG------RRGLFRRPSRADREAVDEaLErVGLEDL----ADRPIGEL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 147 eqhfgpmSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT---ARNSTMIIISHDRHFLNSVCTHMA 223
Cdd:COG1121 141 -------SG---GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHDLGAVREYFDRVL 210
|
250 260
....*....|....*....|....*
gi 489202159 224 DLDYGelRLFPGNYDEYMTAAEQAR 248
Cdd:COG1121 211 LLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-526 |
3.17e-25 |
|
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: 109.46 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVgyfaqdhaddfaD 397
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-NGVDL------------S 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMSLFDWMAQ--WTQGGEQLVRGT------LGRMLFSNDEIKKSVK------VISG---------GEQGRMLFG------ 448
Cdd:COG4988 403 DLDPASWRRQiaWVPQNPYLFAGTirenlrLGRPDASDEELEAALEaagldeFVAAlpdgldtplGEGGRGLSGgqaqrl 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 449 ---RLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSHDREFVsSLATRIIELgENGVTDFSGSYDDYLR 523
Cdd:COG4988 483 alaRALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVL-DDGRIVEQGTHEELLA 560
|
...
gi 489202159 524 SQG 526
Cdd:COG4988 561 KNG 563
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-502 |
5.59e-25 |
|
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: 108.35 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILG--NDLEPSAGQVM-----------LEPNVRLG- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIyhvalcekcgyVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 68 ---------------------KLR-----------QDQFA-YEDFSVIDTVIMGHEELwAVKAErdriyslpemsEADGM 114
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdKLRrrirkriaimlQRTFAlYGDDTVLDNVLEALEEI-GYEGK-----------EAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 115 AVAELE-VQFAEFDGYTAESRAGelllglgipleqhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRW 193
Cdd:TIGR03269 149 AVDLIEmVQLSHRITHIARDLSG----------------------GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 194 ----LEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRlfpgnydeymtaaeqarerllsdnakkkaQIAELQSFV 269
Cdd:TIGR03269 207 vhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK-----------------------------EEGTPDEVV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 270 SRFSANASKAKQATSRARQIDKIQLEEVKpssrvspfirfEQYKKLHRQAVtvenisKGYDgkplfkGLSLQVEAGERVA 349
Cdd:TIGR03269 258 AVFMEGVSEVEKECEVEVGEPIIKVRNVS-----------KRYISVDRGVV------KAVD------NVSLEVKEGEIFG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 350 IIGPNGIGKTTLLRCLVGDLPVDGGEV------KWTDSADVGYFAQDHADDFA----DDMSLF---DWMAQWTQGGEQLV 416
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGPDGRGRAKRYIgilhQEYDLYphrTVLDNLTEAIGLEL 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 417 RGTLGRML---------FSNDEIK----KSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD-------MESIEALN 476
Cdd:TIGR03269 395 PDELARMKavitlkmvgFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAR 474
|
570 580
....*....|....*....|....*.
gi 489202159 477 LALDNypgTLIFVSHDREFVSSLATR 502
Cdd:TIGR03269 475 EEMEQ---TFIIVSHDMDFVLDVCDR 497
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-229 |
1.28e-24 |
|
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: 100.01 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdqfayedfsVIDTV 85
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------------LIDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGHEELWAVkaeRDRIYSLPEMSeadgmavaelevqfaefdgytaesragelllglgipleqhfgpmsavaPGWKLRVL 165
Cdd:cd00267 62 DIAKLPLEEL---RRRIGYVPQLS------------------------------------------------GGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA---RNSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELLRElaeEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-525 |
5.94e-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: 100.27 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADV--------------- 384
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-LIDGEDIsglseaelyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 385 GYFAQDHAddFADDMSLFD----WMAQWTQGGE----QLVRGTLGRMLFSNDEIKKSVKvISGGEQGRMLFGRLILKRPN 456
Cdd:cd03261 80 GMLFQSGA--LFDSLTVFEnvafPLREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 457 VLVMDEPTNHLD---MESIEALNLAL-DNYPGTLIFVSHDREFVSSLATRIIELGeNGVTDFSGSYDDYLRSQ 525
Cdd:cd03261 157 LLLYDEPTAGLDpiaSGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLY-DGKIVAEGTPEELRASD 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
1.16e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 328 GYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHADD------FADDMSl 401
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPdslpltVRDLVA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 402 fdwMAQWTQggeqlvRGTLGRmLFSNDEI---------------KKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:NF040873 80 ---MGRWAR------RGLWRR-LTRDDRAavddalervgladlaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489202159 467 LDMESIEALNLALDNYPG---TLIFVSHDREFVSSlATRIIEL 506
Cdd:NF040873 150 LDAESRERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
321-506 |
2.74e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 103.27 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDG-KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGdlpVD---GGEVKWTDSADVGYFAQD-HADD- 394
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDkefEGEARPAPGIKVGYLPQEpQLDPe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 ---------------------------FADDMSLFDWMAQwtqggEQlvrGTLGRMLFSND--------EI--------- 430
Cdd:PRK11819 85 ktvrenveegvaevkaaldrfneiyaaYAEPDADFDALAA-----EQ---GELQEIIDAADawdldsqlEIamdalrcpp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 431 -KKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK11819 157 wDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILEL 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-221 |
4.78e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.22 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGNdLEPSAGQVMLepnvrLGK---LRQDQFAY----E 77
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGL-LKPTSGSIRV-----FGKpleKERKRIGYvpqrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 DF------SVIDTVIMGheeLWAvkaerdRIYSLPEMSEADGMAVAE-LE-VQFAEFdgytAESRAGELllglgipleqh 149
Cdd:cd03235 78 SIdrdfpiSVRDVVLMG---LYG------HKGLFRRLSKADKAKVDEaLErVGLSEL----ADRQIGEL----------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 150 fgpmSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDrhfLNSVCTH 221
Cdd:cd03235 134 ----SG---GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELlreLRREGMTILVVTHD---LGLVLEY 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-503 |
5.19e-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: 96.94 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGYFAQDHAD------ 393
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPPKDRDiamvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFA--DDMSLFDWMAQwtqggeqlvrgTLGRMLFSNDEIKKSV-----------------KVISGGEQGRMLFGRLILKR 454
Cdd:cd03301 80 NYAlyPHMTVYDNIAF-----------GLKLRKVPKDEIDERVrevaellqiehlldrkpKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 455 PNVLVMDEPTNHLD------MES-IEALNLALDNypgTLIFVSHDREFVSSLATRI 503
Cdd:cd03301 149 PKVFLMDEPLSNLDaklrvqMRAeLKRLQQRLGT---TTIYVTHDQVEAMTMADRI 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-525 |
5.42e-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: 97.74 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAQDHADDFADD 398
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 399 MS-------LFDWMaqwtqggeqlvrgTLG-------RMLF--SNDEIKKSVKV-----------------ISGGEQGRM 445
Cdd:COG1127 84 IGmlfqggaLFDSL-------------TVFenvafplREHTdlSEAEIRELVLEklelvglpgaadkmpseLSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 446 LFGR-LILkRPNVLVMDEPTNHLD---MESIEALNLAL-DNYPGTLIFVSHDREFVSSLATRIIELGEnGVTDFSGSYDD 520
Cdd:COG1127 151 ALARaLAL-DPEILLYDEPTAGLDpitSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLAD-GKIIAEGTPEE 228
|
....*
gi 489202159 521 YLRSQ 525
Cdd:COG1127 229 LLASD 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-506 |
8.48e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.79 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDG----KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDSA----- 382
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 --DVGYFAQDHA--DDF-ADDMSLFDWMAQWTQGGEQLVRGT--LGRM-LfsNDEIKKSVKVISGGEQGRMLFGRLILKR 454
Cdd:cd03255 81 rrHIGFVFQSFNllPDLtALENVELPLLLAGVPKKERRERAEelLERVgL--GDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 455 PNVLVMDEPTNHLD-------MESIEALNlalDNYPGTLIFVSHDREFVsSLATRIIEL 506
Cdd:cd03255 159 PKIILADEPTGNLDsetgkevMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-510 |
8.99e-23 |
|
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: 97.18 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY----DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtdsadvgyfaqdhadd 394
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 faDDMSLFDWMAQWTQGGEQLV----------RGTLGRML------FSNDEIKKSVKVI------------------SGG 440
Cdd:COG1124 65 --DGRPVTRRRRKAFRRRVQMVfqdpyaslhpRHTVDRILaeplriHGLPDREERIAELleqvglppsfldryphqlSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEA--LNLALDN---YPGTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDV-SVQAeiLNLLKDLreeRGLTYLFVSHDLAVVAHLCDRVAVM-QNG 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-513 |
2.67e-22 |
|
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: 95.33 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEvkwTDSADVGYFAQDHADDFAD---- 397
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGA---PDEGEVLLDGKDIYDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 --------------DMSLFDWMA--------QWTQGGEQLVRGTLGRM-LFsnDEIKKSVKV--ISGGEQGRMLFGRLIL 452
Cdd:cd03260 80 rrrvgmvfqkpnpfPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAaLW--DEVKDRLHAlgLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 453 KRPNVLVMDEPTNHLDMES---IEALNLAL-DNYpgTLIFVSHDREFVSSLATRII-----ELGENGVTD 513
Cdd:cd03260 158 NEPEVLLLDEPTSALDPIStakIEELIAELkKEY--TIVIVTHNMQQAARVADRTAfllngRLVEFGPTE 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-510 |
2.91e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 294 LEEVKPSSRVSPFIRFEQYKKLHRQAVTVENiskgYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDG 373
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRT----PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 374 GEVKWTDSADVGYFAQ----------------DHADDFADDMslfdwMAQWtqggeqLVRGTLGRMLFSNDEIKKSVKVI 437
Cdd:COG4178 418 GRIARPAGARVLFLPQrpylplgtlreallypATAEAFSDAE-----LREA------LEAVGLGHLAERLDEEADWDQVL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 438 SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALnLAL--DNYPG-TLIFVSHdREFVSSLATRIIELGENG 510
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL-YQLlrEELPGtTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-511 |
2.92e-22 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.27 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 31 GLIGANGCGKSTFMKILgndlepsAGQvmLEPNvrLGKlrqdqfaYEDFSVIDTVImgheelwavkaerdRIYSLPEMSE 110
Cdd:PRK13409 103 GILGPNGIGKTTAVKIL-------SGE--LIPN--LGD-------YEEEPSWDEVL--------------KRFRGTELQN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 111 -----ADGMAVAELEVQFAE-----FDGytaesRAGELL---------------LGLGIPLEQHFGPMSavapGWKL-RV 164
Cdd:PRK13409 151 yfkklYNGEIKVVHKPQYVDlipkvFKG-----KVRELLkkvdergkldevverLGLENILDRDISELS----GGELqRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 165 LLAQALFSDPDVLLLDEPTNHLDI-------NTIRWLegvltARNSTMIIISHDrhflnsvcthMADLD---------YG 228
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHD----------LAVLDyladnvhiaYG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 229 ElrlfPGNYDeymtaaeqarerLLSDNAKKKAQIAE-LQSFVSrfSANAskakqatsRARQiDKIQLEEVKPSSRVSpfi 307
Cdd:PRK13409 287 E----PGAYG------------VVSKPKGVRVGINEyLKGYLP--EENM--------RIRP-EPIEFEERPPRDESE--- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 308 rfeqykklHRQAVTVENISKGYDGkplFkglSLQVEAG-----ERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTdsA 382
Cdd:PRK13409 337 --------RETLVEYPDLTKKLGD---F---SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--L 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 DVGYFAQDHADDFadDMSLFDWMAQ--------WTQggEQLVRG-TLGRMLfsndeiKKSVKVISGGEQGRMLFGRLILK 453
Cdd:PRK13409 401 KISYKPQYIKPDY--DGTVEDLLRSitddlgssYYK--SEIIKPlQLERLL------DKNVKDLSGGELQRVAIAACLSR 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 454 RPNVLVMDEPTNHLDMEsiEALNLA------LDNYPGTLIFVSHDREFVSSLATRIIEL-GENGV 511
Cdd:PRK13409 471 DADLYLLDEPSAHLDVE--QRLAVAkairriAEEREATALVVDHDIYMIDYISDRLMVFeGEPGK 533
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-508 |
7.33e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK-WTDSADVGYFAQDHADDFADD 398
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 399 MSLFDWMAqwtqGGEQLVRGTLGRMLFSN--DEI----------KKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03268 81 PGFYPNLT----ARENLRLLARLLGIRKKriDEVldvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 467 LDMESIEALN---LALDNYPGTLIFVSHDREFVSSLATRIIELGE 508
Cdd:cd03268 157 LDPDGIKELReliLSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
8.01e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 93.73 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVMLEpnvrlGKLRQDqfayedfs 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-ADLDpPTSGEIYLD-----GKPLSA-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimgheelWAVKAERDRIYSLPEMSEADGMAVAE-LEVQFAEFDGYTAESRAGELLLGLGIP---LEQHFGPMSAv 156
Cdd:COG4619 67 ------------MPPPEWRRQVAYVPQEPALWGGTVRDnLPFPFQLRERKFDRERALELLERLGLPpdiLDKPVERLSG- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 157 apGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:COG4619 134 --GERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-510 |
1.13e-21 |
|
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: 91.83 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 330 DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDhaddfaddmslfdwmaqwt 409
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 410 qggEQLVRGTLGRMLfsndeIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFV 489
Cdd:cd03223 73 ---PYLPLGTLREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
170 180
....*....|....*....|.
gi 489202159 490 SHdREFVSSLATRIIELGENG 510
Cdd:cd03223 145 GH-RPSLWKFHDRVLDLDGEG 164
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
342-526 |
1.32e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 98.70 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 342 VEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQ---------------------------DHADD 394
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdreyrqleaqlHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 FADDMSL------FDWMAQWT--QGGEQLVRGtLGrmlFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:PRK10636 104 RNDGHAIatihgkLDAIDAWTirSRAASLLHG-LG---FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 467 LDMESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYDDYLRSQG 526
Cdd:PRK10636 180 LDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-504 |
1.51e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.00 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY----DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD------SADVGYFA 388
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHAddfaddmsLFDWMaqwTqggeqlVRG--TLGRML--FSNDEIKKSV-----------------KVISGGEQGRMLF 447
Cdd:COG1116 87 QEPA--------LLPWL---T------VLDnvALGLELrgVPKAERRERArellelvglagfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 448 GRLILKRPNVLVMDEPTNHLDMESIEALN-LALD---NYPGTLIFVSHD-REFVsSLATRII 504
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQdELLRlwqETGKTVLFVTHDvDEAV-FLADRVV 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-504 |
3.86e-21 |
|
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: 91.88 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSAD----VG 385
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAglykptsGSVLLDGTDIRQLDPADlrrnIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQD-------------HADDFADDMSLFDwmAQWTQGGEQLVRGT---LGRMLfsndeikksvkvisgGEQGRMLFG- 448
Cdd:cd03245 82 YVPQDvtlfygtlrdnitLGAPLADDERILR--AAELAGVTDFVNKHpngLDLQI---------------GERGRGLSGg 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 449 --------RLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSHdREFVSSLATRII 504
Cdd:cd03245 145 qrqavalaRALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRII 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-507 |
4.80e-21 |
|
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: 91.76 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGK----PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD------SADVGYFAQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddfaddmsLFDWM-----------AQWTQGGEQLVRGTlgRML-------FSNdeikKSVKVISGGEQGRMLFGRLI 451
Cdd:cd03293 81 QDA--------LLPWLtvldnvalgleLQGVPKAEARERAE--ELLelvglsgFEN----AYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 452 LKRPNVLVMDEPTNHLDM---ESIEALNLALDNYPG-TLIFVSHDREFVSSLATRIIELG 507
Cdd:cd03293 147 AVDPDVLLLDEPFSALDAltrEQLQEELLDIWRETGkTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-512 |
4.80e-21 |
|
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: 91.16 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV----KWTDSAD----VGYFAQDH 391
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngKPIKAKErrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 ADDFADDmSLFDWM---AQWTQGGEQLVRGTLGRM-LFSNDEikKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHL 467
Cdd:cd03226 81 DYQLFTD-SVREELllgLKELDAGNEQAETVLKDLdLYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 468 D---MESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGVT 512
Cdd:cd03226 158 DyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-259 |
5.06e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 96.34 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLgklrqdqfAYEDFS--VID 83
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKL--------AYVDQSrdALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 ---TVimgheelWAvkaerdriyslpEMSE-ADGMAVAELEV-------QFAeFDGYTAESRAGELllglgipleqhfgp 152
Cdd:PRK11819 401 pnkTV-------WE------------EISGgLDIIKVGNREIpsrayvgRFN-FKGGDQQKKVGVL-------------- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 153 msavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMadLDY---GE 229
Cdd:PRK11819 447 ----SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFegdSQ 520
|
250 260 270
....*....|....*....|....*....|
gi 489202159 230 LRLFPGNYDEYmtaAEQARERLLSDNAKKK 259
Cdd:PRK11819 521 VEWFEGNFQEY---EEDKKRRLGADAARPH 547
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
282-492 |
1.01e-20 |
|
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: 95.51 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 282 ATSRARqidkiqLEEVKPSSRVSPFIRFEQYKKLHRQAVT--VENISKGYDG-KPLFKGLSLQVEAGERVAIIGPNGIGK 358
Cdd:TIGR02868 301 RAAAER------IVEVLDAAGPVAEGSAPAAGAVGLGKPTleLRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 359 TTLLRCLVGDLPVDGGEVKWTD-----------SADVGYFAQD-H----------------ADDfaDDMS-------LFD 403
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVCAQDaHlfdttvrenlrlarpdATD--EELWaalervgLAD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 404 WMAQwTQGGEQLVRGTLGRMLfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMES----IEALNLAL 479
Cdd:TIGR02868 453 WLRA-LPDGLDTVLGEGGARL-------------SGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAAL 518
|
250
....*....|...
gi 489202159 480 DNYpgTLIFVSHD 492
Cdd:TIGR02868 519 SGR--TVVLITHH 529
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-503 |
1.05e-20 |
|
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: 91.14 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA---------DVGYFAQD 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HAddfaddmsLFDWMAQWtqggEQLVRG-TLGRMlfSNDEIKKSVK-----------------VISGGEQGRMLFGRLIL 452
Cdd:cd03300 81 YA--------LFPHLTVF----ENIAFGlRLKKL--PKAEIKERVAealdlvqlegyanrkpsQLSGGQQQRVAIARALV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 453 KRPNVLVMDEPTNHLDMESIEALNLALDNYPG----TLIFVSHDREFVSSLATRI 503
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-503 |
1.29e-20 |
|
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: 90.51 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGE--------VKwtDSADV----GYF 387
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVR--EPREVrrriGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHADDfaDDMSLFD---WMA--------QWTQGGEQLVRGtLGRMLFSNdeikKSVKVISGGEQGRMLFGRLILKRPN 456
Cdd:cd03265 79 FQDLSVD--DELTGWEnlyIHArlygvpgaERRERIDELLDF-VGLLEAAD----RLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489202159 457 VLVMDEPTNHLDMES-------IEALNLALDNypgTLIFVSHDREFVSSLATRI 503
Cdd:cd03265 152 VLFLDEPTIGLDPQTrahvweyIEKLKEEFGM---TILLTTHYMEEAEQLCDRV 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
320-510 |
1.42e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW--TDSAD------------V 384
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngQDLSRlkrreipylrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 385 GYFAQDHAddFADDMSLFDWMAqwtqggeqL---VRGTlgrmlfSNDEIKKSV-----KV------------ISGGEQGR 444
Cdd:COG2884 82 GVVFQDFR--LLPDRTVYENVA--------LplrVTGK------SRKEIRRRVrevldLVglsdkakalpheLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLDME-SIEALNLALD-NYPG-TLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIMELLEEiNRRGtTVLIATHDLELVDRMPKRVLEL-EDG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
319-504 |
1.69e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.85 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW-----TDSA----DVGYFAQ 389
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvTGLPpekrNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddfaddmsLFDWMaqwTqggeqlVRGTLG---RML-FSNDEIKKSVK-----V------------ISGGEQGRMLFG 448
Cdd:COG3842 85 DYA--------LFPHL---T------VAENVAfglRMRgVPKAEIRARVAellelVglegladryphqLSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 449 RLILKRPNVLVMDEPTNHLDMESIEALNLALDNY----PGTLIFVSHDREFVSSLATRII 504
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQEEALALADRIA 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
321-506 |
2.75e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 89.93 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS--------------ADVG 385
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDHAddFADDMS-----LFDWMAQWTqggeqLVRGTLGrmLFSNDEIKKS----------------VKVISGGEQGR 444
Cdd:cd03256 82 MIFQQFN--LIERLSvlenvLSGRLGRRS-----TWRSLFG--LFPKEEKQRAlaalervglldkayqrADQLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLD-------MESIEALNLALDNypgTLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGL 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-278 |
3.58e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 94.25 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGqvmlepNVRLG-KLrqdQFAYEDfsvidt 84
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG------RIHCGtKL---EVAYFD------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 85 vimgheelwAVKAERDriyslPEMSEADGMAVAELEVqfaefdgyTAESRAGELLLGLGIPLeqhFGPMSAVAP------ 158
Cdd:PRK11147 389 ---------QHRAELD-----PEKTVMDNLAEGKQEV--------MVNGRPRHVLGYLQDFL---FHPKRAMTPvkalsg 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHDRHFLNSVCThmadldygELRLFPGN-- 236
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVT--------ECWIFEGNgk 515
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489202159 237 YDEYMTA---AEQARERLLSDNAKKKAQIAELQSFVSRFSANASK 278
Cdd:PRK11147 516 IGRYVGGyhdARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSK 560
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
321-464 |
5.14e-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: 88.65 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADV-------------GYF 387
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDItglppheraragiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHaDDFAdDMSLFD--WMAQWTQGGEQlVRGTLGRM--LFSN-DEIKKS-VKVISGGEQgRML-FGRLILKRPNVLVM 460
Cdd:cd03224 81 PEGR-RIFP-ELTVEEnlLLGAYARRRAK-RKARLERVyeLFPRlKERRKQlAGTLSGGEQ-QMLaIARALMSRPKLLLL 156
|
....
gi 489202159 461 DEPT 464
Cdd:cd03224 157 DEPS 160
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-506 |
5.82e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY-DGK---PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDSA---- 382
Cdd:COG1136 4 LLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisSLSERElarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 ---DVGYFAQDHAddFADDMSLFD--WMAQWTQGG-----EQLVRGTLGRMLFSnDEIKKSVKVISGGEQGRMLFGRLIL 452
Cdd:COG1136 84 rrrHIGFVFQFFN--LLPELTALEnvALPLLLAGVsrkerRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 453 KRPNVLVMDEPTNHLD-------MESIEALNLALDNypgTLIFVSHDREfVSSLATRIIEL 506
Cdd:COG1136 161 NRPKLILADEPTGNLDsktgeevLELLRELNRELGT---TIVMVTHDPE-LAARADRVIRL 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
6.72e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.33 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGA-KPLfENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 ---------YEDFSVIDTVIMG---HEELWAVKAERDRIYSLPEMSEADGMAVAELEvqFAEFDGYtAESRAGELllglg 143
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAahaRLGRGLLAALLRLPRARREEREARERAEELLE--RVGLADR-ADEPAGNL----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 144 ipleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPT---NHLDIN-TIRWLEGVLTARNSTMIIISHDRHFLNSVC 219
Cdd:COG0411 154 -------------SYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEeLAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250
....*....|.
gi 489202159 220 THMADLDYGEL 230
Cdd:COG0411 221 DRIVVLDFGRV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-464 |
8.00e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKlrqdqfAYEDFSVIDT- 84
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GE------PVRFRSPRDAq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 85 ---VIMGHEELwavkaerdriySL-PEMSEADGMAVAELEVQFAEFDGYTAESRAGELL--LGLGIPLEQhfgPMSAVAP 158
Cdd:COG1129 78 aagIAIIHQEL-----------NLvPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLarLGLDIDPDT---PVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIIShdrHFLN----------------SVC 219
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIirrLKAQGVAIIYIS---HRLDevfeiadrvtvlrdgrLVG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 220 TH-MADLDYGEL-RLfpgnydeyMTaaeqARErlLSDNAKKkaqiaelqsfvsrfsanaskakqatsRARQIDKIQLEev 297
Cdd:COG1129 221 TGpVAELTEDELvRL--------MV----GRE--LEDLFPK--------------------------RAAAPGEVVLE-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 298 kpssrvspfirfeqykklhrqavtVENISkgydGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV- 376
Cdd:COG1129 259 ------------------------VEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIr 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 377 ------KWTDSAD-----VGYFAQD-HADDFADDMSLFD-----WMAQWTQGG-------EQLVRGTLGRMlfsndEIK- 431
Cdd:COG1129 311 ldgkpvRIRSPRDairagIAYVPEDrKGEGLVLDLSIREnitlaSLDRLSRGGlldrrreRALAEEYIKRL-----RIKt 385
|
490 500 510
....*....|....*....|....*....|....*..
gi 489202159 432 ----KSVKVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:COG1129 386 pspeQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
1.08e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 11 FGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQ-----DQFAyedFSVIDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLP---LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGheeLWAvkaerdRIYSLPEMSEADGMAVAE-LE-VQFAEFDGYtaesragelllglgipleqhfgPMSAVAPGWKLR 163
Cdd:NF040873 79 AMG---RWA------RRGLWRRLTRDDRAAVDDaLErVGLADLAGR----------------------QLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 164 VLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL---TARNSTMIIISHDRH 213
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLaeeHARGATVVVVTHDLE 180
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
321-480 |
1.25e-19 |
|
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: 87.03 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW--TDSADVGYFAQD------HA 392
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngTPLAEQRDEPHEnilylgHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 393 DDFADDMSL---FDWMAQWTQGGEQLVRGTLGRMLFSNDEiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM 469
Cdd:TIGR01189 82 PGLKPELSAlenLHFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170
....*....|.
gi 489202159 470 ESIEALNLALD 480
Cdd:TIGR01189 161 AGVALLAGLLR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
1.83e-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: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 -------YEDFSVIDTVIMGH-----EELWAVKAERdriyslpEMSEADGMAVAELEvqFAEFDGYtAESRAGELLLGLg 143
Cdd:cd03219 80 tfqiprlFPELTVLENVMVAAqartgSGLLLARARR-------EEREARERAEELLE--RVGLADL-ADRPAGELSYGQ- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 144 ipleqhfgpmsavapgwKLRVLLAQALFSDPDVLLLDEPT---NHLDIN-TIRWLEGvLTARNSTMIIISHDRHFLNSVC 219
Cdd:cd03219 149 -----------------QRRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLA 210
|
250
....*....|.
gi 489202159 220 THMADLDYGEL 230
Cdd:cd03219 211 DRVTVLDQGRV 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-506 |
2.48e-19 |
|
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: 91.19 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK-PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwtdsadVGYFAQDHADdfAD 397
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA------VNGVPLADAD--AD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 dmslfDWMAQ--WTQGGEQLVRGT------LGRMLFSNDEIKKSVKV------------------------ISGGEQGRM 445
Cdd:TIGR02857 393 -----SWRDQiaWVPQHPFLFAGTiaenirLARPDASDAEIREALERagldefvaalpqgldtpigeggagLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 446 LFGRLILKRPNVLVMDEPTNHLDMES----IEALNLALDNYpgTLIFVSHDREfVSSLATRIIEL 506
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETeaevLEALRALAQGR--TVLLVTHRLA-LAALADRIVVL 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-504 |
2.58e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL------------VGDLPVDGGEVKWTDSADVGY 386
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQdHADDFADDMSLF---DWMAQWTQG-----------GEQLVRGTLGRMLFSNDEiKKSVKVISGGEQGRMLFGRLIL 452
Cdd:PRK11264 83 LRQ-HVGFVFQNFNLFphrTVLENIIEGpvivkgepkeeATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 453 KRPNVLVMDEPTNHLDMESI-EALNL--ALDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-228 |
3.10e-19 |
|
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: 86.16 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKP-LFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQ-----------DQ 73
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRksigyvmqdvdYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 74 FayedFSviDTVimgHEELwavkaerdrIYSLPEMSEADGMAVAELEvqfaefdgytaesragelLLGLGIPLEQHfgPM 153
Cdd:cd03226 84 L----FT--DSV---REEL---------LLGLKELDAGNEQAETVLK------------------DLDLYALKERH--PL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 154 SaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCT---HMADLDY 227
Cdd:cd03226 126 S-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDrvlLLANGAI 204
|
.
gi 489202159 228 G 228
Cdd:cd03226 205 V 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-524 |
3.23e-19 |
|
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: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDG---GEVKWTDSADVGYFAQDHAD 393
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFAddMSLFDWMAQW--TQGGEQLVRGtLGRMLFSNDEIKKSVKVI-----------------SGGEQGRMLFGRLILKR 454
Cdd:COG1123 84 RIG--MVFQDPMTQLnpVTVGDQIAEA-LENLGLSRAEARARVLELleavglerrldryphqlSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 455 PNVLVMDEPTNHLDM----ESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDDYLRS 524
Cdd:COG1123 161 PDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM-DDGRIVEDGPPEEILAA 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
4.03e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.68 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnVRLGKLRqdqfayedfs 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFGERR---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimGHEELWAVKAerdRIyslpemseadGMAVAELEVQFAE------------------FDGYTAE--SRAGELLL 140
Cdd:COG1119 69 -------GGEDVWELRK---RI----------GLVSPALQLRFPRdetvldvvlsgffdsiglYREPTDEqrERARELLE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 141 GLGIP--LEQHFGPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISH 210
Cdd:COG1119 129 LLGLAhlADRPFGTLSQ---GEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
5.02e-19 |
|
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: 85.60 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQ----------DQFaye 77
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRkvglvfqnpdDQF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 dfsVIDTVimgHEELwavkaerdrIYSLpemsEADGMavaelevqfaefDGYTAESRAGELLLGLGI-PLEQHfgPMSAV 156
Cdd:cd03225 89 ---FGPTV---EEEV---------AFGL----ENLGL------------PEEEIEERVEEALELVGLeGLRDR--SPFTL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 157 APGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT---ARNSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03225 136 SGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKklkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
319-504 |
5.68e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW-----TDSA----DVGYFAQ 389
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvTDLPpkdrNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddfaddmsLFDWMaqwTqggeqlVRGTLG---RML-FSNDEIKKSVKVI-----------------SGGEQGRMLFG 448
Cdd:COG3839 83 SYA--------LYPHM---T------VYENIAfplKLRkVPKAEIDRRVREAaellgledlldrkpkqlSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 449 RLILKRPNVLVMDEPTNHLD------MES-IEALNLALDNypgTLIFVSHDREFVSSLATRII 504
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklrveMRAeIKRLHRRLGT---TTIYVTHDQVEAMTLADRIA 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-516 |
7.32e-19 |
|
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: 84.29 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkwtdsadvgYFAQDHADDFAD 397
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMS-----------LFDwmaqwtqggeQLVRGTLGRMLfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03247 72 ALSslisvlnqrpyLFD----------TTLRNNLGRRF-------------SGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 467 LDMES-IEALNLALDNYPG-TLIFVSHDREFVSSlATRIIELgENGVTDFSG 516
Cdd:cd03247 129 LDPITeRQLLSLIFEVLKDkTLIWITHHLTGIEH-MDKILFL-ENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-211 |
7.59e-19 |
|
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: 84.02 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFAyEDFSVIDTV 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA-RKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 ImgheELWAVKAERDRIYSlpEMSeadgmavaelevqfaefdgytaesrAGELllglgipleQhfgpmsavapgwklRVL 165
Cdd:cd03214 82 L----ELLGLAHLADRPFN--ELS-------------------------GGER---------Q--------------RVL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDI-NTIRWLEGV--LTA-RNSTMIIISHD 211
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIaHQIELLELLrrLAReRGKTVVMVLHD 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
317-527 |
8.96e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 317 RQAVTVENISKGYDG-KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVgyfaqdhaddf 395
Cdd:COG1132 337 RGEIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-DGVDI----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 396 aDDMSLFDWMAQW---TQGGeQLVRGT------LGRMLFSNDEIKKSVKV------------------------ISGGEQ 442
Cdd:COG1132 405 -RDLTLESLRRQIgvvPQDT-FLFSGTirenirYGRPDATDEEVEEAAKAaqahefiealpdgydtvvgergvnLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 443 GRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSHdRefVSSL--ATRIIELgENG-VTDfSGS 517
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH-R--LSTIrnADRILVL-DDGrIVE-QGT 557
|
250
....*....|
gi 489202159 518 YDDYLRSQGV 527
Cdd:COG1132 558 HEELLARGGL 567
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-504 |
9.60e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.51 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD-------SA---DVGYFAQ 389
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlPPrerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddfaddmsLFDWMaqwTqggeqlVRG----TLGRMLFSNDEIKKSVK-----V------------ISGGEQGRMLFG 448
Cdd:COG1118 83 HYA--------LFPHM---T------VAEniafGLRVRPPSKAEIRARVEellelVqlegladrypsqLSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 449 RLILKRPNVLVMDEPTNHLD------MESiealNLA--LDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDakvrkeLRR----WLRrlHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-504 |
1.08e-18 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 85.25 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLF----KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD--------------S 381
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 382 ADVGYFAQdhaddfaDDMSLFD-WMAQWTQGGE--QLVRGTLGRMLFSNDEIKKSVKV-------------ISGGEQGRM 445
Cdd:cd03257 82 KEIQMVFQ-------DPMSSLNpRMTIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglpeevlnrypheLSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 446 LFGRLILKRPNVLVMDEPTNHLDMeSIEALNLAL-----DNYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDV-SVQAQILDLlkklqEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-494 |
1.28e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 88.53 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 27 GNRYGLIGANGCGKSTFMKILGNDLEPSAGQvmlepnvrlgklRQDQF---AYEDFSVIDTVImghEELWavkaERDRIY 103
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGE------------RQSQFshiTRLSFEQLQKLV---SDEW----QRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 104 SLPEMSEADGMAVAELeVQfaefDGYTAESRAGELLLGLGIP--LEQHFGPMSAvapGWKLRVLLAQALFSDPDVLLLDE 181
Cdd:PRK10938 90 MLSPGEDDTGRTTAEI-IQ----DEVKDPARCEQLAQQFGITalLDRRFKYLST---GETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 182 PTNHLDINTIRWLEGVLTARNS---TMIIISHDRHFLNSVCTHMADLDYGELrlfpgnydeymtAAEQARERLLSDnakk 258
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTL------------AETGEREEILQQ---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 259 kAQIAELqsfvsrfsanaskakqatSRARQIDKIQLEEV-KPSSRVS-----PFIRFEQykklhrqaVTVEniskgYDGK 332
Cdd:PRK10938 226 -ALVAQL------------------AHSEQLEGVQLPEPdEPSARHAlpanePRIVLNN--------GVVS-----YNDR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 333 PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVD-------------GGEVKWTDSADVGYFA-QDHAD----- 393
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSGETIWDIKKHIGYVSsSLHLDyrvst 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 --------DFADDMSLFDWMAQWTQggeQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTN 465
Cdd:PRK10938 354 svrnvilsGFFDSIGIYQAVSDRQQ---KLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
490 500 510
....*....|....*....|....*....|....*...
gi 489202159 466 HLDmesieALNLAL---------DNYPGTLIFVSHDRE 494
Cdd:PRK10938 431 GLD-----PLNRQLvrrfvdvliSEGETQLLFVSHHAE 463
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-230 |
1.40e-18 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 85.64 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 5 ANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML-----------EPNVRLGKLRQDQ 73
Cdd:TIGR03873 5 SRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 74 FAYEDFSVIDTVIMG---HEELWAVKAERDriyslpemSEADGMAVAELEVQ-FAEFDgytaesragelllglgipleqh 149
Cdd:TIGR03873 85 DTAVPLTVRDVVALGripHRSLWAGDSPHD--------AAVVDRALARTELShLADRD---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 150 fgpMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN----TIRWLEgVLTARNSTMIIISHDRHFLNSVCTHMADL 225
Cdd:TIGR03873 135 ---MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRaqleTLALVR-ELAATGVTVVAALHDLNLAASYCDHVVVL 210
|
....*
gi 489202159 226 DYGEL 230
Cdd:TIGR03873 211 DGGRV 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-216 |
1.63e-18 |
|
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: 88.66 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFaYEDFSVI--------D 83
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPASW-RRQIAWVpqnpylfaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 TVimgheelwavkaeRD--RIYSlPEMSEADGMAVAELeVQFAEF-----DGYtaESRAGELLLGLgipleqhfgpmSav 156
Cdd:COG4988 426 TI-------------REnlRLGR-PDASDEELEAALEA-AGLDEFvaalpDGL--DTPLGEGGRGL-----------S-- 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 157 aPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT--ARNSTMIIISHDRHFLN 216
Cdd:COG4988 476 -GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRrlAKGRTVILITHRLALLA 536
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-249 |
1.67e-18 |
|
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: 84.69 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQ----------DQFAYE 77
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglvfqnpdDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 dfSVIDTVIMGHEELwavkaerdriyslpemseadGMAVAElevqfaefdgytAESRAGELLLGLGI-PLEQHfgpmsav 156
Cdd:COG1122 92 --TVEEDVAFGPENL--------------------GLPREE------------IRERVEEALELVGLeHLADR------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 157 AP-----GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:COG1122 131 PPhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250 260
....*....|....*....|.
gi 489202159 229 ELrLFPGNYDEYMTAAEQARE 249
Cdd:COG1122 211 RI-VADGTPREVFSDYELLEE 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-241 |
2.19e-18 |
|
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: 88.74 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVM--------LEPNV---RLGKLRQDQFAYEDfS 80
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqIDPASlrrQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHeelwavkaerdriyslPEMSEADGMAVAELeVQFAEF-----DGYtaESRAGELllGLGIPLEQhfgpmsa 155
Cdd:COG2274 565 IRENITLGD----------------PDATDEEIIEAARL-AGLHDFiealpMGY--DTVVGEG--GSNLSGGQ------- 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 156 vapgwKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLtaRNSTMIIISHDRHFLNsvcthMAD----LDY 227
Cdd:COG2274 617 -----RQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLL--KGRTVIIIAHRLSTIR-----LADriivLDK 684
|
250
....*....|....
gi 489202159 228 GELRLFpGNYDEYM 241
Cdd:COG2274 685 GRIVED-GTHEELL 697
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-504 |
2.45e-18 |
|
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: 83.73 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDS------ADVGY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTIIIDGLKLTDDKKninelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQdHADDFAdDMSLFD--WMAQ-WTQG-----GEQLVRGTLGRMLFSnDEIKKSVKVISGGEQGRMLFGRLILKRPNVL 458
Cdd:cd03262 81 VFQ-QFNLFP-HLTVLEniTLAPiKVKGmskaeAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 459 VMDEPTNHLDMESI-EAL----NLALDNYpgTLIFVSHDREFVSSLATRII 504
Cdd:cd03262 158 LFDEPTSALDPELVgEVLdvmkDLAEEGM--TMVVVTHEMGFAREVADRVI 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
2.62e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNV-----------RLGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQFAYEDFSVIDTVIMG---HEELWAvkaerdriyslpEMSEADGMAV--AELEVQFAEFdgytAESRAGELllglgi 144
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWG------------RLSAEDNARVnqAMEQTRINHL----ADRRLTDL------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 145 pleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN---TIRWLEGVLTARNSTMIIISHDrhfLNSV--- 218
Cdd:PRK11231 140 ------------SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD---LNQAsry 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489202159 219 CTHMADLDYGELrLFPGNYDEYMTaaeqarERLLSDNAKKKAQI 262
Cdd:PRK11231 205 CDHLVVLANGHV-MAQGTPEEVMT------PGLLRTVFDVEAEI 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
322-503 |
2.62e-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: 84.31 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKgyDGKPLF-KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWT---------DSADVGYFAQDH 391
Cdd:cd03299 3 VENLSK--DWKEFKlKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 AddfaddmsLFDWMAQWtqggEQLVRGtLGRMLFSNDEIKKSVKVI-----------------SGGEQGRMLFGRLILKR 454
Cdd:cd03299 81 A--------LFPHMTVY----KNIAYG-LKKRKVDKKEIERKVLEIaemlgidhllnrkpetlSGGEQQRVAIARALVVN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 455 PNVLVMDEPTNHLDMES----IEALNLALDNYPGTLIFVSHDREFVSSLATRI 503
Cdd:cd03299 148 PKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
321-475 |
2.77e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA--DVGYFAQ----DHADD 394
Cdd:PRK13539 4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAEAchylGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 FADDMSLFDWMAQWtqggeqlvRGTLGRMLFSNDEIKKSV----------KVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:PRK13539 84 MKPALTVAENLEFW--------AAFLGGEELDIAAALEAVglaplahlpfGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170
....*....|.
gi 489202159 465 NHLDMESIEAL 475
Cdd:PRK13539 156 AALDAAAVALF 166
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-506 |
3.25e-18 |
|
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: 83.10 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAQDHADDFADDM 399
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 SLFDWMaqwtQGGEQLV-----RGT------------LGRMLFSNDEiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDE 462
Cdd:cd03269 80 GLYPKM----KVIDQLVylaqlKGLkkeearrridewLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489202159 463 PTNHLDMESIEALNLALDNYPG---TLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
322-504 |
3.58e-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: 83.64 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVgyfAQDHADDFA----- 396
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF-DGEDI---TGLPPHEIArlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ---------DDMSLFDWM---AQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVI-------------SGGEQGRMLFGRLI 451
Cdd:cd03219 79 rtfqiprlfPELTVLENVmvaAQARTGSGLLLARARREEREARERAEELLERVgladladrpagelSYGQQRRLEIARAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 452 LKRPNVLVMDEPTNHLDMESIEAL-----NLALDNYpgTLIFVSHDREFVSSLATRII 504
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELaelirELRERGI--TVLLVEHDMDVVMSLADRVT 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-527 |
4.86e-18 |
|
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: 83.43 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYD-GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTD----SADVGYF 387
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGSILIDGQDIREVTldslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDhaddfaddMSLFD-------WMAQWTQGGEQLVRGTLGRMLfsNDEIKK-----SVKV------ISGGEQGRMLFGR 449
Cdd:cd03253 81 PQD--------TVLFNdtigyniRYGRPDATDEEVIEAAKAAQI--HDKIMRfpdgyDTIVgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 450 LILKRPNVLVMDEPTNHLD----MESIEALNLALDNYpgTLIFVSHDREFVSSlATRIIELGENGVTDfSGSYDDYLRSQ 525
Cdd:cd03253 151 AILKNPPILLLDEATSALDthteREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAKG 226
|
..
gi 489202159 526 GV 527
Cdd:cd03253 227 GL 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-464 |
8.91e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 82.72 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSAD-------------VGYF 387
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-DGEDitglpphriarlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHaDDFAdDMSLFD--WMAQWTQGGEQLVRGTLGRM--LFSN-DEIKKSV-KVISGGEQgRML-FGRLILKRPNVLVM 460
Cdd:COG0410 84 PEGR-RIFP-SLTVEEnlLLGAYARRDRAEVRADLERVyeLFPRlKERRRQRaGTLSGGEQ-QMLaIGRALMSRPKLLLL 160
|
....
gi 489202159 461 DEPT 464
Cdd:COG0410 161 DEPS 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-232 |
9.08e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.88 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrLGKLRQDQfaYEDFSV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-----DGKSYQKN--IEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 IDTVImgheelwavkaERDRIYslPEMSEADGMAVAELEVQFAEfdgytaeSRAGELL--LGLGIPLEQHFGPMSAvapG 159
Cdd:cd03268 74 IGALI-----------EAPGFY--PNLTARENLRLLARLLGIRK-------KRIDEVLdvVGLKDSAKKKVKGFSL---G 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEG---VLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRL 232
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-504 |
9.24e-18 |
|
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: 86.38 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 31 GLIGANGCGKSTFMKILgndlepsAGQvmLEPNvrLGKlrqdqfaYEDFSVIDTVImgheelwavkaerdRIYSLPEMSE 110
Cdd:COG1245 103 GILGPNGIGKSTALKIL-------SGE--LKPN--LGD-------YDEEPSWDEVL--------------KRFRGTELQD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 111 -----ADGMAVAELEVQFAE-----FDGytaesRAGELL---------------LGLGIPLEQHFGPMSavapGWKL-RV 164
Cdd:COG1245 151 yfkklANGEIKVAHKPQYVDlipkvFKG-----TVRELLekvdergkldelaekLGLENILDRDISELS----GGELqRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 165 LLAQALFSDPDVLLLDEPTNHLDIN-------TIRwlegVLTARNSTMIIISHDrhflnsvcthMADLD---------YG 228
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDIYqrlnvarLIR----ELAEEGKYVLVVEHD----------LAILDyladyvhilYG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 229 ElrlfPGNY-------------DEYMT---AAEQARERllsdnakkKAQIaelqsfvsRFsanaskakqatsrarqidki 292
Cdd:COG1245 288 E----PGVYgvvskpksvrvgiNQYLDgylPEENVRIR--------DEPI--------EF-------------------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 293 qleEVKPSSRVSPFirfeqykklhRQAVTVENISKGYDGkplFkglSLQVEAG-----ERVAIIGPNGIGKTTLLRCLVG 367
Cdd:COG1245 328 ---EVHAPRREKEE----------ETLVEYPDLTKSYGG---F---SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 368 DLPVDGGEVKWTdsADVGYFAQDHADDFadDMSLfdwmaqwtqggEQLVRGTLGRMLFS---NDEI----------KKSV 434
Cdd:COG1245 389 VLKPDEGEVDED--LKISYKPQYISPDY--DGTV-----------EEFLRSANTDDFGSsyyKTEIikplglekllDKNV 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 435 KVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMEsiEALNLA------LDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1245 454 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
320-492 |
9.51e-18 |
|
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: 86.34 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwTDSAD------------VG 385
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-LDGADlsqwdreelgrhIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQdhaddfadDMSLFDwmaqwtqggeqlvrGTLG----RMLFSNDEikksvKVIS----------------G-----G 440
Cdd:COG4618 410 YLPQ--------DVELFD--------------GTIAeniaRFGDADPE-----KVVAaaklagvhemilrlpdGydtriG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 441 EQGRMLFG----RLILKR-----PNVLVMDEPTNHLDMESIEALNLALDNY---PGTLIFVSHD 492
Cdd:COG4618 463 EGGARLSGgqrqRIGLARalygdPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
322-528 |
1.12e-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: 82.78 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDG-KPLfKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAqdhADDFA---- 396
Cdd:COG0411 7 VRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DGRDITGLP---PHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ----------DDMSLFD--WMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKV-------------------ISGGEQGRM 445
Cdd:COG0411 82 artfqnprlfPELTVLEnvLVAAHARLGRGLLAALLRLPRARREEREARERAeellervgladradepagnLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 446 LFGRLILKRPNVLVMDEPT---NHLDMESIEALNLALDNYPG-TLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDDY 521
Cdd:COG0411 162 EIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVL-DFGRVIAEGTPAEV 240
|
....*..
gi 489202159 522 LRSQGVI 528
Cdd:COG0411 241 RADPRVI 247
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-504 |
1.18e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 84.61 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGYFAQDHAD------ 393
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGQDITHVPAENRHvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFA--DDMSLFDWMA-----QWTQGGE--QLVRGTLgRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:PRK09452 94 SYAlfPHMTVFENVAfglrmQKTPAAEitPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 465 NHLD------MES-IEALNLALdnypG-TLIFVSHDREFVSSLATRII 504
Cdd:PRK09452 173 SALDyklrkqMQNeLKALQRKL----GiTFVFVTHDQEEALTMSDRIV 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
1.38e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 81.78 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFG--AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML----------EPNVRLGKL 69
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdrkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQFAYEDFSVIDtvimgHEELWAvkaerdRIYSLPemsEADGMAVAELEVQFAEFDGYtAESRAGELllglgipleqh 149
Cdd:cd03263 81 PQFDALFDELTVRE-----HLRFYA------RLKGLP---KSEIKEEVELLLRVLGLTDK-ANKRARTL----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 150 fgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA--RNSTMIIISHDRHFLNSVCTHMADLDY 227
Cdd:cd03263 135 -------SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
....
gi 489202159 228 GELR 231
Cdd:cd03263 208 GKLR 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-516 |
2.04e-17 |
|
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: 81.26 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPL----FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGG--EVKWTDSADVGYFAQDHAD 393
Cdd:cd03266 2 ITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfaTVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFADDMSLFDWMAQWT-----------QGGEQLVR-GTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:cd03266 82 FVSDSTGLYDRLTAREnleyfaglyglKGDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 462 EPTNHLDMESIEALNLALDNYPG---TLIFVSHDREFVSSLATRIIELgENGVTDFSG 516
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVL-HRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
335-509 |
2.09e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 81.19 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 335 FKGLSLQVE---AGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK-----WTDSAD----------VGYFAQDHAddfa 396
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRKkinlppqqrkIGLVFQQYA---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ddmsLFDWM---------AQWTQGGEQLVRGTLGRMLFSNDEIKKS-VKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03297 86 ----LFPHLnvrenlafgLKRKRNREDRISVDELLDLLGLDHLLNRyPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489202159 467 LDMES----IEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGEN 509
Cdd:cd03297 162 LDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-504 |
3.22e-17 |
|
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: 80.31 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGeRVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAD----------VGYFAQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHadDFADDMSLF---DWMAqWTQG-----GEQLVRGTLGRmLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:cd03264 80 EF--GVYPNFTVReflDYIA-WLKGipskeVKARVDEVLEL-VNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 462 EPTNHLDMES-IEALNLALDNYPGTLIFVS-HDREFVSSLATRII 504
Cdd:cd03264 156 EPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVA 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
3.28e-17 |
|
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: 81.39 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAK----PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 -QFAYED--------FSVIDTVimgheelwavkAERDRIYSLPEMseadgmavaelevqfaefdgytaESRAGELLLGLG 143
Cdd:COG1124 81 vQMVFQDpyaslhprHTVDRIL-----------AEPLRIHGLPDR-----------------------EERIAELLEQVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 144 IPLEQHFGPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRhflnSVC 219
Cdd:COG1124 127 LPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDL----AVV 202
|
250
....*....|....*
gi 489202159 220 THMAD----LDYGEL 230
Cdd:COG1124 203 AHLCDrvavMQNGRI 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
3.44e-17 |
|
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: 80.70 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAK----PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVMLE-------PNVRLGK 68
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLErPTSGSVLVDgtdltllSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 69 LRQDqfayedfsvidtviMG----HEELWAVKAERDRIySLPemSEADGMAVAELEvqfaefdgytaeSRAGELLLGLGI 144
Cdd:cd03258 80 ARRR--------------IGmifqHFNLLSSRTVFENV-ALP--LEIAGVPKAEIE------------ERVLELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 145 PLEQHFGPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRHFLNSVCT 220
Cdd:cd03258 131 EDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICD 209
|
250
....*....|
gi 489202159 221 HMADLDYGEL 230
Cdd:cd03258 210 RVAVMEKGEV 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-233 |
3.86e-17 |
|
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: 80.31 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGnRYGLIGANGCGKSTFMKILGNDLEPSAGQVML----------EPNVRLGKLRQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpqKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 DQFAYEDFSVIDTVimgheelwavkaerDRIYSLPEMSEADgmavaelevqfaefdgytAESRAGELLLGLGipLEQHFG 151
Cdd:cd03264 80 EFGVYPNFTVREFL--------------DYIAWLKGIPSKE------------------VKARVDEVLELVN--LGDRAK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 152 -PMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDI-NTIRwLEGVLT--ARNSTMIIISHDRHFLNSVCTHMADLDY 227
Cdd:cd03264 126 kKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIR-FRNLLSelGEDRIVILSTHIVEDVESLCNQVAVLNK 204
|
....*.
gi 489202159 228 GELRLF 233
Cdd:cd03264 205 GKLVFE 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
323-507 |
3.91e-17 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 80.37 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGYDGKPL-FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW--TDSAD------------VGYF 387
Cdd:TIGR02673 5 HNVSKAYPGGVAaLHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIagEDVNRlrgrqlpllrrrIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHAddFADDMSLFDWMA-------QWTQGGEQLVRGTLgRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:TIGR02673 85 FQDFR--LLPDRTVYENVAlplevrgKKEREIQRRVGAAL-RQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489202159 461 DEPTNHLD---MESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELG 507
Cdd:TIGR02673 162 DEPTGNLDpdlSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
4.90e-17 |
|
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: 79.94 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLrqdqfayeDFSVIDTVImG--HEELWAV 95
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTDIRQL--------DPADLRRNI-GyvPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 96 KAE-RDRI-YSLPEMSEADGMAVAElevqFAEFDGYTAESRAG-ELLLGlgiplEQHFGpmsaVAPGWKLRVLLAQALFS 172
Cdd:cd03245 91 YGTlRDNItLGAPLADDERILRAAE----LAGVTDFVNKHPNGlDLQIG-----ERGRG----LSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 173 DPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISHDRHFLNSV 218
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLrqLLGDKTLIIITHRPSLLDLV 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-499 |
6.44e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 302 RVSPFIRFEQYKKLHRQAVTV--------ENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPv 371
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLDLservaivlEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 372 dGGEVKWTDSADVGYFAQDHA--DDFADDMSLFDWMAQWTQGGeqlvrgtlgrmLFSNDEIKKSVKVISGGEQGRMLFGR 449
Cdd:COG2401 82 -GTPVAGCVDVPDNQFGREASliDAIGRKGDFKDAVELLNAVG-----------LSDAVLWLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489202159 450 LILKRPNVLVMDEPTNHLD----MESIEALNLALDNYPGTLIFVSHDREFVSSL 499
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
322-507 |
6.70e-17 |
|
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: 79.07 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAD---VGYFAQD-----HAD 393
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARGllylgHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFADDMSLFDWMAQWTQ-GGEQLVRGTLGRMLFSNDEiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESI 472
Cdd:cd03231 83 GIKTTLSVLENLRFWHAdHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 489202159 473 EALNLALDNYP---GTLIFVSHDREFVSSLATRIIELG 507
Cdd:cd03231 162 ARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-504 |
1.32e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKwTDSADVGYFAQDHA 392
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-DPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 393 DDFaDDMSLFDWMA--QWTQGGEQLVRGTlgrmlfSNDEIKKSV-----KV------------ISGGEQGRMLFGRLILK 453
Cdd:PRK09493 81 MVF-QQFYLFPHLTalENVMFGPLRVRGA------SKEEAEKQArellaKVglaerahhypseLSGGQQQRVAIARALAV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489202159 454 RPNVLVMDEPTNHLDME-SIEALNL--ALDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK09493 154 KPKLMLFDEPTSALDPElRHEVLKVmqDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.59e-16 |
|
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: 76.53 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 17 FENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE-----------PNVRLGKLRQDQFAYEDFSVIDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGheelwavkaerdriyslpemseadgmavaeleVQFAEFDGYTAESRAGELLLGLGIP--LEQHFG-PMSAVAPGWKL 162
Cdd:pfam00005 81 RLG--------------------------------LLLKGLSKREKDARAEEALEKLGLGdlADRPVGeRPGTLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTN 184
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
1.92e-16 |
|
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: 78.30 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGA----KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE-------PNVRLGKLR 70
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 QDQFAY--------EDFSVIDTVIMGheelwavkaerdriyslpemseadgmavaeleVQFAEFDGYTAESRAGELLLGL 142
Cdd:cd03255 81 RRHIGFvfqsfnllPDLTALENVELP--------------------------------LLLAGVPKKERRERAEELLERV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 143 GIPLEQHFGP--MSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDR 212
Cdd:cd03255 129 GLGDRLNHYPseLSG---GQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
2.12e-16 |
|
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: 76.87 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFG--AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGNdLEPSAGQVMLEpNVRLGKLRQDQFayed 78
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGL-LRPTSGRVRLD-GADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 fsvidtvimgheelwavkaeRDRIYSLPEmseadgmavaelEVQFaeFDGYTAESrageLLLGlgipleqhfgpmsavap 158
Cdd:cd03246 75 --------------------GDHVGYLPQ------------DDEL--FSGSIAEN----ILSG----------------- 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSV 218
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLASA 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
2.22e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML-----------EPNVRLGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwspaELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQD---QFAyedFSVIDTVIMGHEELWAVKAERDRIYslpemseADGMAVAELEvQFAEFDgYTAESrAGElllglgipl 146
Cdd:PRK13548 82 PQHsslSFP---FTVEEVVAMGRAPHGLSRAEDDALV-------AAALAQVDLA-HLAGRD-YPQLS-GGE--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 147 eqhfgpmsavapgwKLRVLLAQAL------FSDPDVLLLDEPTNHLDI----NTIRWLEGVLTARNSTMIIISHDrhfLN 216
Cdd:PRK13548 140 --------------QQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LN 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
2.47e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.98 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF----GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML------EPNVRLGklr 70
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 qdqFAYEDF------SVIDTVIMGHEELWAVKAERDRIyslpemseadgmaVAEL--EVQFAEFdgytAESRAGELLLGl 142
Cdd:COG1116 84 ---VVFQEPallpwlTVLDNVALGLELRGVPKAERRER-------------ARELleLVGLAGF----EDAYPHQLSGG- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 143 gipleqhfgpMsavapgwKLRVLLAQALFSDPDVLLLDEPTNHLDINTIR----WLEGVLTARNSTMIIISHD 211
Cdd:COG1116 143 ----------M-------RQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-520 |
2.58e-16 |
|
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: 78.54 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSAD----------VGYFA 388
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDatdvpvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHAddFADDMSLFDWMAQWTQggeqlVRGTLGRMlfSNDEIKKSVKV-----------------ISGGEQGRMLFGRLI 451
Cdd:cd03296 81 QHYA--LFRHMTVFDNVAFGLR-----VKPRSERP--PEAEIRAKVHEllklvqldwladrypaqLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 452 LKRPNVLVMDEPTNHLDMESIEALNLAL----DNYPGTLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDD 520
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHDQEEALEVADRVVVM-NKGRIEQVGTPDE 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-249 |
2.85e-16 |
|
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: 81.74 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQ----FAY--EDFSVIDTV 85
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDlrrrIAVvpQRPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 ImgheelwavkaeRD--RIySLPEMSEADGMAVAELeVQFAEFdgytaesrAGELLLGLGIPLEQHFGPMSAvapGWKLR 163
Cdd:COG4987 425 L------------REnlRL-ARPDATDEELWAALER-VGLGDW--------LAALPDGLDTWLGEGGRRLSG---GERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 164 VLLAQALFSDPDVLLLDEPTNHLDINTIR-WLEGVLTA-RNSTMIIISHDRHFLNSVcTHMADLDYGELRLfPGNYDEYM 241
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEAlAGRTVLLITHRLAGLERM-DRILVLEDGRIVE-QGTHEELL 557
|
....*...
gi 489202159 242 TAAEQARE 249
Cdd:COG4987 558 AQNGRYRQ 565
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
329-508 |
3.76e-16 |
|
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: 77.76 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 329 YDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtdsadVGYFAQDHADDFADDMSLFdwMAQW 408
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-----AGLVPWKRRKKFLRRIGVV--FGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 409 TQ--------GGEQLVRGT--------------LGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03267 104 TQlwwdlpviDSFYLLAAIydlpparfkkrldeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489202159 467 LDMESIEALNLALDNY----PGTLIFVSHDREFVSSLATRIIELGE 508
Cdd:cd03267 184 LDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-507 |
3.80e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 330 DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD---SADVGYFAQD-----HADDFADDMSL 401
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHQDllylgHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 402 FD----WMAQWTQGGEQLVRGTLGRM-LFSNDEIkkSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALN 476
Cdd:PRK13538 92 LEnlrfYQRLHGPGDDEALWEALAQVgLAGFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170 180 190
....*....|....*....|....*....|....
gi 489202159 477 LALDNYP---GTLIFVSHDREFVSSLATRIIELG 507
Cdd:PRK13538 170 ALLAQHAeqgGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
322-506 |
4.23e-16 |
|
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: 77.47 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGY-----DGK--PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV------KWTDSAD----- 383
Cdd:COG4778 7 VENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdgGWVDLAQaspre 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 --------VGYFAQdhaddF--------ADD---MSLFDW-----MAQwTQGGEQLVRGTLGRMLFSNdeikkSVKVISG 439
Cdd:COG4778 87 ilalrrrtIGYVSQ-----FlrviprvsALDvvaEPLLERgvdreEAR-ARARELLARLNLPERLWDL-----PPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 440 GEQGRMLFGRLILKRPNVLVMDEPTNHLDMES----IEALNLALDNypGT-LIFVSHDREFVSSLATRIIEL 506
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTaIIGIFHDEEVREAVADRVVDV 225
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
420-525 |
4.70e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.44 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 420 LGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSHDREFVSSL 499
Cdd:PLN03073 328 LAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
90 100
....*....|....*....|....*.
gi 489202159 500 ATRIIELGENGVTDFSGSYDDYLRSQ 525
Cdd:PLN03073 408 VTDILHLHGQKLVTYKGDYDTFERTR 433
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-230 |
5.44e-16 |
|
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: 77.37 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQvmlepnVRLGKL----RQDQFAyedfSVIdTVIMGH 89
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE------VRVAGLvpwkRRKKFL----RRI-GVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 90 -EELWAVKAERD------RIYSLPemseadgmavaelEVQFAEfdgytaesRAGEL--LLGLGIPLEQhfgPMSAVAPGW 160
Cdd:cd03267 103 kTQLWWDLPVIDsfyllaAIYDLP-------------PARFKK--------RLDELseLLDLEELLDT---PVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 161 KLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA----RNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynreRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
5.80e-16 |
|
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: 80.62 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepNVRLGklrqdqfayEDFsvIDTVIMGHEElwavka 97
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV----NVRVG---------DEW--VDMTKPGPDG------ 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 98 erdriyslpemseaDGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAV--------------------- 156
Cdd:TIGR03269 360 --------------RGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVitlkmvgfdeekaeeildkyp 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 157 ---APGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRWLEGVLTAR---NSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:TIGR03269 426 delSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
.
gi 489202159 230 L 230
Cdd:TIGR03269 506 I 506
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-492 |
6.14e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.89 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwtdsadvgYFAQDHADDFADD 398
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRPLADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 399 MSL------------FDWMAqwtqggEQLVRgtLGRMLFSNDEIK-------------------KSVKVISGGEQGRMLF 447
Cdd:PRK13548 74 LARrravlpqhsslsFPFTV------EEVVA--MGRAPHGLSRAEddalvaaalaqvdlahlagRDYPQLSGGEQQRVQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 448 GRLIL------KRPNVLVMDEPTNHLD----MESIEAL-NLALDNyPGTLIFVSHD 492
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDlahqHHVLRLArQLAHER-GLAVIVVLHD 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
320-506 |
8.59e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSAD--VGYFAQD 390
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsGDLFIGEKRMNDVPPAErgVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HA----DDFADDMSLfdwmaqwtqgGEQLVRGtlgrmlfSNDEIKKSV-----------------KVISGGEQGRMLFGR 449
Cdd:PRK11000 84 YAlyphLSVAENMSF----------GLKLAGA-------KKEEINQRVnqvaevlqlahlldrkpKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 450 LILKRPNVLVMDEPTNHLD------MES-IEALNLALDNypgTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVL 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
9.24e-16 |
|
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: 75.30 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlgklrqdqfayedfsviDTV 85
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID---------------------GED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGHEELwaVKAERDRIyslpemseadGMAVAelevQFAEFDGYTAESRAGELLLGlgipleqhfgpmsavapGWKLRVL 165
Cdd:cd03229 64 LTDLEDE--LPPLRRRI----------GMVFQ----DFALFPHLTVLENIALGLSG-----------------GQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNS----TMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
1.02e-15 |
|
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: 76.02 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlgklrqdqfayedfsviDTV 85
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID---------------------GRD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGheelwaVKAERDRI------YSL-PEMSEADGMAVAeLEVQfaEFDGYTAESRAGELLLGLGIPLEQHFGPmSAVAP 158
Cdd:cd03259 64 VTG------VPPERRNIgmvfqdYALfPHLTVAENIAFG-LKLR--GVPKAEIRARVRELLELVGLEGLLNRYP-HELSG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINtIRW-----LEGVLTARNSTMIIISHDR 212
Cdd:cd03259 134 GQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-239 |
1.24e-15 |
|
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: 76.39 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQD--------- 72
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 ----QFA--YEDFSVIDTVimgheelwAVKAERDRIYSLPEMSE--ADGMAVAELEvqfAEFDGYTAEsragelLLGlgi 144
Cdd:cd03261 80 gmlfQSGalFDSLTVFENV--------AFPLREHTRLSEEEIREivLEKLEAVGLR---GAEDLYPAE------LSG--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 145 pleqhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INT------IRWLEGVLtarNSTMIIISHDRHFLNS 217
Cdd:cd03261 140 --------------GMKKRVALARALALDPELLLYDEPTAGLDpIASgviddlIRSLKKEL---GLTSIMVTHDLDTAFA 202
|
250 260
....*....|....*....|..
gi 489202159 218 VCTHMADLDYGELrLFPGNYDE 239
Cdd:cd03261 203 IADRIAVLYDGKI-VAEGTPEE 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
320-481 |
1.31e-15 |
|
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: 76.11 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYD-GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwTDSAD------------VGY 386
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL-IDGIDirdisrkslrsmIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQD---HADDFADDMSLFDWMAqwTQGGEQLVRGTLGrmlfSNDEIKKSVK-----------VISGGEQGRMLFGRLIL 452
Cdd:cd03254 82 VLQDtflFSGTIMENIRLGRPNA--TDEEVIEAAKEAG----AHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAML 155
|
170 180
....*....|....*....|....*....
gi 489202159 453 KRPNVLVMDEPTNHLDMESIEALNLALDN 481
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
2.61e-15 |
|
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: 75.29 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILG--NDL---EPSAGQVMLEP-NV----------- 64
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlNDLipgAPDEGEVLLDGkDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 65 -RLGKLRQDQFAYeDFSVIDTVIMG---HEELWavKAERDRIyslpemsEADGMAVAELevqFAEFDgytaeSRAGELLL 140
Cdd:cd03260 81 rRVGMVFQKPNPF-PGSIYDNVAYGlrlHGIKL--KEELDER-------VEEALRKAAL---WDEVK-----DRLHALGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 141 glgipleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT--ARNSTMIIISHD 211
Cdd:cd03260 143 ----------------SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-507 |
3.07e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 75.62 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYF-----------A 388
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDL-AGVDLHGLsrrararrvalV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHADDfADDMSLFDWMA--------QW---TQGGEQLVRGTLGRMLFSnDEIKKSVKVISGGEQGRMLFGRLILKRPNV 457
Cdd:TIGR03873 81 EQDSDT-AVPLTVRDVVAlgriphrsLWagdSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 458 LVMDEPTNHLDMES-IEALNLALD-NYPGTLIFVS-HDREFVSSLATRIIELG 507
Cdd:TIGR03873 159 LLLDEPTNHLDVRAqLETLALVRElAATGVTVVAAlHDLNLAASYCDHVVVLD 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-504 |
3.61e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE--------PNV--RLG--- 67
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaiALGigm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 68 -----KLrqdqfaYEDFSVIDTVIMGHEELWAVKAERDRiyslpemseadgmavaelevqfaefdgytAESRAGELL--L 140
Cdd:COG3845 85 vhqhfML------VPNLTVAENIVLGLEPTKGGRLDRKA-----------------------------ARARIRELSerY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 141 GLGIPLEQHFGPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRwlegVLTARNSTMIIISHdrh 213
Cdd:COG3845 130 GLDVDPDAKVEDLSV---GEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILR----RLAAEGKSIIFITH--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 214 flnsvcthmadldygelRLfpgnyDEYMTAAEQA----RERLLsdnakkkaqiaelqsfvsrfsanaskakqATSRARQI 289
Cdd:COG3845 200 -----------------KL-----REVMAIADRVtvlrRGKVV-----------------------------GTVDTAET 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 290 DKIQL------EEVKPSSRVSPfirfeqyKKLHRQAVTVENIS-KGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLL 362
Cdd:COG3845 229 SEEELaelmvgREVLLRVEKAP-------AEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELA 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 363 RCLVGDLPVDGGEVKWTD------------SADVGYFAQD-HADDFADDMSLFDWMAQWTQGGEQLVRGTL---GRML-F 425
Cdd:COG3845 302 EALAGLRPPASGSIRLDGeditglsprerrRLGVAYIPEDrLGRGLVPDMSVAENLILGRYRRPPFSRGGFldrKAIRaF 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 426 SNDEIKK----------SVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEA----LNLALDNypGT-LIFVS 490
Cdd:COG3845 382 AEELIEEfdvrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFihqrLLELRDA--GAaVLLIS 459
|
570
....*....|....
gi 489202159 491 HDREFVSSLATRII 504
Cdd:COG3845 460 EDLDEILALSDRIA 473
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-513 |
3.86e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP-------VDGGEVKWTDSADVGY----FA 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTptagtvlVAGDDVEALSARAASRrvasVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHADDFADDMSLFDWM---------AQWTQGGEQLVRGTLGRM---LFSNdeikKSVKVISGGEQGRMLFGRLILKRPN 456
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphrsrfDTWTETDRAAVERAMERTgvaQFAD----RPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 457 VLVMDEPTNHLDM-ESIEALNLA--LDNYPGTLIFVSHDREFVSSLATRIIELGENGVTD 513
Cdd:PRK09536 160 VLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-231 |
5.24e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML-----------EPNVRLGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQFAYEDFSVIDTVIMGHeelwavKAERDRiysLPEMSEADGMAVaELEVQFAEFDGYTAEsragelllglgipleqh 149
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGR------TPHRSR---FDTWTETDRAAV-ERAMERTGVAQFADR----------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 150 fgPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN-TIRWLEGV--LTARNSTMIIISHDRHFLNSVCTHMADLD 226
Cdd:PRK09536 136 --PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
....*
gi 489202159 227 YGELR 231
Cdd:PRK09536 214 DGRVR 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
5.87e-15 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 74.05 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFG----AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML------EPNVRLGKLRQ 71
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 DQFAYEDFSVIDTVIMGheelwavkaerdriyslpemSEADGMAVAElevqfaefdgytAESRAGELL--LGLGiPLEQH 149
Cdd:cd03293 81 QDALLPWLTVLDNVALG--------------------LELQGVPKAE------------ARERAEELLelVGLS-GFENA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 150 F-----GPMsavapgwKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHD 211
Cdd:cd03293 128 YphqlsGGM-------RQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-507 |
6.82e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 73.60 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLPVDGG-EVKWTDSAD-----VGYFAQDHADD 394
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTiRVNGQDVSDlrgraIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 FAD-----DMSLFDWMA---QWTQGGEQLVR---GTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEP 463
Cdd:cd03292 84 FQDfrllpDRNVYENVAfalEVTGVPPREIRkrvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489202159 464 TNHLDME-SIEALNLALD-NYPGTLIFVS-HDREFVSSLATRIIELG 507
Cdd:cd03292 164 TGNLDPDtTWEIMNLLKKiNKAGTTVVVAtHAKELVDTTRHRVIALE 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
320-376 |
9.65e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 9.65e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV 376
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI 58
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-469 |
9.95e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFA----- 75
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAqlgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 --YEDFSVIDTVIMgHEELWAVKAERDRIYSLPemseadgmavaelEVQFAEFdgytaESRAGELLL--GLGIPLEQHFG 151
Cdd:PRK09700 84 iiYQELSVIDELTV-LENLYIGRHLTKKVCGVN-------------IIDWREM-----RVRAAMMLLrvGLKVDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 152 PMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISH---------DRHFL---- 215
Cdd:PRK09700 145 NLSI---SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLImnqLRKEGTAIVYISHklaeirricDRYTVmkdg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 216 NSVCTHM-ADLDYGEL-RLFPGNydeymtaaeqarerllsdnakkkaqiaELQsfvSRFSANaskaKQATSRARQidkiq 293
Cdd:PRK09700 222 SSVCSGMvSDVSNDDIvRLMVGR---------------------------ELQ---NRFNAM----KENVSNLAH----- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 294 lEEVkpssrvspfirFEqykklhrqavtVENISkGYDGKPLfKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDG 373
Cdd:PRK09700 263 -ETV-----------FE-----------VRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 374 GEVkWTDSADV-------------GYFAQDHADD-FADDMSLFDWMAQWTQGGEQLVRGTLGrmLFSNDE---------- 429
Cdd:PRK09700 318 GEI-RLNGKDIsprspldavkkgmAYITESRRDNgFFPNFSIAQNMAISRSLKDGGYKGAMG--LFHEVDeqrtaenqre 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489202159 430 --------IKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM 469
Cdd:PRK09700 395 llalkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
325-511 |
1.14e-14 |
|
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: 73.60 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 325 ISKGYDGkplfkgLSLQVEAG-----ERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAQDHADDFadDM 399
Cdd:cd03237 6 MKKTLGE------FTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADY--EG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 SLFDWMAQWTQGgeqlvrgtLGRMLFSNDEIKKSVKV----------ISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM 469
Cdd:cd03237 77 TVRDLLSSITKD--------FYTHPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489202159 470 E----SIEALNLALDNYPGTLIFVSHDREFVSSLATRII----ELGENGV 511
Cdd:cd03237 149 EqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIvfegEPSVNGV 198
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
1.38e-14 |
|
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: 73.48 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQD-------- 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 -----QFA--YEDFSVIDTVIMGHEELWavkaerdriySLPEmSEADGMAVAELEvqfaefdgytaesragelLLGLGiP 145
Cdd:COG1127 84 igmlfQGGalFDSLTVFENVAFPLREHT----------DLSE-AEIRELVLEKLE------------------LVGLP-G 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 146 LEQHF-----GPMsavapgwKLRVLLAQALFSDPDVLLLDEPTNHLD----------INTIRwlegvlTARNSTMIIISH 210
Cdd:COG1127 134 AADKMpselsGGM-------RKRVALARALALDPEILLYDEPTAGLDpitsavidelIRELR------DELGLTSVVVTH 200
|
250 260
....*....|....*....|....*....
gi 489202159 211 DRHFLNSVCTHMADLDYGELrLFPGNYDE 239
Cdd:COG1127 201 DLDSAFAIADRVAVLADGKI-IAEGTPEE 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-523 |
1.40e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL--VGDLPvdgGEVKWtdSADVGYFAQD------ 390
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVRV--EGRVEFFNQNiyerrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 ------------HADDFADDMSLFDWMAQ------WTQGGE--QLVRGTLGRMLFSnDEIK----KSVKVISGGEQGRML 446
Cdd:PRK14258 82 nlnrlrrqvsmvHPKPNLFPMSVYDNVAYgvkivgWRPKLEidDIVESALKDADLW-DEIKhkihKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 447 FGRLILKRPNVLVMDEPTNHLDMES---IEAL--NLALDNyPGTLIFVSHDREFVSSLA----------TRIIELGENGV 511
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIAsmkVESLiqSLRLRS-ELTMVIVSHNLHQVSRLSdftaffkgneNRIGQLVEFGL 239
|
250
....*....|....
gi 489202159 512 TD--FSGSYDDYLR 523
Cdd:PRK14258 240 TKkiFNSPHDSRTR 253
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
1.41e-14 |
|
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: 76.17 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQF-GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrlgklrqdqfayedfs 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV-------------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimGHEELWAVKAE--RDRIYSLP------EMSEADGMAVAELEVQFAEFDGytAESRAG--ELLLGLGIPLEQHF 150
Cdd:TIGR02857 382 -------NGVPLADADADswRDQIAWVPqhpflfAGTIAENIRLARPDASDAEIRE--ALERAGldEFVAALPQGLDTPI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 151 GPMSA-VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT-IRWLEGVLT-ARNSTMIIISHDRHflnsvctHMADLDY 227
Cdd:TIGR02857 453 GEGGAgLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEVLEALRAlAQGRTVLLVTHRLA-------LAALADR 525
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
319-526 |
1.53e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK-PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDSA-------- 382
Cdd:PRK13657 334 AVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDIRTVTRAslrrniav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 ---DVGYFAQDHADDF------ADDMSLF---------DWMAQWTQGGEQLVrGTLGRMLfsndeikksvkviSGGEQGR 444
Cdd:PRK13657 414 vfqDAGLFNRSIEDNIrvgrpdATDEEMRaaaeraqahDFIERKPDGYDTVV-GERGRQL-------------SGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNypgtlifVSHDR-EFV-----SSL--ATRIIELgENGVTDFSG 516
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGRtTFIiahrlSTVrnADRILVF-DNGRVVESG 551
|
250
....*....|
gi 489202159 517 SYDDYLRSQG 526
Cdd:PRK13657 552 SFDELVARGG 561
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-232 |
1.69e-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: 72.31 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdQFAYEDFSV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV--------------LFDGKPLDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtvimgheelwavkAERDRIYSLPemsEADG----MAVAELEVQFAEFDGYT---AESRAGELLLGLGI------PLEQ 148
Cdd:cd03269 67 ---------------AARNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWLERLELseyankRVEE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 149 hfgpMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADL 225
Cdd:cd03269 129 ----LSK---GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLL 201
|
....*..
gi 489202159 226 DYGELRL 232
Cdd:cd03269 202 NKGRAVL 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
318-520 |
1.92e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 318 QAVTVENISK----------------------GYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGE 375
Cdd:COG1134 3 SMIEVENVSKsyrlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 376 VKWTdsadvGYFAqdhaddfaddmSLFDWMAqwtqG------GEQLVRgTLGRML-FSNDEIKK---------------- 432
Cdd:COG1134 83 VEVN-----GRVS-----------ALLELGA----GfhpeltGRENIY-LNGRLLgLSRKEIDEkfdeivefaelgdfid 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 433 -SVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDME----SIEALNlALDNYPGTLIFVSHDREFVSSLATRIIELg 507
Cdd:COG1134 142 qPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR-ELRESGRTVIFVSHSMGAVRRLCDRAIWL- 219
|
250
....*....|...
gi 489202159 508 ENGVTDFSGSYDD 520
Cdd:COG1134 220 EKGRLVMDGDPEE 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-504 |
2.69e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 70.54 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtdsadvgyfaqdhaddfaddm 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 slfdwmaqwtqGGEQLVRGTlgrmlfSNDEIKKSVKVI---SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL- 475
Cdd:cd03216 60 -----------DGKEVSFAS------PRDARRAGIAMVyqlSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLf 122
|
170 180 190
....*....|....*....|....*....|...
gi 489202159 476 ----NLALDNypGTLIFVSHDREFVSSLATRII 504
Cdd:cd03216 123 kvirRLRAQG--VAVIFISHRLDEVFEIADRVT 153
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-516 |
2.88e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.43 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYdGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPV--DGGEV--------KWTDSADVGYFAQ 389
Cdd:cd03213 11 VTVKSSPSKS-GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 dhaddfaDDMSLfdwmaqwtqgGEQLVRGTLgrmLFSndeikKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDm 469
Cdd:cd03213 90 -------DDILH----------PTLTVRETL---MFA-----AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 470 eSIEALN-------LALDNYpgTLIFVSHD-REFVSSLATRIIELgENGVTDFSG 516
Cdd:cd03213 144 -SSSALQvmsllrrLADTGR--TIICSIHQpSSEIFELFDKLLLL-SQGRVIYFG 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
3.40e-14 |
|
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: 71.77 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 17 FENVSVKFGNGNRY-----------------GLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDQFAYE-D 78
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 FSVIdtvimgheelwavkaERDRIYSL-PEMSEADgmAVAE-LEVQFAEFDGYTAESRAGELLLGLGIPlEQHFG--P-- 152
Cdd:cd03257 84 IQMV---------------FQDPMSSLnPRMTIGE--QIAEpLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNryPhe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 153 MSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRWLEgvlTARNSTMIIISHDRHFLNSVCTHMADL 225
Cdd:cd03257 146 LSG---GQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQ---EELGLTLLFITHDLGVVAKIADRVAVM 219
|
....*
gi 489202159 226 DYGEL 230
Cdd:cd03257 220 YAGKI 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-226 |
3.50e-14 |
|
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: 72.08 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 15 PLFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGNDLePSAGQVMLEpnvrlgklrqdqfayEDFSVIDTVIMGHEELW 93
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYL-PDSGSILVR---------------HDGGWVDLAQASPREIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 94 AVKaeRDRI-Y------SLPEMSEADgmAVAE--LEVQFAEfdgYTAESRAGELLLGLGIPLEQHfgpmsAVAP-----G 159
Cdd:COG4778 89 ALR--RRTIgYvsqflrVIPRVSALD--VVAEplLERGVDR---EEARARARELLARLNLPERLW-----DLPPatfsgG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRWLEGV--LTARNSTMIIISHDRHFLNSVCTHMADLD 226
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDaANRAVVVELIeeAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-512 |
3.94e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLP------VDGGEV-----KWTDSAdVG 385
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPqrgrvkVMGREVnaeneKWVRSK-VG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDhADDFADDMSLFDWMAQWTQGgeqlvrgtlgrMLFSNDEIKKSVKV-----------------ISGGEQGRMLFG 448
Cdd:PRK13647 83 LVFQD-PDDQVFSSTVWDDVAFGPVN-----------MGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 449 RLILKRPNVLVMDEPTNHLD---MESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELgENGVT 512
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVL-KEGRV 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-468 |
4.67e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS----------ADVGYFA 388
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 Q-DHAD-DFA--DDMSLFD-WMAQWTQGGEQLVRGTLGrmlFSNDEIKKSVKV--ISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:PRK13537 87 QfDNLDpDFTvrENLLVFGrYFGLSAAAARALVPPLLE---FAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLVLD 163
|
....*..
gi 489202159 462 EPTNHLD 468
Cdd:PRK13537 164 EPTTGLD 170
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-524 |
4.87e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.61 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 338 LSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK-----WTDSAD----------VGYFAQDhaddfaddMSLF 402
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRKgiflppekrrIGYVFQE--------ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 403 DWM--AQWTQGGEQLVRGTLGRMLFsnDEI----------KKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM- 469
Cdd:TIGR02142 88 PHLsvRGNLRYGMKRARPSERRISF--ERViellgighllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDp 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 470 ---ESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDDYLRS 524
Cdd:TIGR02142 166 rkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL-EDGRVAAAGPIAEVWAS 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
308-516 |
5.25e-14 |
|
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: 71.41 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 308 RFEQYKKLHRQAVTVENISK--GYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVG 385
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGRkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-TVRGRVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDHAddFADDMSlfdwmaqwtqgGEQLVRgTLGRML-FSNDEIKKS-----------------VKVISGGEQGRMLF 447
Cdd:cd03220 88 LLGLGGG--FNPELT-----------GRENIY-LNGRLLgLSRKEIDEKideiiefselgdfidlpVKTYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 448 GRLILKRPNVLVMDEPTNHLD---ME-SIEALNlALDNYPGTLIFVSHDREFVSSLATRIIELgENGVTDFSG 516
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDaafQEkCQRRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVL-EKGKIRFDG 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-230 |
6.84e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrlgklrqDQFAYEDfsvidtv 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILL-----------DAQPLES------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 imgheelWAVKAERDRIYSLP-EMSEADGMAVAELeVQFAEFDGYTAESRAGE----------LLLGLGiPLEQHFgpMS 154
Cdd:PRK10575 78 -------WSSKAFARKVAYLPqQLPAAEGMTVREL-VAIGRYPWHGALGRFGAadrekveeaiSLVGLK-PLAHRL--VD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 155 AVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDI----NTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
7.87e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFG----AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFAy 76
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERELA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 edfsvidtvimgheELWavkaeRDRI-------YSLPEMSeadgmaVAE---LEVQFAEFDGYTAESRAGELL--LGLGi 144
Cdd:COG1136 82 --------------RLR-----RRHIgfvfqffNLLPELT------ALEnvaLPLLLAGVSRKERRERARELLerVGLG- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 145 PLEQHFgP--MSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRH 213
Cdd:COG1136 136 DRLDHR-PsqLSG---GQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPE 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
8.65e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 70.25 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVMLE------PNVRLGKLRQD-- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEePDSGTIIIDglkltdDKKNINELRQKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 ----QFA-YEDFSVIDTVIMGHEELWavkaerdriyslpemseadGMAVAElevqfaefdgytAESRAGELLLGLGIPLE 147
Cdd:cd03262 80 mvfqQFNlFPHLTVLENITLAPIKVK-------------------GMSKAE------------AEERALELLEKVGLADK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 148 QHFGPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMAD 224
Cdd:cd03262 129 ADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGFAREVADRVIF 207
|
....*.
gi 489202159 225 LDYGEL 230
Cdd:cd03262 208 MDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
1.14e-13 |
|
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: 68.95 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQdQFAYED-----FSvi 82
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvdlRDLDLESLRK-NIAYVPqdpflFS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DTVimgheelwavkaeRDRIYSlpemseadgmavaelevqfaefdgytaesrAGElllglgipleqhfgpmsavapgwKL 162
Cdd:cd03228 90 GTI-------------RENILS------------------------------GGQ-----------------------RQ 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTNHLDINT-IRWLEGVLT-ARNSTMIIISHDRH 213
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETeALILEALRAlAKGKTVIVIAHRLS 156
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
322-503 |
1.18e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLPVDGGEVkwTDSADVGYFA--QDHADDFADD 398
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIM--LDGVDLSHVPpyQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 399 MSLFDWMAQwtqggEQLVRGTLGRMLFSNDEIKKSVK-----------------VISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:PRK11607 100 YALFPHMTV-----EQNIAFGLKQDKLPKAEIASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489202159 462 EPTNHLDMESIEALNLA----LDNYPGTLIFVSHDREFVSSLATRI 503
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
321-508 |
1.19e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVD---GGEVkWTDSAD----------VGYF 387
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV-LLNGRRltalpaeqrrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDhaddfaddMSLFDWMAQW---------TQGGEQ---LVRGTLGRM----LFSNDeikksVKVISGGEQGRMLFGRLI 451
Cdd:COG4136 82 FQD--------DLLFPHLSVGenlafalppTIGRAQrraRVEQALEEAglagFADRD-----PATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 452 LKRPNVLVMDEPTNHLDM-----------ESIEALNLAldnypgtLIFVSHDREFVSSlATRIIELGE 508
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAalraqfrefvfEQIRQRGIP-------ALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-504 |
1.34e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.29 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW-------TDSADVGYF---- 387
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYLpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 -------AQDHADDFAD--DMSLFD---WMAQWtqggeqLVRGTLGrmlfsnDEIKKSVKVISGGEQGRMLFGRLILKRP 455
Cdd:COG4152 81 glypkmkVGEQLVYLARlkGLSKAEakrRADEW------LERLGLG------DRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 456 NVLVMDEPTNHLD-------MESIEALNLAldnypG-TLIFVSHDREFVSSLATRII 504
Cdd:COG4152 149 ELLILDEPFSGLDpvnvellKDVIRELAAK-----GtTVIFSSHQMELVEELCDRIV 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-463 |
1.48e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.26 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADV-------------GY 386
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDItklpmhkrarlgiGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHaddfaddmSLFDWM-----------------AQWTQGGEQLVRgtlgrmLFSNDEIKKSVKV-ISGGEQGRMLFG 448
Cdd:cd03218 80 LPQEA--------SIFRKLtveenilavleirglskKEREEKLEELLE------EFHITHLRKSKASsLSGGERRRVEIA 145
|
170
....*....|....*
gi 489202159 449 RLILKRPNVLVMDEP 463
Cdd:cd03218 146 RALATNPKFLLLDEP 160
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-525 |
1.75e-13 |
|
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: 70.02 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDSAD----VGYF 387
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEIFIDGEDIREQDPVElrrkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQdhaddfadDMSLFDWMAQWTQGGeqLVRGTLGrmlFSNDEIKKSVK-------------------VISGGEQGRMLFG 448
Cdd:cd03295 81 IQ--------QIGLFPHMTVEENIA--LVPKLLK---WPKEKIRERADellalvgldpaefadryphELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 449 RLILKRPNVLVMDEPTNHLDMESIEALN---LALDNYPG-TLIFVSHDREFVSSLATRIIELGENGVTDFsGSYDDYLRS 524
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGkTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILRS 226
|
.
gi 489202159 525 Q 525
Cdd:cd03295 227 P 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.81e-13 |
|
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: 68.22 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKLRqdQFAyedfSV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEV--SFA----SP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 IDtvimgheelwavkAERDRIYSLPEMSeadgmaVAElevqfaefdgytaesragelllglgipleqhfgpmsavapgwK 161
Cdd:cd03216 70 RD-------------ARRAGIAMVYQLS------VGE------------------------------------------R 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-504 |
1.81e-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: 68.61 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISkgydGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV-------KWTDSAD-----VGY 386
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEItldgkpvTRRSPRDairagIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQD-HADDFADDMSLFDWMAqwtqggeqlvrgtLGRMLfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTN 465
Cdd:cd03215 80 VPEDrKREGLVLDLSVAENIA-------------LSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489202159 466 HLDMESIEA-----LNLALDNypGTLIFVSHDREFVSSLATRII 504
Cdd:cd03215 134 GVDVGAKAEiyrliRELADAG--KAVLLISSELDELLGLCDRIL 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
2.43e-13 |
|
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: 72.39 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFAY------EDFSVIDTV 85
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRRrvsvcaQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGHEELWAvkaerdriyslPEMSEADGMAVAElEVQFAEFdgytaesrAGELLLGLGIPLeqhfGPMSA-VAPGWKLRV 164
Cdd:TIGR02868 425 VRENLRLAR-----------PDATDEELWAALE-RVGLADW--------LRALPDGLDTVL----GEGGArLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 165 LLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARnsTMIIISHD 211
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR--TVVLITHH 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
339-510 |
2.51e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 71.29 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 339 SLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK-----WTDSAD----------VGYFAQDHaddfaddmSLFD 403
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARgiflpphrrrIGYVFQEA--------RLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 404 WMAqwtqggeqlVRGTL---------GRMLFSNDEI----------KKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:COG4148 91 HLS---------VRGNLlygrkraprAERRISFDEVvellgighllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 465 NHLDMES-------IEALNLALDnYPgtLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG4148 162 AALDLARkaeilpyLERLRDELD-IP--ILYVSHSLDEVARLADHVVLL-EQG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
2.57e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML--EP--------NVRLGKLRQ 71
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 DQFAYEDFSVIDTV-IMGHEELWAVKAERDRIYSLPEMseadgmavAELEVQfaefdgytAESRAGELllglgipleqhf 150
Cdd:PRK13537 88 FDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEF--------AKLENK--------ADAKVGEL------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 151 gpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT--IRW--LEGVLtARNSTMIIISHDRHFLNSVCTHMADLD 226
Cdd:PRK13537 140 ------SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIE 212
|
..
gi 489202159 227 YG 228
Cdd:PRK13537 213 EG 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
320-496 |
2.64e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQD-HAD-DFAD 397
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLDtTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMSLFDWMAQWTQGGE---QLVRGTLGRMLfsndeiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEA 474
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDilpALKRVQAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*.
gi 489202159 475 LNLALDNYPGTL----IFVSHDREFV 496
Cdd:PRK09544 159 LYDLIDQLRRELdcavLMVSHDLHLV 184
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-230 |
2.69e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVMLE-PNVRLGKLRQDQFAYEDF 79
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEkPSEGSIVVNgQTINLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 SVID------TVIMGHEELWAvkaerdriyslpEMSEADGmaVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPM 153
Cdd:PRK10619 85 NQLRllrtrlTMVFQHFNLWS------------HMTVLEN--VMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 154 SAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD---INTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-209 |
2.81e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEP-NVRLGKLRQdQFAYedf 79
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgDIDDPDVAE-ACHY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 svidtviMGHEElwAVKAErdriyslpemseadgMAVAElEVQF-AEFDGyTAESRAGELL--LGLGIPLEQHFGPMSAv 156
Cdd:PRK13539 78 -------LGHRN--AMKPA---------------LTVAE-NLEFwAAFLG-GEELDIAAALeaVGLAPLAHLPFGYLSA- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 157 apGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNST--MIIIS 209
Cdd:PRK13539 131 --GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQggIVIAA 183
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-500 |
3.05e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGYFAQDH-------- 391
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRlytvrkrm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 -----ADDFADDMSLFDWMA----QWTQGGEQLVRGTLgRMLFSNDEIKKSVKV----ISGGEQGRMLFGRLILKRPNVL 458
Cdd:PRK11831 87 smlfqSGALFTDMNVFDNVAyplrEHTQLPAPLLHSTV-MMKLEAVGLRGAAKLmpseLSGGMARRAALARAIALEPDLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489202159 459 VMDEP-------TNHLDMESIEALNLALDNypgTLIFVSHDREFVSSLA 500
Cdd:PRK11831 166 MFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIA 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-503 |
3.12e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGklrqdqfayedfs 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimgheeLWAVKAERDRIYSLPEmsEAdgMAVAELEVQ----FAEFDGYTAESRAGELLLGLGIPLEQHfgpMSA- 155
Cdd:PRK15439 78 -----------LTPAKAHQLGIYLVPQ--EP--LLFPNLSVKenilFGLPKRQASMQKMKQLLAALGCQLDLD---SSAg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 156 ---VAPGWKLRVLlaQALFSDPDVLLLDEPTNHLD-INTIRWLEGV--LTARNSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:PRK15439 140 sleVADRQIVEIL--RGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 230 LRLFpGNYDEYMTAaeqarerllsdnakkkaqiaELQSFVSRfsanASKAKQATsrarqiDKIQLEEVKPSSRvspfirf 309
Cdd:PRK15439 218 IALS-GKTADLSTD--------------------DIIQAITP----AAREKSLS------ASQKLWLELPGNR------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 310 eqykklHRQA-----VTVENIS-KGydgkplFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSAD 383
Cdd:PRK15439 260 ------RQQAagapvLTVEDLTgEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKE 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 VG-------------YFAQD-HADDFADDMSL--------FDWMAQWTQGGEQlvRGTLGR------MLFSNDEikKSVK 435
Cdd:PRK15439 327 INalstaqrlarglvYLPEDrQSSGLYLDAPLawnvcaltHNRRGFWIKPARE--NAVLERyrralnIKFNHAE--QAAR 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 436 VISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD----------MESIEALNLAldnypgtLIFVSHDREFVSSLATRI 503
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlIRSIAAQNVA-------VLFISSDLEEIEQMADRV 473
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-231 |
3.14e-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: 68.93 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPL----FENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPnvrlgklrqdqfay 76
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 edfsvIDTvimgHEELWAVKAerdRIYSLPE-MSEADGMAVAELEVQFAEFDGY---TAESRAGEL--LLGLGIPLEQHF 150
Cdd:cd03266 67 -----FDV----VKEPAEARR---RLGFVSDsTGLYDRLTARENLEYFAGLYGLkgdELTARLEELadRLGMEELLDRRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 151 GPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADLDY 227
Cdd:cd03266 135 GGFST---GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFirqLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
....
gi 489202159 228 GELR 231
Cdd:cd03266 212 GRVV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
321-523 |
3.14e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.01 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPL-FkglSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFA----------Q 389
Cdd:COG3840 3 RLDDLTYRYGDFPLrF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTALPpaerpvsmlfQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DH--------ADDFA----DDMSLFDwmAQWTQggeqlVRGTLGRMLFSNDEIKKSVKvISGGEQGRMLFGR-LILKRPn 456
Cdd:COG3840 79 ENnlfphltvAQNIGlglrPGLKLTA--EQRAQ-----VEQALERVGLAGLLDRLPGQ-LSGGQRQRVALARcLVRKRP- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 457 VLVMDEPTNHLD------MesiealnLAL-----DNYPGTLIFVSHDREFVSSLATRIIeLGENGVTDFSGSYDDYLR 523
Cdd:COG3840 150 ILLLDEPFSALDpalrqeM-------LDLvdelcRERGLTVLMVTHDPEDAARIADRVL-LVADGRIAADGPTAALLD 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-511 |
4.77e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSADV----GYFAQDH 391
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHYASKEVarriGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 ADdfADDMSLFDWMA-----------QWTQGGEQLVRGTLgRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:PRK10253 91 TT--PGDITVQELVArgryphqplftRWRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 461 DEPTNHLDM-ESIEALNL--ALDNYPG-TLIFVSHDREFVSSLATRIIELGENGV 511
Cdd:PRK10253 168 DEPTTWLDIsHQIDLLELlsELNREKGyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
4.99e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQDqfAYEDFS 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK--LYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVimgheelwavkaerDRIYSL-PEMSEADGMAVAElEVQfaefdgytaesrAGELllglgipLEQhfgPMSAVAPG 159
Cdd:PRK09544 82 LPLTV--------------NRFLRLrPGTKKEDILPALK-RVQ------------AGHL-------IDA---PMQKLSGG 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWL----EGVLTARNSTMIIISHDRHFLnsvcthMADLD 226
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLV------MAKTD 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-468 |
5.41e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS----------ADVGYFA 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlarARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QdhaddfaddmslFDWM-AQWTQGGEQLVRGTLGRML-------------FSNDEIKKSVKV--ISGGEQGRMLFGRLIL 452
Cdd:PRK13536 121 Q------------FDNLdLEFTVRENLLVFGRYFGMStreieavipslleFARLESKADARVsdLSGGMKRRLTLARALI 188
|
170
....*....|....*.
gi 489202159 453 KRPNVLVMDEPTNHLD 468
Cdd:PRK13536 189 NDPQLLILDEPTTGLD 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-233 |
7.28e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.94 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV--------MLEPNVRLGklrqdqfayEDFSVID 83
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgrvssLLGLGGGFN---------PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 TVIMGHeelwavkaerdRIYSlpeMSEADGMAVAELEVQFAEfdgytaesragelllglgipLEQHFG-PMSAVAPGWKL 162
Cdd:cd03220 104 NIYLNG-----------RLLG---LSRKEIDEKIDEIIEFSE--------------------LGDFIDlPVKTYSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGvLTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLF 233
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFqekcQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
320-478 |
9.25e-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: 67.29 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP-------------VDGGEVKWTDSADVGY 386
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvsvegdihyngIPYKEFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDhaddfaddmslfDW-MAQWTqggeqlVRGTLGrmlFS----NDEIkksVKVISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:cd03233 88 VSEE------------DVhFPTLT------VRETLD---FAlrckGNEF---VRGISGGERKRVSIAEALVSRASVLCWD 143
|
170
....*....|....*..
gi 489202159 462 EPTNHLDmeSIEALNLA 478
Cdd:cd03233 144 NSTRGLD--SSTALEIL 158
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-506 |
9.60e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD------SADVGYFAQDHA 392
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 393 ddfaddmsLFDWmaQWTQG----GEQLV-------RGTLGRMLFSNDEI---KKSVKVISGGEQGRMLFGRLILKRPNVL 458
Cdd:PRK11248 81 --------LLPW--RNVQDnvafGLQLAgvekmqrLEIAHQMLKKVGLEgaeKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 459 VMDEPTNHLDM---ESIEALNLALDNYPGTLIF-VSHDREFVSSLATRIIEL 506
Cdd:PRK11248 151 LLDEPFGALDAftrEQMQTLLLKLWQETGKQVLlITHDIEEAVFMATELVLL 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-477 |
9.69e-13 |
|
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: 67.68 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 334 LFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDG---GEV----------KWTDSadVGYFAQDhaDDFADDMS 400
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqprkpdQFQKC--VAYVRQD--DILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 lfdwmaqwtqggeqlVRGTL-------GRMLFSNDEIKKSVKV------------------ISGGEQGRMLFGRLILKRP 455
Cdd:cd03234 98 ---------------VRETLtytailrLPRKSSDAIRKKRVEDvllrdlaltriggnlvkgISGGERRRVSIAVQLLWDP 162
|
170 180
....*....|....*....|..
gi 489202159 456 NVLVMDEPTNHLDmeSIEALNL 477
Cdd:cd03234 163 KVLILDEPTSGLD--SFTALNL 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
320-471 |
1.19e-12 |
|
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: 67.05 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwTDSADVGYFaqdhadDFAD 397
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE-IDGIDISTI------PLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMSLFDWMAQwtqgGEQLVRGTLGRML-----FSNDEIKKSVKVISGGE---QGR---MLFGRLILKRPNVLVMDEPTNH 466
Cdd:cd03369 80 LRSSLTIIPQ----DPTLFSGTIRSNLdpfdeYSDEEIYGALRVSEGGLnlsQGQrqlLCLARALLKRPRVLVLDEATAS 155
|
....*
gi 489202159 467 LDMES 471
Cdd:cd03369 156 IDYAT 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-492 |
1.23e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHADDFA--- 396
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAllp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ------DDMSLFD--------WMAQW---TQGGEQLVRGTLGRMlfSNDEI-KKSVKVISGGEQGRMLFGRLILKRPNVL 458
Cdd:PRK11231 83 qhhltpEGITVRElvaygrspWLSLWgrlSAEDNARVNQAMEQT--RINHLaDRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489202159 459 VMDEPTNHLDM-ESIEALNL--ALDNYPGTLIFVSHD 492
Cdd:PRK11231 161 LLDEPTTYLDInHQVELMRLmrELNTQGKTVVTVLHD 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-510 |
1.40e-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: 69.83 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG--DLPVDGGEVKWTDS-------ADVGYFAQD 390
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HADDFADDMSLFD---W----------------MAQWTQG--GEQLVRGTLGRML----FSNDE-IKKSVKVI------- 437
Cdd:TIGR03269 81 PCPVCGGTLEPEEvdfWnlsdklrrrirkriaiMLQRTFAlyGDDTVLDNVLEALeeigYEGKEaVGRAVDLIemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 438 ---------SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESI----EALNLALDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:TIGR03269 161 rithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*.
gi 489202159 505 ELgENG 510
Cdd:TIGR03269 241 WL-ENG 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-230 |
1.43e-12 |
|
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: 67.05 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAK-PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE-------PNVRLGKLRQD- 72
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 QFAYEDFSVidtvimgheelwavkaerdriysLPEMSEADGMAVAeLEVqfAEFDGYTAESRAGELLLGLGIPLEQHFGP 152
Cdd:cd03292 81 GVVFQDFRL-----------------------LPDRNVYENVAFA-LEV--TGVPPREIRKRVPAALELVGLSHKHRALP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 153 MSaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVlTARNSTMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:cd03292 135 AE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweiMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
..
gi 489202159 229 EL 230
Cdd:cd03292 213 KL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
320-493 |
1.56e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRcLV--------GDLPVDGGEVkwTDSA----DVGYF 387
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVaglekpteGQIFIDGEDV--THRSiqqrDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHAddfaddmsLFDWMAQwtqgGEQLVRGTlgRML-FSNDEIKKSVK-----------------VISGGEQGRMLFGR 449
Cdd:PRK11432 84 FQSYA--------LFPHMSL----GENVGYGL--KMLgVPKEERKQRVKealelvdlagfedryvdQISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 450 -LILKrPNVLVMDEPTNHLD------M-ESIEALNLALDNypgTLIFVSHDR 493
Cdd:PRK11432 150 aLILK-PKVLLFDEPLSNLDanlrrsMrEKIRELQQQFNI---TSLYVTHDQ 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
322-503 |
1.57e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTL-------LRCLVGDLPVDGGEVKWTDSA------DVGYF 387
Cdd:PRK13639 4 TRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLflhfngiLKPTSGEVLIKGEPIKYDKKSllevrkTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHADD-FADDMSlfdwmaqwtqggEQLVRGTLGrMLFSNDEIKKSVKV-----------------ISGGEQGRMLFGR 449
Cdd:PRK13639 84 FQNPDDQlFAPTVE------------EDVAFGPLN-LGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 450 LILKRPNVLVMDEPTNHLD-MESIEALNLALD-NYPG-TLIFVSHDREFVSSLATRI 503
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDlNKEGiTIIISTHDVDLVPVYADKV 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-503 |
1.59e-12 |
|
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: 66.76 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSAD-----------VGY 386
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGYSirtdrkaarqsLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDhaDDFADDMSLFDWMAQWTQ------GGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:cd03263 80 CPQF--DALFDELTVREHLRFYARlkglpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 461 DEPTNHLDMESIEAL-NLALDNYPG-TLIFVSHDREFVSSLATRI 503
Cdd:cd03263 158 DEPTSGLDPASRRAIwDLILEVRKGrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
1.80e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 66.62 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdqfayedfsv 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtVIMGHEELWAVKAERDRIYSLPEMSEAD-GMAVAELEVQFAEFDGY---TAESRAGELLLGLGIpLEQHFGPMSAVA 157
Cdd:cd03265 58 ---TVAGHDVVREPREVRRRIGIVFQDLSVDdELTGWENLYIHARLYGVpgaERRERIDELLDFVGL-LEAADRLVKTYS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 158 PGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELR 231
Cdd:cd03265 134 GGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-504 |
1.80e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 317 RQAVTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK-----------WTDSAD 383
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 VGYFAQDHADDF-----ADDMSlF---------DWMAQWTQGGEQLVrgtlgRML-FSNDEIKKsvkvISGGEQGRMLFG 448
Cdd:PRK13635 83 VGMVFQNPDNQFvgatvQDDVA-FglenigvprEEMVERVDQALRQV-----GMEdFLNREPHR----LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 449 RLILKRPNVLVMDEPTNHLD-------MESIEALNlalDNYPGTLIFVSHDREFVSSlATRII 504
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDprgrrevLETVRQLK---EQKGITVLSITHDLDEAAQ-ADRVI 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
2.06e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrLGKlrqdQFAYEDfs 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-----DGE----PLDPED-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimgheelwavkaeRDRI-YsLPEMSeadG----MAVAELEVQFAEFDGYT---AESRAGELLLGLGI------PL 146
Cdd:COG4152 70 ------------------RRRIgY-LPEER---GlypkMKVGEQLVYLARLKGLSkaeAKRRADEWLERLGLgdrankKV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 147 EQhfgpMSavaPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTiRWLEGVLT--ARNSTMIIIS-HDrhfLNSV---C 219
Cdd:COG4152 128 EE----LS---KGNQQKVQLIAALLHDPELLILDEPFSGLDpVNV-ELLKDVIRelAAKGTTVIFSsHQ---MELVeelC 196
|
250
....*....|...
gi 489202159 220 THMADLDYGELRL 232
Cdd:COG4152 197 DRIVIINKGRKVL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
321-513 |
2.09e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV-------KWTDSA----------- 382
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgQLRDLYalseaerrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 --DVGYFAQDHADDFADDMS--------LfdwMAQ-WTQGGEqlVRGT----LGRMLFSNDEIKKSVKVISGGEQGRMLF 447
Cdd:PRK11701 88 rtEWGFVHQHPRDGLRMQVSaggnigerL---MAVgARHYGD--IRATagdwLERVEIDAARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 448 GRLILKRPNVLVMDEPTNHLDMeSIEA------------LNLAldnypgtLIFVSHDREFVSSLATRII-----ELGENG 510
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDV-SVQArlldllrglvreLGLA-------VVIVTHDLAVARLLAHRLLvmkqgRVVESG 234
|
...
gi 489202159 511 VTD 513
Cdd:PRK11701 235 LTD 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-230 |
2.17e-12 |
|
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: 69.16 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKlrqdqfayedfsviDTVIMGHEELwavKA 97
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-----GK--------------DLTKLSRRSL---RE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 98 ERDRI--------YSL-PEMSEADgmAVAE-LEVqFAEFDGYTAESRAGELL--LGLGIPLEQHFgpmsavaP-----GW 160
Cdd:COG1123 340 LRRRVqmvfqdpySSLnPRMTVGD--IIAEpLRL-HGLLSRAERRERVAELLerVGLPPDLADRY-------PhelsgGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 161 KLRVLLAQALFSDPDVLLLDEPTNHLDInTIRW-----LEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
320-527 |
2.47e-12 |
|
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: 66.49 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDSAD----VGY 386
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdSGRILIDGHDVRDYTLASlrrqIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQD-------------------------------HADDFADDMSL-FDwmaqwTQGGEqlvRGtlgrmlfsndeikksV 434
Cdd:cd03251 81 VSQDvflfndtvaeniaygrpgatreeveeaaraaNAHEFIMELPEgYD-----TVIGE---RG---------------V 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 435 KvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSHDREFVSSlATRIIELGENGVT 512
Cdd:cd03251 138 K-LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
250
....*....|....*
gi 489202159 513 DfSGSYDDYLRSQGV 527
Cdd:cd03251 216 E-RGTHEELLAQGGV 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
322-391 |
3.77e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.21 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADV-------------GYFA 388
Cdd:COG1137 6 AENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI-FLDGEDIthlpmhkrarlgiGYLP 84
|
...
gi 489202159 389 QDH 391
Cdd:COG1137 85 QEA 87
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-504 |
4.36e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSAD--VGYFAQ 389
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglehqtsGHIRFHGTDVSRLHARDrkVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHAddFADDMSLFDWMAqwtQGGEQLVRgtlgRMLFSNDEIKKSVKV-----------------ISGGEQGRMLFGRLIL 452
Cdd:PRK10851 82 HYA--LFRHMTVFDNIA---FGLTVLPR----RERPNAAAIKAKVTQllemvqlahladrypaqLSGGQKQRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 453 KRPNVLVMDEPTNHLDMESIEALNLAL----DNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
5.79e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.50 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLEPSAGqvmlepnvrlGKLRQDQFAYEDFS 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITS----------GDLIVDGLKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVImgHEELWAVKAErdrIYSLPEMSEADGMAVAELEVQFAEFDgyTAESRAGELLLGLGIPLEQHFGPmSAVAPGW 160
Cdd:PRK09493 70 VDERLI--RQEAGMVFQQ---FYLFPHLTALENVMFGPLRVRGASKE--EAEKQARELLAKVGLAERAHHYP-SELSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 161 KLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRWL--EGVltarnsTMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDpelrhevLKVMQDLaeEGM------TMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-212 |
6.10e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKIL-GndLE-PSAGQVMLepnvrlgklrqdqfayedf 79
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaG--LEtPDSGRIVL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 svidtvimGHEELWAVKAERDR-I------YSL-PEMSeadgmaVAE-----LEVQF---AEfdgytAESRAGELL--LG 141
Cdd:COG1118 62 --------NGRDLFTNLPPRERrVgfvfqhYALfPHMT------VAEniafgLRVRPpskAE-----IRARVEELLelVQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 142 LGiPLEQHFgpmsavaP-----GWKLRVLLAQALFSDPDVLLLDEPTNHLDI---NTIR-WLEGVLTARNSTMIIISHDR 212
Cdd:COG1118 123 LE-GLADRY-------PsqlsgGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-491 |
6.23e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL--VGDLpVDG----GEVkWTDSAD--------- 383
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDL-IPGarveGEI-LLDGEDiydpdvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 -----VGYFAQdHADDFAddMSLFDWMA------QWTQGGE--QLVRGTLGR-MLFsnDEIK----KSVKVISGGEQGRM 445
Cdd:COG1117 89 elrrrVGMVFQ-KPNPFP--KSIYDNVAyglrlhGIKSKSEldEIVEESLRKaALW--DEVKdrlkKSALGLSGGQQQRL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489202159 446 LFGRLILKRPNVLVMDEPTNHLDMES---IEALNLAL-DNYpgTLIFVSH 491
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPIStakIEELILELkKDY--TIVIVTH 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
6.33e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML-----------EPNVRLGKLRQDQF 74
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 75 AYEDFSVIDTVIMG---HEELWAVKAERDriyslpemseADGMAVAELEVQFAEFDGYTAESRAGelllglgipleqhfg 151
Cdd:PRK10253 92 TPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKAMQATGITHLADQSVDTLSG--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 152 pmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN-TIRWLEgVLTARNS----TMIIISHDrhfLNSVC---THMA 223
Cdd:PRK10253 147 -------GQRQRAWIAMVLAQETAIMLLDEPTTWLDIShQIDLLE-LLSELNRekgyTLAAVLHD---LNQACryaSHLI 215
|
....*..
gi 489202159 224 DLDYGEL 230
Cdd:PRK10253 216 ALREGKI 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-210 |
7.10e-12 |
|
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: 65.18 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKP---LFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGK-LRQDQFAYEDfSV 81
Cdd:cd03248 16 NVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD-----GKpISQYEHKYLH-SK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 IDTVimGHEELWAVKAERDRIyslpemseADGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAvapGWK 161
Cdd:cd03248 90 VSLV--GQEPVLFARSLQDNI--------AYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSG---GQK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA--RNSTMIIISH 210
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAH 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-526 |
8.60e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 329 YDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP------VDGGEVKwtdsadvgyfaqdhaddfadDMSLF 402
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslkINGIELR--------------------ELDPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 403 DWMAQ--WTQGGEQLVRGT------LGRMLFSNDEIKKSVKV------------------------ISGGEQGRMLFGRL 450
Cdd:PRK11174 420 SWRKHlsWVGQNPQLPHGTlrdnvlLGNPDASDEQLQQALENawvseflpllpqgldtpigdqaagLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 451 ILKRPNVLVMDEPTNHLDMES----IEALNLALDNYpgTLIFVSHDREFVSSLATriIELGENGVTDFSGSYDDYLRSQG 526
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRRQ--TTLMVTHQLEDLAQWDQ--IWVMQDGQIVQQGDYAELSQAGG 575
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-247 |
9.27e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVM-----LEPNVR-LGKLRQDqf 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpLDYSKRgLLALRQQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 75 ayedfsvIDTVIMG-HEELWAVKAERDRIYSLpemseaDGMAVAELEVQfaefdgytaeSRAGElllGLGIPLEQHF--G 151
Cdd:PRK13638 79 -------VATVFQDpEQQIFYTDIDSDIAFSL------RNLGVPEAEIT----------RRVDE---ALTLVDAQHFrhQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 152 PMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRwlegVLTARNSTMIIISHDRHFLNSVCTHMAD 224
Cdd:PRK13638 133 PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIR----RIVAQGNHVIISSHDIDLIYEISDAVYV 208
|
250 260
....*....|....*....|....*
gi 489202159 225 LDYGELRLF--PGNYDEYMTAAEQA 247
Cdd:PRK13638 209 LRQGQILTHgaPGEVFACTEAMEQA 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-510 |
1.18e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.05 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 338 LSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLPVDGGEVkwTDSADVGyfAQDHADD-----FADDmSLFDWMAQWTQG 411
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVL--INGVDVT--AAPPADRpvsmlFQEN-NLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 412 G-------------EQLVRGTLGRMLFSNDEiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD-MESIEALNL 477
Cdd:cd03298 92 GlglspglkltaedRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 489202159 478 ALDNYPG---TLIFVSHDREFVSSLATRIIELgENG 510
Cdd:cd03298 171 VLDLHAEtkmTVLMVTHQPEDAKRLAQRVVFL-DNG 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-210 |
1.69e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQF-GAKPLfENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPnvrlgklRQDQFAYEDFSVIDT 84
Cdd:PRK11288 9 GIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-------QEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 85 VIMGHEELWAVkaerdriyslPEMSEADGMAVAELEVQFAEFDGYTAESRAGELLLGLGIPLEQHfGPMSAVAPGWKLRV 164
Cdd:PRK11288 81 VAIIYQELHLV----------PEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPD-TPLKYLSIGQRQMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489202159 165 LLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISH 210
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVireLRAEGRVILYVSH 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
320-506 |
1.71e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDSAD--VGYFAQD 390
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKDgqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HADDFADDMSL-FDWMAQWTQGG--EQLVRGTLGRMLFSNDEIKKSV-----KV-------------ISGGEQGRMLFGR 449
Cdd:PRK10619 86 QLRLLRTRLTMvFQHFNLWSHMTvlENVMEAPIQVLGLSKQEARERAvkylaKVgideraqgkypvhLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 450 LILKRPNVLVMDEPTNHLDMESI-EALNL--ALDNYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVgEVLRImqQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
1.78e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.33 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 19 NVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV--------MLEPNVrlGklrqdqFaYEDFSVIDTVIMghe 90
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsaLLELGA--G------F-HPELTGRENIYL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 91 elwavkaeRDRIYslpemseadGMAVAELE------VQFAEfdgytaesragelllglgipLEQHFG-PMSAVAPGWKLR 163
Cdd:COG1134 112 --------NGRLL---------GLSRKEIDekfdeiVEFAE--------------------LGDFIDqPVKTYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 164 VLLAQALFSDPDVLLLDEptnhldintirWLeGV---------------LTARNSTMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:COG1134 155 LAFAVATAVDPDILLVDE-----------VL-AVgdaafqkkclarireLRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
....*
gi 489202159 229 ELRLF 233
Cdd:COG1134 223 RLVMD 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
321-463 |
1.93e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 64.22 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTD------------SADVGYFA 388
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGqdithlpmheraRLGIGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDhADDFAdDMSLFDWMAQWTQGGEQLVRGTLGRML------FSNDEIKKSVKV-ISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:TIGR04406 83 QE-ASIFR-KLTVEENIMAVLEIRKDLDRAEREERLealleeFQISHLRDNKAMsLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 489202159 462 EP 463
Cdd:TIGR04406 161 EP 162
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-526 |
2.01e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 305 PFIRF--EQYKKLHRQAVTVENISKGYDGK--PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK--- 377
Cdd:PRK11160 322 PEVTFptTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlng 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 378 -----WTDSA--------------------DVGYFAQDHADDFA---------------DDMSLFDWMAqwtQGGEQLvr 417
Cdd:PRK11160 402 qpiadYSEAAlrqaisvvsqrvhlfsatlrDNLLLAAPNASDEAlievlqqvgleklleDDKGLNAWLG---EGGRQL-- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 418 gtlgrmlfsndeikksvkviSGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMES-IEALNLALDNYPG-TLIFVSH---- 491
Cdd:PRK11160 477 --------------------SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHrltg 536
|
250 260 270
....*....|....*....|....*....|....*....
gi 489202159 492 ----DRefvsslatriIELGENGVTDFSGSYDDYLRSQG 526
Cdd:PRK11160 537 leqfDR----------ICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
320-376 |
2.66e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 2.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 320 VTVENISKGY-----DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV 376
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
320-526 |
2.67e-11 |
|
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: 63.66 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSA----DVGY 386
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQrfyvpenGRVLVDGHDLALADPAwlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHA---DDFADDMSL-------------------FDWMAQWTQGGEQLVrGTLGRMLfsndeikksvkviSGGEQGR 444
Cdd:cd03252 81 VLQENVlfnRSIRDNIALadpgmsmervieaaklagaHDFISELPEGYDTIV-GEQGAGL-------------SGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLDMESIEAL--NLALDNYPGTLIFVSHDREFVSSlATRIIELGENGVTDfSGSYDDYL 522
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAImrNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELL 224
|
....
gi 489202159 523 RSQG 526
Cdd:cd03252 225 AENG 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
2.69e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 63.51 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE------PNVR---LGKLRQD 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 QFAYEDFSVIDTVIMG----HEELWAVKAE-RDRIYSLPEMSEADGMAvaelevqfaefDGYTAEsragelLLGlgiple 147
Cdd:cd03296 83 YALFRHMTVFDNVAFGlrvkPRSERPPEAEiRAKVHELLKLVQLDWLA-----------DRYPAQ------LSG------ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 148 qhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHD 211
Cdd:cd03296 140 -----------GQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHD 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-504 |
4.68e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.85 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 345 GERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDsadvgyfaqdhADDFADDMslfdwmaqwtqggeqlvrgtlgRML 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------GEDILEEV----------------------LDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 425 FSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDN---------YPGTLIFVSHDREF 495
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllkseKNLTVILTTNDEKD 128
|
....*....
gi 489202159 496 VSSLATRII 504
Cdd:smart00382 129 LGPALLRRR 137
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
320-376 |
4.85e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 4.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV 376
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV 58
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
5.08e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE-------PNVRLGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQfayeDFSVIDTVimghEEL-----WAvkaerdriYSLPEMSEADGMAVAE-LEvqfaefdgytaesragelLLGLG 143
Cdd:COG4604 81 RQEN----HINSRLTV----RELvafgrFP--------YSKGRLTAEDREIIDEaIA------------------YLDLE 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 144 iPLEQHF-----GpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDI----NTIRWLEGVLTARNSTMIIISHD 211
Cdd:COG4604 127 -DLADRYldelsG-------GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-210 |
5.20e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdqfayedfsv 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI----------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtVIMGHEELWAVKAERDRIYSLPEMSEAD----------------GMAVAELE------VQFAEFdgytaESRAGell 139
Cdd:PRK13536 99 ---TVLGVPVPARARLARARIGVVPQFDNLDleftvrenllvfgryfGMSTREIEavipslLEFARL-----ESKAD--- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 140 lglgipleqhfGPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT--IRW--LEGVLtARNSTMIIISH 210
Cdd:PRK13536 168 -----------ARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLL-ARGKTILLTTH 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
321-511 |
5.29e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLF---------KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDsADVGYFAQDH 391
Cdd:PRK10419 5 NVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-EPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 ADDFADDMSLFDWMAQWTQGGEQLVRGTLG---RMLFSNDEIKKSVKV--------------------ISGGEQGRMLFG 448
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAVNPRKTVREIIReplRHLLSLDKAERLARAsemlravdlddsvldkrppqLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 449 RLILKRPNVLVMDEPTNHLD-MESIEALNL--ALDNYPGT-LIFVSHDREFVSSLATRIIELGENGV 511
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDlVLQAGVIRLlkKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-211 |
5.86e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 62.31 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFG-NGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlgklrqdqfayedfsviDT 84
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN---------------------GT 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 85 VIMGHEELWAVKAERDRI------YSL-PEMSEAD----GMAVAELEVQFAEFDGYTAesragelLLGLGIPLEQHFGPM 153
Cdd:cd03297 60 VLFDSRKKINLPPQQRKIglvfqqYALfPHLNVREnlafGLKRKRNREDRISVDELLD-------LLGLDHLLNRYPAQL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 154 SAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHD 211
Cdd:cd03297 133 SG---GEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
316-378 |
6.34e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 62.83 E-value: 6.34e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 316 HRQAVTVENISKGYDGkplFK---GLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW 378
Cdd:COG4674 7 HGPILYVEDLTVSFDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLF 69
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
7.50e-11 |
|
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: 62.25 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAK--PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEP-NVR---LGKLR----- 70
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVRdytLASLRrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 --QDQFAyedFSviDTVimgheelwavkaeRDRI-YSLPEMSEADGMAVAELeVQFAEF-----DGYtaESRAGElllgL 142
Cdd:cd03251 81 vsQDVFL---FN--DTV-------------AENIaYGRPGATREEVEEAARA-ANAHEFimelpEGY--DTVIGE----R 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 143 GIPLeqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT--ARNSTMIIISH 210
Cdd:cd03251 136 GVKL----------SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALErlMKNRTTFVIAH 195
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-472 |
7.92e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS------------ADVGYF 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDhADDFAdDMSLFDWMAQWTQGGEQLV---RGTLGRML---FSNDEIKKSV-KVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:PRK10895 84 PQE-ASIFR-RLSVYDNLMAVLQIRDDLSaeqREDRANELmeeFHIEHLRDSMgQSLSGGERRRVEIARALAANPKFILL 161
|
170
....*....|..
gi 489202159 461 DEPTNHLDMESI 472
Cdd:PRK10895 162 DEPFAGVDPISV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
326-389 |
9.99e-11 |
|
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: 61.33 E-value: 9.99e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 326 SKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSadVGYFAQ 389
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQ 73
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
1.01e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVM---LEPNvrlgkLRQDQFAYEdfsvIdTVIMGH-EELW 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPF-----KRRKEFARR----I-GVVFGQrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 94 ---AVkaeRD------RIYSLPEmseadgmavaelevqfAEFdgytaESRAGEL--LLGLG----IPLEQhfgpMSAvap 158
Cdd:COG4586 109 wdlPA---IDsfrllkAIYRIPD----------------AEY-----KKRLDELveLLDLGelldTPVRQ----LSL--- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINT-------IRWLEgvlTARNSTMIIISHD 211
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeairefLKEYN---RERGTTILLTSHD 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-508 |
1.10e-10 |
|
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: 61.83 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGK----PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEVKWTDSA------ 382
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTLLSGKelrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 -DVGYFAQdHaddfaddmslFDWMAQWTqggeqlVRGTLGRML----FSNDEIKKSVK-----V------------ISGG 440
Cdd:cd03258 82 rRIGMIFQ-H----------FNLLSSRT------VFENVALPLeiagVPKAEIEERVLellelVgledkadaypaqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLDME---SIEALNLALDNYPG-TLIFVSHDREFVSSLATR--------IIELGE 508
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITHEMEVVKRICDRvavmekgeVVEEGT 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
1.27e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.65 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQdQFAY--ED---FSvi 82
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESLRR-QIGVvpQDtflFS-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DTVimgheelwavkaeRDRI-YSLPEMSEADGMAVAELeVQFAEF-----DGYtaESRAGELllglGIPLeqhfgpmSAv 156
Cdd:COG1132 428 GTI-------------RENIrYGRPDATDEEVEEAAKA-AQAHEFiealpDGY--DTVVGER----GVNL-------SG- 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 157 apGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA--RNSTMIIISH 210
Cdd:COG1132 480 --GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-187 |
1.28e-10 |
|
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: 61.55 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGA-KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgklrqdqFAYEDFS 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF--------------IDGEDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVimgheELwavkaeRDRI-YS------LPEMSEADGMA-VAELEvqfaEFDGYTAESRAGELLLGLGIPlEQHFG- 151
Cdd:cd03295 67 EQDPV-----EL------RRKIgYViqqiglFPHMTVEENIAlVPKLL----KWPKEKIRERADELLALVGLD-PAEFAd 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 489202159 152 --PmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:cd03295 131 ryP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-211 |
1.52e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQvMLEPNVRLGKLRQD-QFAYEDF----- 79
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDtRLMFQDArllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 -SVIDTVIMGHEELWAVKAErdriyslpEMSEADGMAvaelevqfaefdgytaeSRAGELllglgiPleqhfgpmSAVAP 158
Cdd:PRK11247 96 kKVIDNVGLGLKGQWRDAAL--------QALAAVGLA-----------------DRANEW------P--------AALSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIISHD 211
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-183 |
1.55e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAkplF---ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML-----EPN-----VRLGKLRQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGdiatrRRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 QFA-YEDFSVidtvimgHE--ELWAvkaerdRIYSLPEmsEADGMAVAELEVQFaEFDGYtAESRAGELLLGLgipleqh 149
Cdd:NF033858 347 AFSlYGELTV-------RQnlELHA------RLFHLPA--AEIAARVAEMLERF-DLADV-ADALPDSLPLGI------- 402
|
170 180 190
....*....|....*....|....*....|....
gi 489202159 150 fgpmsavapgwKLRVLLAQALFSDPDVLLLDEPT 183
Cdd:NF033858 403 -----------RQRLSLAVAVIHKPELLILDEPT 425
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-210 |
1.78e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLgklRQDQFAYEDFSVidtVIMGHEELW 93
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPL---VQYDHHYLHRQV---ALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 94 AVKAERDRI-YSLPEMSEADGMAVAELEvqfaefdgyTAESRAGELLLGLGIPLEQHFGPMSAvapGWKLRVLLAQALFS 172
Cdd:TIGR00958 567 FSGSVRENIaYGLTDTPDEEIMAAAKAA---------NAHDFIMEFPNGYDTEVGEKGSQLSG---GQKQRIAIARALVR 634
|
170 180 190
....*....|....*....|....*....|....*...
gi 489202159 173 DPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISH 210
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.97e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQV-----MLEPNVRLGK------ 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEqPEAGTIrvgdiTIDTARSLSQqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 69 -LRQD-QFAYEDF------SVIDTVIMGHEelwAVKAE-RDRiyslpemseadgmavaelevqfaefdgytAESRAGELL 139
Cdd:PRK11264 82 qLRQHvGFVFQNFnlfphrTVLENIIEGPV---IVKGEpKEE-----------------------------ATARARELL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 140 LGLGIPLEQHFGPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRwlegVLTARNSTMIIISHDR 212
Cdd:PRK11264 130 AKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEM 204
|
250
....*....|....*.
gi 489202159 213 HFLNSVCTHMADLDYG 228
Cdd:PRK11264 205 SFARDVADRAIFMDQG 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
319-480 |
2.27e-10 |
|
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: 62.92 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK-PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW--TDSADV---------GY 386
Cdd:COG5265 357 EVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdgQDIRDVtqaslraaiGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQD-------------------------------HADDFAddMSLFDWMAqwTQGGEqlvRGtlgrmlfsndeikksVK 435
Cdd:COG5265 437 VPQDtvlfndtiayniaygrpdaseeeveaaaraaQIHDFI--ESLPDGYD--TRVGE---RG---------------LK 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 436 ViSGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALD 480
Cdd:COG5265 495 L-SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
2.39e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 19 NVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNvRLGKLRQdqfayedfsvidtvimgheelwAVKAE 98
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-PMSKLSS----------------------AAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 99 -RDR----IYS----LPEMSEADGMAVAEL--EVQFAEfdgytAESRAGELLLGLGIPLEQHFGPmSAVAPGWKLRVLLA 167
Cdd:PRK11629 84 lRNQklgfIYQfhhlLPDFTALENVAMPLLigKKKPAE-----INSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 168 QALFSDPDVLLLDEPTNHLDI---NTIRWLEGVLTARNST-MIIISHD 211
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
2.45e-10 |
|
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: 60.66 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEP----NVRLGKLRQ--DQFAY--------E 77
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQlrRQIGMifqqfnliE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 DFSVIDTVIMGheelwavkaerdriySLPEMSEADGMA--VAELEVQfaefdgytaesRAGELLLGLGIpLEQHFGPMSA 155
Cdd:cd03256 92 RLSVLENVLSG---------------RLGRRSTWRSLFglFPKEEKQ-----------RALAALERVGL-LDKAYQRADQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 156 VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA----RNSTMIIISHD 211
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinreEGITVIVSLHQ 204
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-476 |
2.45e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 330 DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV----KWTDSAD----VGYFAqdHADDFADDMS- 400
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDrsrfMAYLG--HLPGLKADLSt 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 ---------LFDWMAQWTQGGEQLVRGTLGRMlfsndeiKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMES 471
Cdd:PRK13543 100 lenlhflcgLHGRRAKQMPGSALAIVGLAGYE-------DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
....*
gi 489202159 472 IEALN 476
Cdd:PRK13543 173 ITLVN 177
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-510 |
2.49e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGYfAQDHADDFADDM 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE-AREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 SLFDWM-----------AQWTQGGEQLVRgTLGRMLFSNDeikkSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:PRK11247 91 RLLPWKkvidnvglglkGQWRDAALQALA-AVGLADRANE----WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 469 ------MES-IEALNLaldNYPGTLIFVSHDREFVSSLATRI--IELGENG 510
Cdd:PRK11247 166 altrieMQDlIESLWQ---QHGFTVLLVTHDVSEAVAMADRVllIEEGKIG 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
320-527 |
2.54e-10 |
|
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: 60.63 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKP---LFKGLSLQVEAGERVAIIGPNGIGKTT----LLR---CLVGDLPVDGGEVK-----WTdSADV 384
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERfydPTSGEILLDGVDIRdlnlrWL-RSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 385 GYFAQD----------------------HADDFADDMSLFDWMAQWTQGGEQLVrGTLGRMLfsndeikksvkviSGGEQ 442
Cdd:cd03249 80 GLVSQEpvlfdgtiaenirygkpdatdeEVEEAAKKANIHDFIMSLPDGYDTLV-GERGSQL-------------SGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 443 GRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSHdRefVSSL--ATRIIELGENGVTDfSGSY 518
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH-R--LSTIrnADLIAVLQNGQVVE-QGTH 221
|
....*....
gi 489202159 519 DDYLRSQGV 527
Cdd:cd03249 222 DELMAQKGV 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-230 |
2.59e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNV-RLGKlrqdqfayeDFSVIDTVIMGHEel 92
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlYFGK---------DIFQIDAIKLRKE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 93 waVKAERDRIYSLPEMSEADGMAVAeLEVQFAEfDGYTAESRAGELLLGLGIPLEQH---FGPMSAVAPGWKLRVLLAQA 169
Cdd:PRK14246 92 --VGMVFQQPNPFPHLSIYDNIAYP-LKSHGIK-EKREIKKIVEECLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 170 LFSDPDVLLLDEPTNHLDINTIRWLEGVLT--ARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-504 |
2.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGY-DGKPL----FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkwtdsadvgyfaqdhaddFA 396
Cdd:PRK13637 5 IENLTHIYmEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI------------------II 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 DDMSLFDWMAQWT----------QGGE-QLVRGTL--------GRMLFSNDEIKKSVKV-------------------IS 438
Cdd:PRK13637 67 DGVDITDKKVKLSdirkkvglvfQYPEyQLFEETIekdiafgpINLGLSEEEIENRVKRamnivgldyedykdkspfeLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 439 GGEQGRMLFGRLILKRPNVLVMDEPTNHLD-------MESIEALNlalDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-210 |
2.72e-10 |
|
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: 60.71 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLR-------QDQFAYEDfSVI 82
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRraigvvpQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DTVIMGH-----EELW-AVKAER--DRIYSLPemseadgmavaelevqfaefDGYtaESRAGELLLGLgipleqhfgpms 154
Cdd:cd03253 93 YNIRYGRpdatdEEVIeAAKAAQihDKIMRFP--------------------DGY--DTIVGERGLKL------------ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 155 avAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISH 210
Cdd:cd03253 139 --SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALrdVSKGRTTIVIAH 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-523 |
3.39e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 338 LSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP------VDGGEVKWTDSADV----GYFAQDHADDFAddMSLFDWMA- 406
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiqFAGQPLEAWSAAELarhrAYLSQQQTPPFA--MPVFQYLTl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 407 -QWTQGGEQLVRGTLG---RMLFSNDEIKKSVKVISGGEQGRMLFGRLILK-----RPN--VLVMDEPTNHLDMESIEAL 475
Cdd:PRK03695 93 hQPDKTRTEAVASALNevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 476 NLALDNYP---GTLIFVSHDREFVSSLATRIIELgENGVTDFSGSYDDYLR 523
Cdd:PRK03695 173 DRLLSELCqqgIAVVMSSHDLNHTLRHADRVWLL-KQGKLLASGRRDEVLT 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-211 |
3.69e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFE-----NVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlEPNVRLGKLRQDQFAY 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI--EWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 EdfSVIDTVIMG---HEELWAVKAERDRI--------YSLPEMS-EAD------GMAVAELEvqfaefdgytAESRAGEL 138
Cdd:PRK13651 81 E--KVLEKLVIQktrFKKIKKIKEIRRRVgvvfqfaeYQLFEQTiEKDiifgpvSMGVSKEE----------AKKRAAKY 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 139 LLGLGIPLEqhFGPMS--AVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRWLE--GVLTARNSTMIIISHD 211
Cdd:PRK13651 149 IELVGLDES--YLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-504 |
4.97e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.87 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 336 KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwtdsadV-GYFAQDHADDFADDMSLFdwMAQWTQ---- 410
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VlGYVPFKRRKEFARRIGVV--FGQRSQlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 411 ---------------GGEQLVRGTLGRM--LFS-NDEIKKSVKVISGGEqgRMLfGRLI---LKRPNVLVMDEPTNHLDM 469
Cdd:COG4586 111 lpaidsfrllkaiyrIPDAEYKKRLDELveLLDlGELLDTPVRQLSLGQ--RMR-CELAaalLHRPKILFLDEPTIGLDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489202159 470 ES-------IEALNlalDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG4586 188 VSkeairefLKEYN---RERGTTILLTSHDMDDIEALCDRVI 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
7.18e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrlgklrqdqfayedfs 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimGHEELWAVKAERDRI------YSL-PEMSeadgmaVAE-----LEVQfaEFDGYTAESRAGELL--LGLGipl 146
Cdd:COG3842 65 -------DGRDVTGLPPEKRNVgmvfqdYALfPHLT------VAEnvafgLRMR--GVPKAEIRARVAELLelVGLE--- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 147 eqHFG---P--MSavaPGWKLRVLLAQALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIISHDR 212
Cdd:COG3842 127 --GLAdryPhqLS---GGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
337-468 |
8.90e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 337 GLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPvDGGEVKW--TDSADV---------GYFAQDHADDFAddMSLFDWM 405
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLngRPLSDWsaaelarhrAYLSQQQSPPFA--MPVFQYL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 406 A--QWTQGGEQLVRGTLGRM---LFSNDEIKKSVKVISGGEQGRMLFGRLILK-------RPNVLVMDEPTNHLD 468
Cdd:COG4138 91 AlhQPAGASSEAVEQLLAQLaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
320-504 |
9.01e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPL-FkglSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSAD----------VGYFA 388
Cdd:PRK10771 2 LKLTDITWLYHHLPMrF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNGQDhtttppsrrpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHaddfaddmSLFDWMAQWTQGGEQLVRGtlgrmLFSNDEIKKSVKVI-----------------SGGEQGRMLFGRLI 451
Cdd:PRK10771 78 QEN--------NLFSHLTVAQNIGLGLNPG-----LKLNAAQREKLHAIarqmgiedllarlpgqlSGGQRQRVALARCL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 452 LKRPNVLVMDEPTNHLD----MESIEALNLALDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK10771 145 VREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSL 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
9.48e-10 |
|
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: 57.71 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFG--AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML--EPNVRLGKLRQDQfaye 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgVPVSDLEKALSSL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 dFSVIDtvimgheelwavkaerDRIYSlpemseadgmavaelevqfaeFDgytaesraGELLLGLGIPLeqhfgpmsavA 157
Cdd:cd03247 77 -ISVLN----------------QRPYL---------------------FD--------TTLRNNLGRRF----------S 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 158 PGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISH 210
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfeVLKDKTLIWITH 155
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-190 |
1.02e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.33 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE------PNVRLGKLRQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 75 AYEDFSVIDTVIMGHEELWAVKAERdriyslpemseadgmavaelevqfaefdgytaESRAGELLLGLGIP-LEQHFgpM 153
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQR--------------------------------LEIAHQMLKKVGLEgAEKRY--I 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 489202159 154 SAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT 190
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
336-508 |
1.07e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 336 KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtdsadvgyFAQDhaddfADDMSLFDWMAqwTQGGEQL 415
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--------LGKD-----LLGMKDDEWRA--VRSDIQM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 416 V----------RGTLGRML----------FSNDEIKKSVKVI------------------SGGEQGRMLFGR-LILKrPN 456
Cdd:PRK15079 103 IfqdplaslnpRMTIGEIIaeplrtyhpkLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIARaLILE-PK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 457 VLVMDEPTNHLDMeSIEA--LNL--ALDNYPG-TLIFVSHDREFVSSLATRI--------IELGE 508
Cdd:PRK15079 182 LIICDEPVSALDV-SIQAqvVNLlqQLQREMGlSLIFIAHDLAVVKHISDRVlvmylghaVELGT 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-502 |
1.08e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL--VGDLPVD---GGEVKW---------TDSAD-- 383
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYnghniysprTDTVDlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 --VGYFAQdHADDFAddMSLFdwmaqwtqggEQLVRG----------TLGRMLFSN-------DEIK----KSVKVISGG 440
Cdd:PRK14239 86 keIGMVFQ-QPNPFP--MSIY----------ENVVYGlrlkgikdkqVLDEAVEKSlkgasiwDEVKdrlhDSALGLSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLDMES---IEALNLAL-DNYpgTLIFVSHDREFVSSLATR 502
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISagkIEETLLGLkDDY--TMLLVTRSMQQASRISDR 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
330-506 |
1.09e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.57 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 330 DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA-----------DVGYFAQDHAdDFAD- 397
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqQVSYCAQTPT-LFGDt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 --DMSLFDWMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL 475
Cdd:PRK10247 97 vyDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|....*
gi 489202159 476 NLALDNYPG----TLIFVSHDREFVSSlATRIIEL 506
Cdd:PRK10247 177 NEIIHRYVReqniAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
1.57e-09 |
|
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: 58.50 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE--------PNVR-LGKLRQDQFAYEDFSVIDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 89 HEELWAVKAERDRiySLPEMSEadgmavaelevqfaefdgytaesragelLLGLGIPLEQHFGPMSAvapGWKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAE----------------------------MLGIDHLLNRKPETLSG---GEQQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489202159 169 ALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
331-491 |
2.29e-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: 60.15 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 331 GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQ----------------DHADD 394
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymtlgtlrdqiiypDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 FAD-DMSLFDW--MAQWTQGGEQLVRGTlgrmlfSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMES 471
Cdd:TIGR00954 544 MKRrGLSDKDLeqILDNVQLTHILEREG------GWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|
gi 489202159 472 IEALNLALDNYPGTLIFVSH 491
Cdd:TIGR00954 618 EGYMYRLCREFGITLFSVSH 637
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-211 |
2.57e-09 |
|
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: 58.04 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 3 STANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKlrqdqfayedfsvi 82
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID-----GQ-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DTVIMGHEELWAVKaeRDRIYS-------LPEMSEADGMAVAeLEVQfaEFDGYTAESRAGELL--LGLGIPLEQHFGPM 153
Cdd:cd03294 87 DIAAMSRKELRELR--RKKISMvfqsfalLPHRTVLENVAFG-LEVQ--GVPRAEREERAAEALelVGLEGWEHKYPDEL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 154 SAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTA----RNSTMIIISHD 211
Cdd:cd03294 162 SG---GMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqaeLQKTIVFITHD 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-212 |
3.06e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKLRQDQFAYEdfSVIDTV 85
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-----GVDLSHVPPYQ--RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMGHEELWAVKAERDRIYSLPEmseaDGMAVAELevqfaefdgytaESRAGELllgLGIPLEQHFGPMS--AVAPGWKLR 163
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQ----DKLPKAEI------------ASRVNEM---LGLVHMQEFAKRKphQLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 164 VLLAQALFSDPDVLLLDEPTNHLD--------INTIRWLEGVltarNSTMIIISHDR 212
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQ 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-506 |
3.32e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 336 KGLSLQVEAGERVAIIGPNGIGKTTL---LRCL----VGDLPVDGGEVKWTDSADVGYFAQDHaddFADDMSLFDWMAQW 408
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLmniLGCLdkptSGTYRVAGQDVATLDADALAQLRREH---FGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 409 T-----------QGGEQLVRGTLGRMLFSN----DEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIE 473
Cdd:PRK10535 102 TaaqnvevpavyAGLERKQRLLRAQELLQRlgleDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 489202159 474 ---ALNLALDNYPGTLIFVSHDREfVSSLATRIIEL 506
Cdd:PRK10535 182 evmAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
323-492 |
3.33e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL--VGDLpVDGGEVKwtdsADVGYFAQDHADDFADDM- 399
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGFRVE----GKVTFHGKNLYAPDVDPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 -----------------SLFDWMA-----QWTQGG-EQLVRGTLGRMLFSN---DEIKKSVKVISGGEQGRMLFGRLILK 453
Cdd:PRK14243 89 vrrrigmvfqkpnpfpkSIYDNIAygariNGYKGDmDELVERSLRQAALWDevkDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489202159 454 RPNVLVMDEPTNHLDMES---IEALNLAL-DNYpgTLIFVSHD 492
Cdd:PRK14243 169 QPEVILMDEPCSALDPIStlrIEELMHELkEQY--TIIIVTHN 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-508 |
3.43e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADV---------------GY 386
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-WFSGHDItrlknrevpflrrqiGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHadDFADDMSLFDWMAQwtqggEQLVRGTlgrmlfSNDEIKKSV-----KV------------ISGGEQGRMLFGR 449
Cdd:PRK10908 84 IFQDH--HLLMDRTVYDNVAI-----PLIIAGA------SGDDIRRRVsaaldKVglldkaknfpiqLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 450 LILKRPNVLVMDEPTNHLD---MESIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGE 508
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
5.20e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.71 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE--PNVRLGKLRQDQFayEDFSVIDtvimgheelWav 95
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkQITEPGPDRMVVF--QNYSLLP---------W-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 96 KAERDRIY-----SLPEMSEADGMAVAELEVQfaefdgytaesragelLLGLGIPLEQHFGPMSAvapGWKLRVLLAQAL 170
Cdd:TIGR01184 69 LTVRENIAlavdrVLPDLSKSERRAIVEEHIA----------------LVGLTEAADKRPGQLSG---GMKQRVAIARAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 171 FSDPDVLLLDEPTNHLDINTIRWLEGVL----TARNSTMIIISHD 211
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
5.69e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.58 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQ-------VMLEPNVRLGKLRQDQFAYedfsvidtvIMghe 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLRREHFGF---------IF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 91 elwavkaerDRIYSLPEMSEADGMavaELEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPmSAVAPGWKLRVLLAQAL 170
Cdd:PRK10535 93 ---------QRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489202159 171 FSDPDVLLLDEPTNHLDINTIRWLEGVL---TARNSTMIIISHD 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILhqlRDRGHTVIIVTHD 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
321-491 |
6.32e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG--DLPVDGGEVkwtdsadvgyfaqdhaddfadd 398
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 399 msLFDwmaqwtqgGEQLV------RGTLGRML-FSNDEIKKSVKVI----------SGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:cd03217 60 --LFK--------GEDITdlppeeRARLGIFLaFQYPPEIPGVKNAdflryvnegfSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190
....*....|....*....|....*....|...
gi 489202159 462 EPTNHLDMESIEALNLALDNY--PGT-LIFVSH 491
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLreEGKsVLIITH 162
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
320-507 |
6.83e-09 |
|
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: 56.35 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGyfaqdhaddfad 397
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI-LIDGVDIS------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 398 DMSLFDW---MAQWTQggE-QLVRGTLgRM------LFSNDEI---------KKSVK---------VISGGE---QG-RM 445
Cdd:cd03244 70 KIGLHDLrsrISIIPQ--DpVLFSGTI-RSnldpfgEYSDEELwqalervglKEFVEslpggldtvVEEGGEnlsVGqRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 446 LF--GRLILKRPNVLVMDEPTNHLDMESIEALNLAL-DNYPG-TLIFVSH--------DREFVSSlATRIIELG 507
Cdd:cd03244 147 LLclARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDcTVLTIAHrldtiidsDRILVLD-KGRVVEFD 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-511 |
6.99e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVD----------GGEVKWT---------D 380
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellGRTVQREgrlardirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 381 SADVGYFAQDHadDFADDMSLFD------------W---MAQWTQGGEQLVRGTLGRMLFSNDEIKKsVKVISGGEQGRM 445
Cdd:PRK09984 85 RANTGYIFQQF--NLVNRLSVLEnvligalgstpfWrtcFSWFTREQKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 446 LFGRLILKRPNVLVMDEPTNHLDMES----IEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGENGV 511
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-232 |
8.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILG--NDLEPSA---------GQVMLEPNVRLGKL- 69
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVrvegrveffNQNIYERRVNLNRLr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQFAYED-----FSVIDTVIMGHEEL-WAVKAERDRIYSlpemseaDGMAVAEL--EVQfaefdgYTAESRAGELllg 141
Cdd:PRK14258 88 RQVSMVHPKpnlfpMSVYDNVAYGVKIVgWRPKLEIDDIVE-------SALKDADLwdEIK------HKIHKSALDL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 142 lgipleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNS-TMIIISHDRHFLNS 217
Cdd:PRK14258 152 ---------------SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLiqsLRLRSElTMVIVSHNLHQVSR 216
|
250
....*....|....*
gi 489202159 218 VCTHMADLDYGELRL 232
Cdd:PRK14258 217 LSDFTAFFKGNENRI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-504 |
8.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDG---KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV-----------KWTDSADVG 385
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDHADDFA-----DDMSL--------FDWMAQWTQGGEQLVrgtlGRMLFSNDEIKKsvkvISGGEQGRMLFGRLIL 452
Cdd:PRK13650 85 MVFQNPDNQFVgatveDDVAFglenkgipHEEMKERVNEALELV----GMQDFKEREPAR----LSGGQKQRVAIAGAVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 453 KRPNVLVMDEPTNHLD----MESIEALNLALDNYPGTLIFVSHDREFVsSLATRII 504
Cdd:PRK13650 157 MRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
320-491 |
9.56e-09 |
|
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: 55.94 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKP---LFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV------------KWTDSA-- 382
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyehKYLHSKvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 ---------------DVGYFAQD-------------HADDFADDMSLfdwmAQWTQGGEqlvRGTLgrmlfsndeikksv 434
Cdd:cd03248 92 lvgqepvlfarslqdNIAYGLQScsfecvkeaaqkaHAHSFISELAS----GYDTEVGE---KGSQ-------------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 435 kvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG--TLIFVSH 491
Cdd:cd03248 151 --LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
319-504 |
1.37e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.78 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK-PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADVGyfAQDHAD-DFA 396
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVN--ELEPADrDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ---------DDMSLFDWMAQWTQggeqlVRGTlgrmlfSNDEIKKSVK-----------------VISGGEQGRMLFGRL 450
Cdd:PRK11650 80 mvfqnyalyPHMSVRENMAYGLK-----IRGM------PKAEIEERVAeaarileleplldrkprELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 451 ILKRPNVLVMDEPTNHLD------ME-SIEALNLALDNypgTLIFVSHDREFVSSLATRII 504
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDaklrvqMRlEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVV 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
322-510 |
1.60e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.40 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-VGDLPvDGGEVKWTDSAdvgyfaqdhaddfaddms 400
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETP-DSGQLNIAGHQ------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 401 lFDWMAQWTQGGEQLVRGTLGrMLFSN-----------DEIKKSVKV-------------------------------IS 438
Cdd:COG4161 66 -FDFSQKPSEKAIRLLRQKVG-MVFQQynlwphltvmeNLIEAPCKVlglskeqarekamkllarlrltdkadrfplhLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 439 GGEQGRMLFGRLILKRPNVLVMDEPTNHLDME---SIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM-EKG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
1.62e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNdLEPSA---GQVMLEpnvrlGKLRQDQfayedfSVI 82
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFE-----GEELQAS------NIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DT-----VIMgHEELWAVkaerdriyslPEMSEADGMAVAELEVQFAEFDGYTAESRAGELL--LGLGIPLEQhfgPMSA 155
Cdd:PRK13549 78 DTeragiAII-HQELALV----------KELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqLKLDINPAT---PVGN 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 156 VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDrhfLNSV 218
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISHK---LNEV 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-187 |
1.80e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 54.95 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV--------MLEPNVR-LGKLRQDqfay 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRdIAMVFQN---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 edfsvidtvimgheelwavkaerdriYSL-PEMSEADGMAVAeLEVQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSA 155
Cdd:cd03301 81 --------------------------YALyPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSG 133
|
170 180 190
....*....|....*....|....*....|..
gi 489202159 156 vapGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:cd03301 134 ---GQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
320-504 |
1.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.76 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--KWTDSAD----------VGY 386
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvSGIDTGDfsklqgirklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDHADDFA-----DDMSLfdwmaqwtqGGEQL------VRGTLGRMLfsnDEIK------KSVKVISGGEQGRMLFGR 449
Cdd:PRK13644 82 VFQNPETQFVgrtveEDLAF---------GPENLclppieIRKRVDRAL---AEIGlekyrhRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 450 LILKRPNVLVMDEPTNHLDMESIEAL--NLALDNYPG-TLIFVSHDREFVSSlATRII 504
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVleRIKKLHEKGkTIVYITHNLEELHD-ADRII 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-491 |
2.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.30 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 317 RQAVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL------------VGDLPVDGGEVKWTDSADV 384
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlielypearvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 385 GYFAQD--HADDFADDMSLFDWMA---------QWTQGGEQLVRGTLGRMLFSnDEIKKSVKV----ISGGEQGRMLFGR 449
Cdd:PRK14247 81 RRRVQMvfQIPNPIPNLSIFENVAlglklnrlvKSKKELQERVRWALEKAQLW-DEVKDRLDApagkLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 450 LILKRPNVLVMDEPTNHLDMES---IEALNLALDNyPGTLIFVSH 491
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-500 |
2.11e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 317 RQAVTVENISKGY---DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtdSADVGYFAQD--- 390
Cdd:PRK14246 5 KSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--DGKVLYFGKDifq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 ---------------HADDFADdMSLFDWMA------------QWTQGGEQLVRgTLGRMLFSNDEIKKSVKVISGGEQG 443
Cdd:PRK14246 83 idaiklrkevgmvfqQPNPFPH-LSIYDNIAyplkshgikekrEIKKIVEECLR-KVGLWKEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 444 RMLFGRLILKRPNVLVMDEPTNHLDM---ESIEALNLALDNyPGTLIFVSHDREFVSSLA 500
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVA 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
311-492 |
2.41e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 311 QYKKLHRQAV-TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDS 381
Cdd:PRK10575 2 QEYTNHSDTTfALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 382 A---DVGYFAQDHADdfADDMSLFDWMAQwtqgGEQLVRGTLGRMLFSNDE--------------IKKSVKVISGGEQGR 444
Cdd:PRK10575 82 AfarKVAYLPQQLPA--AEGMTVRELVAI----GRYPWHGALGRFGAADREkveeaislvglkplAHRLVDSLSGGERQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 445 MLFGRLILKRPNVLVMDEPTNHLDM-ESIEALNLA--LDNYPG-TLIFVSHD 492
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLALVhrLSQERGlTVIAVLHD 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-212 |
2.57e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPnvrlgklrqdqfayEDfsVIDTV 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG--------------ED--VTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 86 IMgheelwavkaERD-----RIYSL-PEMSEAD--GMAVAELEVQFAEFDGYTAESRAGELLLGLgiplEQHFgpMSAVA 157
Cdd:PRK11432 75 IQ----------QRDicmvfQSYALfPHMSLGEnvGYGLKMLGVPKEERKQRVKEALELVDLAGF----EDRY--VDQIS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 158 PGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN-------TIRWLEGVLtarNSTMIIISHDR 212
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsmreKIRELQQQF---NITSLYVTHDQ 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
2.77e-08 |
|
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: 54.55 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGKLRQDQFAYEdfSV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-----GKDITNLPPHK--RP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 IDTVIMGheelwavkaerdriYSL-PEMSEADGMAVAeleVQFAEFDGYTAESRAGElLLGLgIPLEQHFGPM-SAVAPG 159
Cdd:cd03300 74 VNTVFQN--------------YALfPHLTVFENIAFG---LRLKKLPKAEIKERVAE-ALDL-VQLEGYANRKpSQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEgvLTARN------STMIIISHD 211
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ--LELKRlqkelgITFVFVTHD 190
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-508 |
2.85e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNdLEPS---------AGQVMLEPNVR------LGKLR 70
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwdgeiywSGSPLKASNIRdteragIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 QDQFAYEDFSVIDTVIMGHEelwavkaerdriYSLPEMSEADGMAVAelevqfaefdgytaesRAGELLLGLGIPLEQHF 150
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNE------------ITLPGGRMAYNAMYL----------------RAKNLLRELQLDADNVT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 151 GPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSVCTHMADLDY 227
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 228 GElrlfpgnydeymTAAEQARERLLSDNAKKKAQIAELQSFVSRfsaNASKAKQATSRARQIdkiqleevkpssrvspfi 307
Cdd:TIGR02633 217 GQ------------HVATKDMSTMSEDDIITMMVGREITSLYPH---EPHEIGDVILEARNL------------------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 308 rfEQYKKLHRQAVTVENIskgydgkplfkglSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP--------VDGGEVKWT 379
Cdd:TIGR02633 264 --TCWDVINPHRKRVDDV-------------SFSLRRGEILGVAGLVGAGRTELVQALFGAYPgkfegnvfINGKPVDIR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 380 DSAD-----VGYFAQDHA-DDFADDMSL-----------FDWMAQWTQGGE-QLVRGTLGRMLFSNDEIKKSVKVISGGE 441
Cdd:TIGR02633 329 NPAQairagIAMVPEDRKrHGIVPILGVgknitlsvlksFCFKMRIDAAAElQIIGSAIQRLKVKTASPFLPIGRLSGGN 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 442 QGRMLFGRLILKRPNVLVMDEPTNHLDMES---IEALNLALDNYPGTLIFVSHDREFVSSLATRIIELGE 508
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-503 |
3.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 323 ENISKGYDG-KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA-----------DVGYFAQD 390
Cdd:PRK13652 7 RDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenirevrkFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 HADDFADDMSLFDW------MAQWTQGGEQLVRGTLgRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:PRK13652 87 PDDQIFSPTVEQDIafgpinLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489202159 465 NHLDMESIEALNLALDNYPG----TLIFVSHDREFVSSLATRI 503
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYI 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
3.53e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF-GAKPLFE---NVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVMLEpNVRLGKLRQDQFA 75
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLErPTSGRVLVD-GQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 YEDFSVidTVIMGHEELWAVKAERDRIySLPemSEADGMAVAELEvqfaefdgytaeSRAGELLLGLGIPLEQHFGPmSA 155
Cdd:PRK11153 79 KARRQI--GMIFQHFNLLSSRTVFDNV-ALP--LELAGTPKAEIK------------ARVTELLELVGLSDKADRYP-AQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 156 VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNS----TMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
3.71e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 19 NVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVmlepnvrlgklrqdqfayedfSVIDTVIMGHEELWAVKAE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV---------------------TVDDITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 99 RDRI---YSLPEMSEADGMAVAELEVQFAEF--DGYTAESRAGELLLGLGIP---LEQHFGPMSAvapGWKLRVLLAQAL 170
Cdd:PRK13646 84 RKRIgmvFQFPESQLFEDTVEREIIFGPKNFkmNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMSG---GQMRKIAIVSIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489202159 171 FSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHD 211
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
4.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLEPSAGQVMLEPNVRLGKlrQDQFAYEDfsv 81
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDKVSGYRYSGDVLLGG--RSIFNYRD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtvIMGHEELWAVKAERDRIYSLPEMSEADGMAVAELEVQFAEFDGyTAESRAGELLLGLGIPLEQHFGPMSaVAPGWK 161
Cdd:PRK14271 96 ----VLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLT--ARNSTMIIISHD 211
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRslADRLTVIIVTHN 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-210 |
4.55e-08 |
|
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: 53.57 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAK--PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRqdqfa 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidiSTIPLEDLR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 yEDFSVI---DTVIMGheelwAVKAERDRiyslpemseadgmavaelevqfaeFDGYTAESRAGEL-LLGLGIPLEQhfg 151
Cdd:cd03369 82 -SSLTIIpqdPTLFSG-----TIRSNLDP------------------------FDEYSDEEIYGALrVSEGGLNLSQ--- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 152 pmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISH 210
Cdd:cd03369 129 -------GQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIreEFTNSTILTIAH 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-378 |
5.89e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 5.89e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW 378
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL 63
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
6.62e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.92 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML--EPnvrLGKL-RQDQFAYEDfsviDTVIMG 88
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgEP---LAKLnRAQRKAFRR----DIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 89 HEELWAVKAERD--RIYSLP-----EMSEADGMAvaelevqfaefdgytaesRAGELLLGLGIPLEqHFGPMSAVAPGWK 161
Cdd:PRK10419 96 QDSISAVNPRKTvrEIIREPlrhllSLDKAERLA------------------RASEMLRAVDLDDS-VLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 162 L-RVLLAQALFSDPDVLLLDEPTNHLDI----NTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10419 157 LqRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-504 |
7.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGK-PL----FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHADD 394
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 395 FADDMSLfdwmaQWT-------------------QGGE-QLVRGTLGR--------MLFSNDEIKKSVKVI--------- 437
Cdd:PRK13651 83 VLEKLVI-----QKTrfkkikkikeirrrvgvvfQFAEyQLFEQTIEKdiifgpvsMGVSKEEAKKRAAKYielvgldes 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 438 ---------SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDME-SIEALNL--ALDNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK13651 158 ylqrspfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIfdNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-231 |
7.30e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 32 LIGANGCGKSTFMKILGNDLEPSAGQVML--EPNVRL-----GKLRQDQ--FAYEDFSVIDTV-IMGHEELWA-VKAERD 100
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLvgQPLHQMdeearAKLRAKHvgFVFQSFMLIPTLnALENVELPAlLRGESS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 101 RiyslpemseadgmavaelevqfaefdgyTAESRAGELL--LGLGIPLEQHFGPMSAvapGWKLRVLLAQALFSDPDVLL 178
Cdd:PRK10584 121 R----------------------------QSRNGAKALLeqLGLGKRLDHLPAQLSG---GEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 179 LDEPTNHLDINTIRWLEGVLTARN----STMIIISHDRHfLNSVCTHMADLDYGELR 231
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHDLQ-LAARCDRRLRLVNGQLQ 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
320-365 |
7.37e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.31 E-value: 7.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489202159 320 VTVENISKGYDGKP-----LfKGLSLQVEAGERVAIIGPNGIGKTTLLRCL 365
Cdd:COG1135 2 IELENLSKTFPTKGgpvtaL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCI 51
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-506 |
7.85e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 53.24 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 336 KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLPVDGGEVkwTDSADVGYFAQDHADDFaDDMSLFDWMAQW------ 408
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVI--LEGKQITEPGPDRMVVF-QNYSLLPWLTVReniala 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 409 ---------TQGGEQLVRGTLgRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEAL---- 475
Cdd:TIGR01184 79 vdrvlpdlsKSERRAIVEEHI-ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqeel 157
|
170 180 190
....*....|....*....|....*....|..
gi 489202159 476 -NLALDNYPgTLIFVSHDREFVSSLATRIIEL 506
Cdd:TIGR01184 158 mQIWEEHRV-TVLMVTHDVDEALLLSDRVVML 188
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
334-502 |
8.01e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 334 LFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDSADVGYFAQDHADDFADDMSLFDWM 405
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 406 AQWTQGGEQLVRG-----------TLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM---ES 471
Cdd:PRK10584 105 ALENVELPALLRGessrqsrngakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDK 184
|
170 180 190
....*....|....*....|....*....|..
gi 489202159 472 IEALNLALD-NYPGTLIFVSHDrefvSSLATR 502
Cdd:PRK10584 185 IADLLFSLNrEHGTTLILVTHD----LQLAAR 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-231 |
9.08e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 13 AKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPN---VRLGKLRQDQFAYEDFSVIDTVIMGH 89
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 90 EELWAVKAERdriyslpemseadGMAVAELEvqfaEFDGYTAESragellLGLGIPLEQHFGPMSAvapGWKLRVLLAQA 169
Cdd:TIGR01257 2031 EHLYLYARLR-------------GVPAEEIE----KVANWSIQS------LGLSLYADRLAGTYSG---GNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489202159 170 LFSDPDVLLLDEPTNHLDINTIRWLEGVLTA---RNSTMIIISHDRHFLNSVCTHMADLDYGELR 231
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiirEGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
320-508 |
9.19e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADV--------------- 384
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVtlngeplaaidaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 385 ----GYFAQDHADDF---ADDMSLFDWMAQWTQGGEQLVR--GTLGRMLFSNDE---IKKSVKVISGGEQGRMLFGRLIL 452
Cdd:PRK13547 82 arlrAVLPQAAQPAFafsAREIVLLGRYPHARRAGALTHRdgEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 453 K---------RPNVLVMDEPTNHLDMESIEAL-----NLALDNYPGTLIFVsHDREFVSSLATRIIELGE 508
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRIAMLAD 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-503 |
9.53e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF----GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVRLGKLRQdqfay 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 edfsVIDTVIMGHEELWAVK-AERDRIYSLPEMSEADGMAVAElevQFAE-------FDGYTAESRAGELLLGLGIPLEQ 148
Cdd:PRK10261 87 ----VIELSEQSAAQMRHVRgADMAMIFQEPMTSLNPVFTVGE---QIAEsirlhqgASREEAMVEAKRMLDQVRIPEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 149 hfgPMSAVAP-----GWKLRVLLAQALFSDPDVLLLDEPTNHLDIN---TIRWLEGVLTARNST-MIIISHDRHFLNSVC 219
Cdd:PRK10261 160 ---TILSRYPhqlsgGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMgVIFITHDMGVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 220 THMADLDYGEL-------RLFPGNYDEYMTAAEQARERLLSDNAkkkaqiaelQSFVSRFSANAskAKQATSRARQIDKI 292
Cdd:PRK10261 237 DRVLVMYQGEAvetgsveQIFHAPQHPYTRALLAAVPQLGAMKG---------LDYPRRFPLIS--LEHPAKQEPPIEQD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 293 QLEEVKPSSRVSPFI-RFEQ----YKKLHRQAVTVENISkgYDGKPlfkglslqveaGERVAIIGPNGIGKTTLLRCLVG 367
Cdd:PRK10261 306 TVVDGEPILQVRNLVtRFPLrsglLNRVTREVHAVEKVS--FDLWP-----------GETLSLVGESGSGKSTTGRALLR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 368 DLPVDGGEVKW--------TDSA------DVGYFAQDHADDFADDMSLFDWMAQ------WTQGGEQLVRGT--LGRMLF 425
Cdd:PRK10261 373 LVESQGGEIIFngqridtlSPGKlqalrrDIQFIFQDPYASLDPRQTVGDSIMEplrvhgLLPGKAAAARVAwlLERVGL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 426 SNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEA--LNLALD---NYPGTLIFVSHDREFVSSLA 500
Cdd:PRK10261 453 LPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDlqrDFGIAYLFISHDMAVVERIS 531
|
...
gi 489202159 501 TRI 503
Cdd:PRK10261 532 HRV 534
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-504 |
1.03e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.90 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYD-GKPLFK---GLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP---VDGGEVKWtDSADVGYFAQDHA 392
Cdd:COG0444 2 LEVRNLKVYFPtRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILF-DGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 393 DDF-ADDMSL-FdwmaqwtQG-----------GEQLVRGTLGRMLFSNDEIKKsvKVI---------------------- 437
Cdd:COG0444 81 RKIrGREIQMiF-------QDpmtslnpvmtvGDQIAEPLRIHGGLSKAEARE--RAIellervglpdperrldryphel 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 438 SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEA--LNLALD---NYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLNLLKDlqrELGLAILFITHDLGVVAEIADRVA 222
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
320-376 |
1.18e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 1.18e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG--DLPVDGGEV 376
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTV 60
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-295 |
1.19e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 10 QFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNvrlgklrqdqFAYEDfsvidtvimgh 89
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS----------IAYVP----------- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 90 EELWAVKAE-RDRIYSLPEMSEA---DGMAVAELEVQFAEFDGyTAESRAGElllgLGIPLeqhfgpmsavAPGWKLRVL 165
Cdd:PTZ00243 728 QQAWIMNATvRGNILFFDEEDAArlaDAVRVSQLEADLAQLGG-GLETEIGE----KGVNL----------SGGQKARVS 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 166 LAQALFSDPDVLLLDEPTNHLDINT-IRWLEGVLTAR--NSTMIIISHDRHFLnSVCTHMADLDYGELRlFPGNYDEYM- 241
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGAlaGKTRVLATHQVHVV-PRADYVVALGDGRVE-FSGSSADFMr 870
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 242 -----TAAEQARERLLSDNAKKKAQIAELQSFVSRFSANASKAKQATSRARQIDKIQLE 295
Cdd:PTZ00243 871 tslyaTLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALD 929
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
1.27e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.54 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 17 FENVSVKFGNGNR-----------------YGLIGANGCGKSTFMKILgNDLE-PSAGQVMLEpNVRLGKLRQdqfayed 78
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCI-NLLErPTSGSVLVD-GVDLTALSE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 fsvidtvimghEELWAVkaeRDRIyslpemseadGMA-----------VAE-----LEVqfAEFDGYTAESRAGELL--L 140
Cdd:COG1135 75 -----------RELRAA---RRKI----------GMIfqhfnllssrtVAEnvalpLEI--AGVPKAEIRKRVAELLelV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 141 GLGiPLEQHFgPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRwleGVLT--AR-----NSTMIIISHDRH 213
Cdd:COG1135 129 GLS-DKADAY-P-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR---SILDllKDinrelGLTIVLITHEMD 202
|
250
....*....|....*..
gi 489202159 214 FLNSVCTHMADLDYGEL 230
Cdd:COG1135 203 VVRRICDRVAVLENGRI 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-492 |
1.32e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 342 VEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAD--VGYFA----QDHADDFAD-DMSlfdwMAQWTQGGEQ 414
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDevLKRFRgtelQNYFKKLYNgEIK----VVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 415 L---VRGTLGRMLFSNDE----------------IKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM-ESIEA 474
Cdd:PRK13409 172 IpkvFKGKVRELLKKVDErgkldevverlgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrQRLNV 251
|
170 180
....*....|....*....|..
gi 489202159 475 LN----LALDNYpgtLIFVSHD 492
Cdd:PRK13409 252 ARlireLAEGKY---VLVVEHD 270
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-230 |
1.39e-07 |
|
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: 52.27 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 16 LFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGNDLEPSA--GQVMLEPNVRLGKLRQDQFAY----EDFSVIDTVimg 88
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGTtsGQILFNGQPRKPDQFQKCVAYvrqdDILLPGLTV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 89 hEELWAVKAerdrIYSLPE-MSEADGMAVAELEVQfaefdGYTAESRAGELLlglgipleqhfgpMSAVAPGWKLRVLLA 167
Cdd:cd03234 99 -RETLTYTA----ILRLPRkSSDAIRKKRVEDVLL-----RDLALTRIGGNL-------------VKGISGGERRRVSIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 168 QALFSDPDVLLLDEPTNHLD----INTIRWLEGvLTARNSTMIIISHD-RHFLNSVCTHMADLDYGEL 230
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQ-LARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
337-503 |
1.64e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 337 GLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQDHAD-----DFaDDMSLFDWM------ 405
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmgvvrTF-QHVRLFREMtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 406 --AQWTQGGEQLVRGTLGRMLFSNDEIK-------------------KSVKVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:PRK11300 102 lvAQHQQLKTGLFSGLLKTPAFRRAESEaldraatwlervgllehanRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489202159 465 NHLDMESIEALNLALDN----YPGTLIFVSHDREFVSSLATRI 503
Cdd:PRK11300 182 AGLNPKETKELDELIAElrneHNVTVLLIEHDMKLVMGISDRI 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
145-217 |
1.96e-07 |
|
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: 51.45 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 145 PLEQHFGPMSA---VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRW-----LEGVLTARNSTMIIISHDRHFLN 216
Cdd:cd03240 108 PLLDMRGRCSGgekVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
.
gi 489202159 217 S 217
Cdd:cd03240 188 A 188
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
1.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 11 FGAKPLFEnVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGqvmlepNVRLGklrqdqfayedfSVIDTVIMGHE 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG------KVTVG------------DIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 91 ELWAVKAERDRIYSLPEMSEADGMAVAELEVQFAEF--DGYTAESRAGELLLGLGIPLEQHFGPMSAVAPGWKLRVLLAQ 168
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489202159 169 ALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTArNSTMIIISH 210
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS-GQTVVLVTH 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-228 |
2.08e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 51.34 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 4 TANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNvrlgklrqdqfayedfsvid 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 tvimgheelwAVKAERDRIY-SLPEMSEADGM--AVAELE-VQFAEFDGYTAESRAGELLLGLGIPLEQHFGPMSAvapG 159
Cdd:cd03231 63 ----------PLDFQRDSIArGLLYLGHAPGIktTLSVLEnLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSA---G 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL---TARNSTMIIISHdrHFLNSVCTHMADLDYG 228
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTH--QDLGLSEAGARELDLG 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-468 |
2.79e-07 |
|
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: 53.76 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV------GDLPVDGgeVKWtdsadvgyfaqdh 391
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQIDG--VSW------------- 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 addfaDDMSLFDWMAQWTQGGEQ--LVRGTLGRML-----FSNDEIKKSVK------------------------VISGG 440
Cdd:TIGR01271 1283 -----NSVTLQTWRKAFGVIPQKvfIFSGTFRKNLdpyeqWSDEEIWKVAEevglksvieqfpdkldfvlvdggyVLSNG 1357
|
170 180
....*....|....*....|....*...
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
322-508 |
3.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKP---LFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDG----GEVKWTDSADVGYF 387
Cdd:PRK13642 7 VENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIdglfeefEGKVKIDGelltAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 388 AQDHADDFA-----DDMSLfdWMAQWTQGGEQLVRGTLGRMLFSN--DEIKKSVKVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:PRK13642 87 FQNPDNQFVgatveDDVAF--GMENQGIPREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489202159 461 DEPTNHLD----MESIEALNLALDNYPGTLIFVSHD-REFVSSLATRIIELGE 508
Cdd:PRK13642 165 DESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDlDEAASSDRILVMKAGE 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-210 |
3.28e-07 |
|
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: 51.39 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 15 PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRqDQFAY---E----DFSVID 83
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLR-SQIGLvsqEpvlfDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 TVIMGHEELWAVKAER--------DRIYSLPemseadgmavaelevqfaefDGYtaESRAGE---LLLGlgipleqhfgp 152
Cdd:cd03249 96 NIRYGKPDATDEEVEEaakkanihDFIMSLP--------------------DGY--DTLVGErgsQLSG----------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 153 msavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISH 210
Cdd:cd03249 143 ------GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALdrAMKGRTTIVIAH 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
3.94e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.94 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEP---SAGQVMLEPNV---------RLGK 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltalpaeqrRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 69 LRQDQFAYEDFSVIDTVIMGHEELWAVKAERDRIYSLPEMSEADGMA---VAELevqfaefdgytaesrAGelllglgip 145
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFAdrdPATL---------------SG--------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 146 leqhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIISHD 211
Cdd:COG4136 137 -------------GQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
4.93e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.93 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILG--NDLEPSA---------GQVMLEPNVRLGKL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitgsivynGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQD------QFAYEDFSVIDTVIMGHEelwaVKAERDRiYSLPEMSEAD--GMAVAElEVQfaefdgytaeSRAGELLLG 141
Cdd:PRK14239 85 RKEigmvfqQPNPFPMSIYENVVYGLR----LKGIKDK-QVLDEAVEKSlkGASIWD-EVK----------DRLHDSALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 142 LgipleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRWLEGVLTARNS-TMIIISH 210
Cdd:PRK14239 149 L--------------SGGQQQRVCIARVLATSPKIILLDEPTSALDpISAGKIEETLLGLKDDyTMLLVTR 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-210 |
5.33e-07 |
|
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: 50.69 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPN----VRLGKLR-------QDQFAYEDfSVI 82
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdISRKSLRsmigvvlQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 83 DTVIMGHEElwavkAERDRIyslpemseadgmAVAELEVQFAEF-----DGY-TAESRAGELLlglgipleqhfgpmSAv 156
Cdd:cd03254 95 ENIRLGRPN-----ATDEEV------------IEAAKEAGAHDFimklpNGYdTVLGENGGNL--------------SQ- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 157 apGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISH 210
Cdd:cd03254 143 --GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-249 |
5.45e-07 |
|
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: 50.62 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKST-FMKILGndLE-PSAGQVMLEpNVRLGKLRQDQFAyedf 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTtFYMIVG--LVkPDSGKILLD-GQDITKLPMHKRA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 svidtvimgheelwavkaeRDRIYSLP-EMSEADGMAVAE---LEVQFAEFDGYTAESRAGELLLGLGI-PLEQHFGpmS 154
Cdd:cd03218 74 -------------------RLGIGYLPqEASIFRKLTVEEnilAVLEIRGLSKKEREEKLEELLEEFHItHLRKSKA--S 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 155 AVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD---INTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELr 231
Cdd:cd03218 133 SLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV- 211
|
250
....*....|....*...
gi 489202159 232 LFPGNYDEyMTAAEQARE 249
Cdd:cd03218 212 LAEGTPEE-IAANELVRK 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-510 |
6.51e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY-DGKPLFKgLSLQVEAGERVAIIGPNGIGKTTLLRCL-VGDLPvDGGEVKwtdsadvgyFAQDHaddfa 396
Cdd:PRK11124 2 SIQLNGINCFYgAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMP-RSGTLN---------IAGNH----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ddmslFDWMAQWTQGGEQLVRGTLGrMLF-------------------------SNDEIKKSVKVI-------------- 437
Cdd:PRK11124 66 -----FDFSKTPSDKAIRELRRNVG-MVFqqynlwphltvqqnlieapcrvlglSKDQALARAEKLlerlrlkpyadrfp 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 438 ---SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDME---SIEALNLALDNYPGTLIFVSHDREFVSSLATRIIELgENG 510
Cdd:PRK11124 140 lhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYM-ENG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
332-491 |
7.88e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 332 KPLFKGLSLQVEAGERVAIIGPNGIGKTT---LLR-----------------------------CLVGDLPVD-GGEVK- 377
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQnlyqptggqvlldgvplvqydhhylhrqvALVGQEPVLfSGSVRe 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 378 -------WTDSADVGYFAQD-HADDFADDMslfdwmaqwTQGgeqlvrgtlgrmlfSNDEIKKSVKVISGGEQGRMLFGR 449
Cdd:TIGR00958 574 niaygltDTPDEEIMAAAKAaNAHDFIMEF---------PNG--------------YDTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489202159 450 LILKRPNVLVMDEPTNHLDMESIEALNLALDNYPGTLIFVSH 491
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-228 |
8.19e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLE-PSAGQVML---------EPNVRLG-KLR 70
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIagnhfdfskTPSDKAIrELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 QDqfayedfsvidtVIMGHEE--LWavkaerdriyslPEMSEADGMAVAELEVqfAEFDGYTAESRAGELLLGLgiPLEQ 148
Cdd:PRK11124 82 RN------------VGMVFQQynLW------------PHLTVQQNLIEAPCRV--LGLSKDQALARAEKLLERL--RLKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 149 HFG--PMSaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRWLEGVltarNSTMIIISHDRHFLNSVC 219
Cdd:PRK11124 134 YADrfPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAET----GITQVIVTHEVEVARKTA 208
|
....*....
gi 489202159 220 THMADLDYG 228
Cdd:PRK11124 209 SRVVYMENG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
320-464 |
8.27e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYF--AQDHADDFA- 396
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-DGKDITDWqtAKIMREAVAi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 --------------DDMSLFDWMAQWTQGGEQLVR--GTLGRMLfsnDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVM 460
Cdd:PRK11614 85 vpegrrvfsrmtveENLAMGGFFAERDQFQERIKWvyELFPRLH---ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
....
gi 489202159 461 DEPT 464
Cdd:PRK11614 162 DEPS 165
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
313-377 |
8.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 8.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 313 KKLHRQAVTVENISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK 377
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
321-381 |
8.54e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 8.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 321 TVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG--DLPVDGGEVKWTDS 381
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE 71
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
343-468 |
9.03e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 343 EAGERVAIIGPNGIGKTTLLRCLVGDL-PVDG---GEVKWTDSADvgYFA----QDHADDFAD-DMSlfdwMAQWTQGGE 413
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkPNLGdydEEPSWDEVLK--RFRgtelQDYFKKLANgEIK----VAHKPQYVD 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 414 QL---VRGTLGRMLFSNDE----------------IKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:COG1245 171 LIpkvFKGTVRELLEKVDErgkldelaeklgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-491 |
9.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRC------LVGDLPVDG-----GEVKWTDSAD---- 383
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEGevrlfGRNIYSPDVDpiev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 ---VGYFAQdHADDFADdMSLFDWMA------QWTQGGEQL---VRGTLGRMLFSnDEIKKSVK----VISGGEQGRMLF 447
Cdd:PRK14267 84 rreVGMVFQ-YPNPFPH-LTIYDNVAigvklnGLVKSKKELderVEWALKKAALW-DEVKDRLNdypsNLSGGQRQRLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489202159 448 GRLILKRPNVLVMDEPTNHLD---MESIEALNLAL-DNYpgTLIFVSH 491
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELkKEY--TIVLVTH 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-511 |
9.78e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.62 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 330 DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV----KWTDSA---------DVGYFAQDhaddfa 396
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgKPIDYSrkglmklreSVGMVFQD------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 DDMSLFDWMAQwtqggEQLVRGTLGrMLFSNDEIKKSVK-----------------VISGGEQGRMLFGRLILKRPNVLV 459
Cdd:PRK13636 91 PDNQLFSASVY-----QDVSFGAVN-LKLPEDEVRKRVDnalkrtgiehlkdkpthCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 460 MDEPTNHLDMESI-EALNLALDNYPG---TLIFVSHDREFVSSLATRIIELGENGV 511
Cdd:PRK13636 165 LDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-187 |
1.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF-GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgkLRQDQFAYEDF 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL---------IRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 SVIDTVIMgheelWAVKAERDRIYSlpemseadgmAVAELEVQFAE----FDGYTAESRAGELLLGLGIPLEQHFGPMSa 155
Cdd:PRK13652 74 REVRKFVG-----LVFQNPDDQIFS----------PTVEQDIAFGPinlgLDEETVAHRVSSALHMLGLEELRDRVPHH- 137
|
170 180 190
....*....|....*....|....*....|..
gi 489202159 156 VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-210 |
1.26e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILG--NDLEPSA---GQVMLE------PNVRLGKLR 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmNDLIPGArveGEILLDgediydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 71 QD-----Q----FAyedFSVIDTVIMG---HEelWAVKAERDRI--YSLPEmseadgmavAEL--EVQfaefDgytaesR 134
Cdd:COG1117 92 RRvgmvfQkpnpFP---KSIYDNVAYGlrlHG--IKSKSELDEIveESLRK---------AALwdEVK----D------R 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 135 AGELLLGLgipleqhfgpmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRwLEGVLT--ARNSTMIIISH 210
Cdd:COG1117 148 LKKSALGL--------------SGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILelKKDYTIVIVTH 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
320-480 |
1.31e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.17 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGK--PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkWTDSADV-GYFAQDHADDFA 396
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDGHDLrDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 397 ---DDMSLF-DWMA---------QWTQggEQLVRGtlGRMLFSNDEIKKSVK----VI-------SGGEQGRMLFGRLIL 452
Cdd:PRK11176 421 lvsQNVHLFnDTIAnniayarteQYSR--EQIEEA--ARMAYAMDFINKMDNgldtVIgengvllSGGQRQRIAIARALL 496
|
170 180
....*....|....*....|....*...
gi 489202159 453 KRPNVLVMDEPTNHLDMESIEALNLALD 480
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALD 524
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
332-504 |
1.40e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 332 KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVkwtdsadvgyfaqdhaddFADDMSLFDWMAQWTqg 411
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV------------------YVDGLDTSDEENLWD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 412 geqlVRGTLGrMLFSN-------------------------DEIKKSVK-----------------VISGGEQGRMLFGR 449
Cdd:PRK13633 83 ----IRNKAG-MVFQNpdnqivativeedvafgpenlgippEEIRERVDeslkkvgmyeyrrhaphLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 450 LILKRPNVLVMDEPTNHLD-------MESIEALNlalDNYPGTLIFVSHDREFVSSlATRII 504
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDpsgrrevVNTIKELN---KKYGITIILITHYMEEAVE-ADRII 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
131-504 |
1.79e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.45 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 131 AESRAGELLLGLGIP-LEQHFG--P--MSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDInTIR-----WLEGVLTA 200
Cdd:COG4172 130 ARARALELLERVGIPdPERRLDayPhqLSG---GQRQRVMIAMALANEPDLLIADEPTTALDV-TVQaqildLLKDLQRE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 201 RNSTMIIISHDrhfLNSVcTHMAD----LDYGELRlfpgnydeymtaaEQARerllsdnakkKAQIaelqsfvsrFSAna 276
Cdd:COG4172 206 LGMALLLITHD---LGVV-RRFADrvavMRQGEIV-------------EQGP----------TAEL---------FAA-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 277 skAKQATSRarqidkiQLEEVKPSSRVSPfirfeqykkLHRQA---VTVENISKGYDGKP-LF----------KGLSLQV 342
Cdd:COG4172 248 --PQHPYTR-------KLLAAEPRGDPRP---------VPPDApplLEARDLKVWFPIKRgLFrrtvghvkavDGVSLTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 343 EAGERVAIIGPNGIGKTTLLRCLVGDLPvDGGEVKWtDSADVgyfaqdHADDFADDMSLFDWMaqwtqggeQLV------ 416
Cdd:COG4172 310 RRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF-DGQDL------DGLSRRALRPLRRRM--------QVVfqdpfg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 417 ----RGTLGR-----MLFSNDEIKKS---VKVI--------------------SGGEQGRMLFGR-LILKrPNVLVMDEP 463
Cdd:COG4172 374 slspRMTVGQiiaegLRVHGPGLSAAerrARVAealeevgldpaarhryphefSGGQRQRIAIARaLILE-PKLLVLDEP 452
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489202159 464 TNHLDMeSIEALNLAL-----DNYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG4172 453 TSALDV-SVQAQILDLlrdlqREHGLAYLFISHDLAVVRALAHRVM 497
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-508 |
1.90e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINT-------IRWLEGVLtarNSTMIIISHDrhfLNSVcthmadldygelr 231
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVqaqilqlLRELQQEL---NMGLLFITHN---LSIV------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 232 lfpgnydeymtaaeqareRLLSDNAK--KKAQIAELQSFVSRFSANASKAKQatsrarqidkiQLEEVKPSSRVSPfirf 309
Cdd:PRK15134 221 ------------------RKLADRVAvmQNGRCVEQNRAATLFSAPTHPYTQ-----------KLLNSEPSGDPVP---- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 310 eqykkLHRQAVT---VENISKGY-----------DGKPLFKGLSLQVEAGERVAIIGPNGIGKTT----LLRCLV--GDL 369
Cdd:PRK15134 268 -----LPEPASPlldVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 370 PVDGGEV-KWTDSADVGYFAQDHADdFADDMSLFD---WMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKV--------- 436
Cdd:PRK15134 343 WFDGQPLhNLNRRQLLPVRHRIQVV-FQDPNSSLNprlNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVgldpetrhr 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 437 ----ISGGEQGRMLFGR-LILKrPNVLVMDEPTNHLDmESIEALNLAL-----DNYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK15134 422 ypaeFSGGQRQRIAIARaLILK-PSLIILDEPTSSLD-KTVQAQILALlkslqQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
....
gi 489202159 507 --GE 508
Cdd:PRK15134 500 rqGE 503
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-230 |
2.25e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPnvrlgklrqdqfayedfsvIDTVIMGHEELWAVKA 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 98 ER-----DRIYSLPEMSEADGMAVAelevqfAEFDGYTAESRAGELLLGL-GIPLEQH-FGPMSAVAPGWKLRVLLAQAL 170
Cdd:PRK10070 106 KKiamvfQSFALMPHMTVLDNTAFG------MELAGINAEERREKALDALrQVGLENYaHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489202159 171 FSDPDVLLLDEPTNHLD--INTIRWLEGV-LTARNS-TMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10070 180 AINPDILLMDEAFSALDplIRTEMQDELVkLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
2.60e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.22 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGA--KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNV----RLGKLRQ--- 71
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskeNLKEIRKkig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 -------DQFAyeDFSVIDTVIMGHEelwavkaerDRIYSLPEMSEAdgmavaelevqfaeFDGYTAESRAGELLlglgi 144
Cdd:PRK13632 87 iifqnpdNQFI--GATVEDDIAFGLE---------NKKVPPKKMKDI--------------IDDLAKKVGMEDYL----- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 145 PLEQHFgpmsaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD----------INTIRwlegvlTARNSTMIIISHD 211
Cdd:PRK13632 137 DKEPQN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreikkiMVDLR------KTRKKTLISITHD 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
3.01e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.30 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKIL-GndLE-PSAGQVMlepnvrlgklrqdqfayed 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIaG--LEdPTSGEIL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 fsvIDTVIMGHEELwavkAERDrI------YSL-PEMSEADGMAVAeLEVqfAEFDGYTAESRAGEL--LLGLGiPLEQH 149
Cdd:COG3839 62 ---IGGRDVTDLPP----KDRN-IamvfqsYALyPHMTVYENIAFP-LKL--RKVPKAEIDRRVREAaeLLGLE-DLLDR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 150 FgPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIISHD 211
Cdd:COG3839 130 K-P-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
332-468 |
3.06e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 332 KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV----------GDLPVDGGEV-KWTDSADVGYFAQD---------- 390
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkgvkgsGSVLLNGMPIdAKEMRAISAYVQQDdlfiptltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 391 -----HA-----------------DDFADDMSLFDwmAQwtqggeQLVRGTLGRMlfsndeikksvKVISGGEQGRMLFG 448
Cdd:TIGR00955 118 ehlmfQAhlrmprrvtkkekrervDEVLQALGLRK--CA------NTRIGVPGRV-----------KGLSGGERKRLAFA 178
|
170 180
....*....|....*....|
gi 489202159 449 RLILKRPNVLVMDEPTNHLD 468
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
3.56e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQF--GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVML------EPNV-----RLGK 68
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlsEETVwdvrrQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 69 LRQ---DQFAyeDFSVIDTVIMGHEElwaVKAERDriyslpEMSEADGMAVAELEVQfaEFDGYTAESRAGelllglgip 145
Cdd:PRK13635 86 VFQnpdNQFV--GATVQDDVAFGLEN---IGVPRE------EMVERVDQALRQVGME--DFLNREPHRLSG--------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 146 leqhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLD-------INTIRWLEgvlTARNSTMIIISHD 211
Cdd:PRK13635 144 -------------GQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLK---EQKGITVLSITHD 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-183 |
3.60e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgklrqdqFAYEDFS 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV--------------FDGKDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 VIDTVIMGHEELwAVKAERDRIYSlpEMSEADGMAVAELevqFAEFDGYTAE-SRAGELLLGLGIPLEQHFGPMSAvapG 159
Cdd:PRK11614 71 DWQTAKIMREAV-AIVPEGRRVFS--RMTVEENLAMGGF---FAERDQFQERiKWVYELFPRLHERRIQRAGTMSG---G 141
|
170 180
....*....|....*....|....
gi 489202159 160 WKLRVLLAQALFSDPDVLLLDEPT 183
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
3.67e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.31 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE-PNV-RL-GKLRQDQFAYED 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTDVsRLhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 F------SVIDTVIMGheelWAVKAERDRiyslPEMSEADGMAVAELE-VQFAEF-DGYTAESRAGElllglgipleqhf 150
Cdd:PRK10851 83 YalfrhmTVFDNIAFG----LTVLPRRER----PNAAAIKAKVTQLLEmVQLAHLaDRYPAQLSGGQ------------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 151 gpmsavapgwKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTMIIISHDR 212
Cdd:PRK10851 142 ----------KQRVALARALAVEPQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
4.51e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNvrlgklrqdQFAYEDFSvidtvimgheelwaVKA 97
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---------PLHFGDYS--------------YRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 98 ERDR-IYSLPEMSEADGMAVAE-LEVQF---AEFDGYTAESRAGELLLGLGI-PLEQHFGPmSAVAPGWKLRVLLAQALF 171
Cdd:PRK15112 87 QRIRmIFQDPSTSLNPRQRISQiLDFPLrlnTDLEPEQREKQIIETLRQVGLlPDHASYYP-HMLAPGQKQRLGLARALI 165
|
170
....*....|....*..
gi 489202159 172 SDPDVLLLDEPTNHLDI 188
Cdd:PRK15112 166 LRPKVIIADEALASLDM 182
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
5.38e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGN--DLEPSA---GQVMLE-------PNVRLGKL 69
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDgqdifkmDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 70 RQDQFAYED----FSVIDTVIMGHEELWAVKAERDRIYSLPEMSEAdgmavAEL--EVQfaefdgytaeSRAGelllglg 143
Cdd:PRK14247 84 VQMVFQIPNpipnLSIFENVALGLKLNRLVKSKKELQERVRWALEK-----AQLwdEVK----------DRLD------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 144 ipleqhfGPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD-INTIRWLEGVLT-ARNSTMIIISH 210
Cdd:PRK14247 142 -------APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpENTAKIESLFLElKKDMTIVLVTH 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-190 |
5.61e-06 |
|
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: 49.52 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 15 PLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV------------------MLEPNVRLGkLRQDQFAY 76
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgTIKDNIIFG-LSYDEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 EdfSVIDTVIMghEELWAVKAERDRIyslpemseadgmavaelevqfaefdgytaesrageLLLGLGIPLeqhfgpmsav 156
Cdd:TIGR01271 519 T--SVIKACQL--EEDIALFPEKDKT-----------------------------------VLGEGGITL---------- 549
|
170 180 190
....*....|....*....|....*....|....
gi 489202159 157 APGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT 190
Cdd:TIGR01271 550 SGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-468 |
6.21e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQF-GAKPLfENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVM-LEPNVRLGKLRQDQFAyeDFSVId 83
Cdd:PRK10762 9 GIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEA--GIGII- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 84 tvimgHEELwavkaerdriYSLPEMSEADGMAVA-ELEVQFAEFDGYTAESRAGELLLGLGIPLEQHfGPMSAVAPGWKL 162
Cdd:PRK10762 85 -----HQEL----------NLIPQLTIAENIFLGrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSD-KLVGELSIGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTNHL-DINT------IRWLEgvltARNSTMIIISHDRHFLNSVCTHMADLDYGELrlfpg 235
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTETeslfrvIRELK----SQGRGIVYISHRLKEIFEICDDVTVFRDGQF----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 236 nydeymtAAEQARERLLSDnakkkaQIAELqsFVSRfsanaskakqatsrarqidkiQLEEvkpssrvspfirfeQYKKL 315
Cdd:PRK10762 220 -------IAEREVADLTED------SLIEM--MVGR---------------------KLED--------------QYPRL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 316 HRQA----VTVENISKgydgkPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW------TDSADVG 385
Cdd:PRK10762 250 DKAPgevrLKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvTRSPQDG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 ------YFAQDHADD-------FADDMSLFDwMAQWTQGG-------EQLVRGTLGRmLFSndeIK-----KSVKVISGG 440
Cdd:PRK10762 325 langivYISEDRKRDglvlgmsVKENMSLTA-LRYFSRAGgslkhadEQQAVSDFIR-LFN---IKtpsmeQAIGLLSGG 399
|
490 500
....*....|....*....|....*...
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
342-511 |
6.82e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 342 VEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWtDSADVGYFAQdhaddfaddmslfdwmaqwtqggeqlvrgtlg 421
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ-------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 422 rmlfsndEIKksvkvISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDME----SIEALNLALDNYPGTLIFVSHDREFVS 497
Cdd:cd03222 69 -------YID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLD 136
|
170
....*....|....*
gi 489202159 498 SLATRIIEL-GENGV 511
Cdd:cd03222 137 YLSDRIHVFeGEPGV 151
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-183 |
7.59e-06 |
|
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: 47.04 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMK-ILGNdLEPSAGQVMLEPnVRLGKLRQDQFA-------------YE 77
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGL-LPPRSGSIRFDG-RDITGLPPHERAragigyvpegrriFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 78 DFSVIDTVIMGHEELW--AVKAERDRIYSL-PEMSEAdgmavaelevqfaefdgytAESRAGELLLGlgiplEQHfgpMS 154
Cdd:cd03224 89 ELTVEENLLLGAYARRraKRKARLERVYELfPRLKER-------------------RKQLAGTLSGG-----EQQ---ML 141
|
170 180
....*....|....*....|....*....
gi 489202159 155 AVapgwklrvllAQALFSDPDVLLLDEPT 183
Cdd:cd03224 142 AI----------ARALMSRPKLLLLDEPS 160
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
319-491 |
7.83e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA-----------DVGY 386
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshsvlrqGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 387 FAQDH---ADDFADDMSL---FDWMAQWtQGGEQLVRGTLGRMLfsNDEIKKSVkvisgGEQGRML---------FGRLI 451
Cdd:PRK10790 420 VQQDPvvlADTFLANVTLgrdISEEQVW-QALETVQLAELARSL--PDGLYTPL-----GEQGNNLsvgqkqllaLARVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489202159 452 LKRPNVLVMDEPTNHLDMESIEALN--LALDNYPGTLIFVSH 491
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQqaLAAVREHTTLVVIAH 533
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
337-508 |
8.04e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 337 GLSLQVEAGERVAIIGPNGIGKTTLLRCLV-------GDLPVDGGEVKWTDSADVGYFAQDhaddfaddmslfdwmaqwt 409
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELYYQGQDLLKADPEAQKLLRQK------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 410 qggEQLV----------RGTLGRML---------FSNDEIKKSV-----KV-------------ISGGEQGRMLFGRLIL 452
Cdd:PRK11308 94 ---IQIVfqnpygslnpRKKVGQILeepllintsLSAAERREKAlammaKVglrpehydryphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 453 KRPNVLVMDEPTNHLDMeSIEA--LNLALD---NYPGTLIFVSHDREFVSSLAT--------RIIELGE 508
Cdd:PRK11308 171 LDPDVVVADEPVSALDV-SVQAqvLNLMMDlqqELGLSYVFISHDLSVVEHIADevmvmylgRCVEKGT 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
320-519 |
1.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGK-PL-FKGL---SLQVEAGERVAIIGPNGIGKTTLLR------------CLVGDLPVDGGEVKWTDSA 382
Cdd:PRK13645 7 IILDNVSYTYAKKtPFeFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 D----VGYF-----AQDHADDFADDMSLFDW-MAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLIL 452
Cdd:PRK13645 87 RlrkeIGLVfqfpeYQLFQETIEKDIAFGPVnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 453 KRPNVLVMDEPTNHLDMESIEA-LNLAL---DNYPGTLIFVSHDREFVSSLATRIIELGENGVTDFSGSYD 519
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDfINLFErlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-527 |
1.10e-05 |
|
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: 47.90 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDG--GEVKW------------TDSADVG 385
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWsgsplkasnirdTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDHAddFADDMSLFDWM---AQWTQGGEQL--------VRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKR 454
Cdd:TIGR02633 82 IIHQELT--LVPELSVAENIflgNEITLPGGRMaynamylrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 455 PNVLVMDEPTNHLDMESIEA-LNLALD--NYPGTLIFVSHDREFVSSLATRI--IELGEN-GVTDFSGSYDDYLRSQGV 527
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEIlLDIIRDlkAHGVACVYISHKLNEVKAVCDTIcvIRDGQHvATKDMSTMSEDDIITMMV 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.90 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQF-GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGklrqdqfayeDF 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS-GIDTG----------DF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 80 SvidtvimgheelwavkaerdriySLPEMSEADGMAVAELEVQFAefdGYTAES------------------RAGELLLG 141
Cdd:PRK13644 70 S-----------------------KLQGIRKLVGIVFQNPETQFV---GRTVEEdlafgpenlclppieirkRVDRALAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 142 LGIPLEQHFGPMSaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT-IRWLEGV--LTARNSTMIIISHDRHFLnsv 218
Cdd:PRK13644 124 IGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL--- 199
|
250
....*....|....*...
gi 489202159 219 ctHMAD----LDYGELRL 232
Cdd:PRK13644 200 --HDADriivMDRGKIVL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-383 |
1.22e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 324 NISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGD-------LPVDGGEVKWTDSAD 383
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyqpdagsILIDGQEMRFASTTA 75
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
1.22e-05 |
|
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: 46.31 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 13 AKPLFENVSVKFGNGNRYGLIGANGCGKSTF-MKILGnDLEPSAGQVMLEPNVrlgklrqdqfAY---EDF----SVIDT 84
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLG-ELEKLSGSVSVPGSI----------AYvsqEPWiqngTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 85 VIMGHE--ELW---AVKA---ERDriysLPEMSEADgmavaELEVqfaefdgytaesraGELllglGIPLeqhfgpmSAv 156
Cdd:cd03250 86 ILFGKPfdEERyekVIKAcalEPD----LEILPDGD-----LTEI--------------GEK----GINL-------SG- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 157 apGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWL-EGVLT---ARNSTMIIISHDRHFL 215
Cdd:cd03250 131 --GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILgllLNNKTRILVTHQLQLL 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-248 |
1.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.15 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 19 NVSVKfgNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPN----VRLGKLRQDQFAYEDFSVIDtvimghEELWA 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidySRKGLMKLRESVGMVFQDPD------NQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 95 VKAERDRIYSlpemseADGMAVAELEVQfaefdgytaeSRAGELLLGLGIPLEQHfGPMSAVAPGWKLRVLLAQALFSDP 174
Cdd:PRK13636 98 ASVYQDVSFG------AVNLKLPEDEVR----------KRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 175 DVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGELrLFPGNYDEYMTAAEQAR 248
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNPKEVFAEKEMLR 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
1.36e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.88 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKIL--------GNDLEPSAGQVML---EPNVRLGKLRqDQFAY----ED 78
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsGRIARPAGARVLFlpqRPYLPLGTLR-EALLYpataEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 79 FSvidtvimgHEELWAVkaerdriyslpemseadgmavaeLE-VQFAEFDGYTAESRAGELLLGLGiplEQHfgpmsava 157
Cdd:COG4178 455 FS--------DAELREA-----------------------LEaVGLGHLAERLDEEADWDQVLSLG---EQQ-------- 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 158 pgwklRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTAR--NSTMIIISHdRHFLNSVCTHMADLD 226
Cdd:COG4178 493 -----RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
140-217 |
1.38e-05 |
|
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: 45.78 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 140 LGLG-IPLEQhfgPMSAVAPGWKLRVLLAQALFSDPD--VLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRH 213
Cdd:cd03238 74 VGLGyLTLGQ---KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLD 150
|
....
gi 489202159 214 FLNS 217
Cdd:cd03238 151 VLSS 154
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
315-479 |
1.44e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 315 LHRQAVTVENISKGY-DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV--------KWTDSADVG 385
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 386 YFAQDHADDFADDMSLFD-----------WMAQWTQGGEQLVRGTLGRMLFSnDEIKKSVKVISGGEQGRMLFGRLILKR 454
Cdd:PRK15056 82 YVPQSEEVDWSFPVLVEDvvmmgryghmgWLRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180
....*....|....*....|....*
gi 489202159 455 PNVLVMDEPTNHLDMESiEALNLAL 479
Cdd:PRK15056 161 GQVILLDEPFTGVDVKT-EARIISL 184
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
310-503 |
1.44e-05 |
|
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: 46.87 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 310 EQYKKLHRQAVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSADVGYFAQ 389
Cdd:cd03294 15 QKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 390 DHADDFADDMSL----FDWMAQWT-----------QG---GEQLVRGT--LGRMLFSNDEIKKsVKVISGGEQGRMLFGR 449
Cdd:cd03294 95 ELRELRRKKISMvfqsFALLPHRTvlenvafglevQGvprAEREERAAeaLELVGLEGWEHKY-PDELSGGMQQRVGLAR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 450 LILKRPNVLVMDEPTNHLD------MESiEALNLAlDNYPGTLIFVSHDREFVSSLATRI 503
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDplirreMQD-ELLRLQ-AELQKTIVFITHDLDEALRLGDRI 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-468 |
1.60e-05 |
|
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: 46.77 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGY--DGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV------GDLPVDGgeVKWtdsadvgyfaqdh 391
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIDG--VSW------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 392 addfaDDMSLFDWMAQWTQGGEQ--LVRGTLGRML-----FSNDEIKKSVK------------------------VISGG 440
Cdd:cd03289 68 -----NSVPLQKWRKAFGVIPQKvfIFSGTFRKNLdpygkWSDEEIWKVAEevglksvieqfpgqldfvlvdggcVLSHG 142
|
170 180
....*....|....*....|....*...
gi 489202159 441 EQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-510 |
1.74e-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: 45.68 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 349 AIIGPNGIGKTTLLRCLV----GDLP--VDGGevkwtdsadvgyfaqDHADDFAddmslfdwmaqwtqgGEQLVRGTLgR 422
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPpnSKGG---------------AHDPKLI---------------REGEVRAQV-K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 423 MLFSNDEiKKSVKVI----------------------------SGGEqgRMLFG---RLILKRP-----NVLVMDEPTNH 466
Cdd:cd03240 75 LAFENAN-GKKYTITrslailenvifchqgesnwplldmrgrcSGGE--KVLASliiRLALAETfgsncGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489202159 467 LDMESIE-ALNLALDNYPGTLIF----VSHDREFVsSLATRIIELGENG 510
Cdd:cd03240 152 LDEENIEeSLAEIIEERKSQKNFqlivITHDEELV-DAADHIYRVEKDG 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
324-513 |
2.29e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 324 NISKGY-DGK---PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVG-DLPVdGGEV--------KWTDSA-------D 383
Cdd:PRK11629 10 NLCKRYqEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPT-SGDVifngqpmsKLSSAAkaelrnqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 384 VGYFAQDH--ADDFAD----DMSLFDWMAQWTQGGEQLVRgtlgrMLFSNDEIKKS---VKVISGGEQGRMLFGRLILKR 454
Cdd:PRK11629 89 LGFIYQFHhlLPDFTAlenvAMPLLIGKKKPAEINSRALE-----MLAAVGLEHRAnhrPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 455 PNVLVMDEPTNHLDM---ESIEALNLALDNYPGT-LIFVSHDREFVSSLaTRIIELGENGVTD 513
Cdd:PRK11629 164 PRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
332-471 |
2.72e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.93 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 332 KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLV---------GDLPVDGGEVKWTDSADVGYFAQdhaddfaddmslf 402
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEILINGRPLDKNFQRSTGYVEQ------------- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 403 dwmaQWTQGGEQLVRGTLgrmLFSNDeikksVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMES 471
Cdd:cd03232 87 ----QDVHSPNLTVREAL---RFSAL-----LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-526 |
2.91e-05 |
|
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: 47.25 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 274 ANASKAKQATSRARQIdkIQLEEVKPSSrvspfIRFEQYKKLHRQAVTVENISKGY--DGKPLFKGLSLQVEAGERVAII 351
Cdd:TIGR00957 598 SSIVQASVSLKRLRIF--LSHEELEPDS-----IERRTIKPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGALVAVV 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 352 GPNGIGKTTLLRCLVGDLpvDGGEVKWTDSADVGYFAQDH--ADDFADDMSLFDWMAQwtqggEQLVRGTLG-------- 421
Cdd:TIGR00957 671 GQVGCGKSSLLSALLAEM--DKVEGHVHMKGSVAYVPQQAwiQNDSLRENILFGKALN-----EKYYQQVLEacallpdl 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 422 RMLFSND--EIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMESIEALnlaLDNYPG--------TLIFVSH 491
Cdd:TIGR00957 744 EILPSGDrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGpegvlknkTRILVTH 820
|
250 260 270
....*....|....*....|....*....|....*
gi 489202159 492 DREFVSSLATrIIELGENGVTDFsGSYDDYLRSQG 526
Cdd:TIGR00957 821 GISYLPQVDV-IIVMSGGKISEM-GSYQELLQRDG 853
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-244 |
3.12e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 45.60 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 20 VSVKFGNGNRYGLIGANGCGKSTFMKILGnDLEPSAGQVMLE-------PNVRLGKLR----QDQ--------FAYEDFS 80
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMA-GLLPGQGEILLNgrplsdwSAAELARHRaylsQQQsppfampvFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 81 vidtvimgheelwavkaerdriYSLPEMSEADGMAVAELevqfaefdgytaeSRAGELLLGLGIPLEQHFGpmsavapG- 159
Cdd:COG4138 94 ----------------------QPAGASSEAVEQLLAQL-------------AEALGLEDKLSRPLTQLSG-------Ge 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 160 WKlRVLLAQALFS-DPDV------LLLDEPTNHLDIN----TIRWLEGvLTARNSTMIIISHDrhfLNSVCTHmAD---- 224
Cdd:COG4138 132 WQ-RVRLAAVLLQvWPTInpegqlLLLDEPMNSLDVAqqaaLDRLLRE-LCQQGITVVMSSHD---LNHTLRH-ADrvwl 205
|
250 260
....*....|....*....|
gi 489202159 225 LDYGELrLFPGNYDEYMTAA 244
Cdd:COG4138 206 LKQGKL-VASGETAEVMTPE 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-77 |
4.62e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 4.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNvrlgKLRQDQFAYE 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ----SIKKDLCTYQ 73
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
331-469 |
5.58e-05 |
|
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: 45.23 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 331 GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwtDSADVGYFAQdhaddfaddmslFDWMAQWTQ 410
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQ------------FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 411 gGEQLVRGTlgrmlfSNDEIK-KSVK-------------------------VISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:cd03291 115 -KENIIFGV------SYDEYRyKSVVkacqleeditkfpekdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....*
gi 489202159 465 NHLDM 469
Cdd:cd03291 188 GYLDV 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
6.04e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 44.73 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 20 VSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLepnvrLGKLRQDQFAYEDFSVIDTVIMGHEelwavkaer 99
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV-----MGREVNAENEKWVRSKVGLVFQDPD--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 100 DRIYSlpemseadgmAVAELEVQFA----EFDGYTAESRAGELLLGLGIPLEQHFGPMSaVAPGWKLRVLLAQALFSDPD 175
Cdd:PRK13647 90 DQVFS----------STVWDDVAFGpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPYH-LSYGQKKRVAIAGVLAMDPD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 489202159 176 VLLLDEPTNHLD---INTIRWLEGVLTARNSTMIIISHD 211
Cdd:PRK13647 159 VIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-187 |
6.37e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQ------F- 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENrhvntvFq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 75 AYEDF---SVIDTVIMGheeLWAVKAERDRIYslPEMSEADGMavaeleVQFAEFdgytAESRAGELllglgipleqhfg 151
Cdd:PRK09452 94 SYALFphmTVFENVAFG---LRMQKTPAAEIT--PRVMEALRM------VQLEEF----AQRKPHQL------------- 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 489202159 152 pmsavAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:PRK09452 146 -----SGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
320-376 |
6.87e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.18 E-value: 6.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 320 VTVENISKGYDGK----PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCL-------VGDLPVDGGEV 376
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerptSGRVLVDGQDL 69
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-226 |
7.09e-05 |
|
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: 43.30 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGnDLEPSAGqvmlepnvrlGKLrqdqfayedfsvidtvimgheelw 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-GLWPWGS----------GRI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 94 aVKAERDRIYSLPEMSeadgmavaelevqfaefdgYtaesragellLGLGIPLEQHFGPMSAV-APGWKLRVLLAQALFS 172
Cdd:cd03223 59 -GMPEGEDLLFLPQRP-------------------Y----------LPLGTLREQLIYPWDDVlSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489202159 173 DPDVLLLDEPTNHLDINTIRWLEGVLTARNSTMIIISHdRHFLNSVCTHMADLD 226
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-244 |
7.18e-05 |
|
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: 44.32 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 31 GLIGANGCGKSTFMKILGNDLEPSAGQvmlepnvrlgklrqdqfayedfsvidtvimgheelwaVKAERDRIYSLPEMSE 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGD-------------------------------------IEIELDTVSYKPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 111 AD-GMAVAELEVQFAEfDGYTAESRAGELLLGLGIP--LEQHFGPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:cd03237 72 ADyEGTVRDLLSSITK-DFYTHPYFKTEIAKPLQIEqiLDREVPELSG---GELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489202159 188 INtirwlEGVLTAR---------NSTMIIISHDrhFLnsvcthMADLDYGELRLFPGNYDEYMTAA 244
Cdd:cd03237 148 VE-----QRLMASKvirrfaennEKTAFVVEHD--II------MIDYLADRLIVFEGEPSVNGVAN 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-183 |
8.04e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 44.20 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 31 GLIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDQFA-------------YEDFSVIDTVIMG---HEELWA 94
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRIArlgigyvpegrriFPSLTVEENLLLGayaRRDRAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 95 VKAERDRIYSL-PEMseadgmavaelevqfAEFdgytAESRAGELLLGlgiplEQHfgpMSAVApgwklRvllaqALFSD 173
Cdd:COG0410 112 VRADLERVYELfPRL---------------KER----RRQRAGTLSGG-----EQQ---MLAIG-----R-----ALMSR 154
|
170
....*....|
gi 489202159 174 PDVLLLDEPT 183
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
324-378 |
8.73e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 8.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 324 NISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVD--GGEVKW 378
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIF 66
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
342-511 |
8.73e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.28 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 342 VEAGERVAIIGPNGIGKTTLLRCLVG----DLPVDGGEVKWTDSADvgYFA----QDHADDFADDMSLFDWMAQWTQGGE 413
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpNLGKFDDPPDWDEILD--EFRgselQNYFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 414 QLVRGTLGRMLFSNDEIKKSVKVI----------------SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMEsiEALNL 477
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDELVdqlelrhvldrnidqlSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489202159 478 A-----LDNYPGTLIFVSHDREFVSSLATRI-IELGENGV 511
Cdd:cd03236 179 ArlireLAEDDNYVLVVEHDLAVLDYLSDYIhCLYGEPGA 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-187 |
9.09e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.93 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGnRYGLI-GANGCGKSTFMKILGNDLEPSAGQVMLEpnvrlGK---------LRQdQFA 75
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAG-EFKLItGPSGCGKSTLLKIVASLISPTSGTLLFE-----GEdistlkpeiYRQ-QVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 76 Y--------EDfSVIDTVIMGheelWAVKAERdriyslPEMSE-ADGMAvaelevQFaefdgytaesragelllglGIPL 146
Cdd:PRK10247 85 YcaqtptlfGD-TVYDNLIFP----WQIRNQQ------PDPAIfLDDLE------RF-------------------ALPD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489202159 147 EQHFGPMSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:PRK10247 129 TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-211 |
1.22e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.25 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVM--------LEPNVR-LGKLRQDQFAY 76
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrmndVPPAERgVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 77 EDFSVIDTVIMGHEELWAVKAERDRIYSlpemseadgmAVAELevqfaefdgytaesragellLGLGIPLEQHfgPmSAV 156
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRVN----------QVAEV--------------------LQLAHLLDRK--P-KAL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 157 APGWKLRVLLAQALFSDPDVLLLDEPTNHLDInTIRWLEGVLTAR-----NSTMIIISHD 211
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-ALRVQMRIEISRlhkrlGRTMIYVTHD 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-468 |
1.25e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 329 YDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWT----DSADVGYFA--QDHADDFAD-DMSL 401
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLAlrQQVATVFQDpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 402 FdwmaqWTQGGEQLVRgTLGRMLFSNDEIKKSV-----------------KVISGGEQGRMLFGRLILKRPNVLVMDEPT 464
Cdd:PRK13638 91 F-----YTDIDSDIAF-SLRNLGVPEAEITRRVdealtlvdaqhfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
....
gi 489202159 465 NHLD 468
Cdd:PRK13638 165 AGLD 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
336-469 |
1.26e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 336 KGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDS----ADVGYFAQDHADDFAD-------------- 397
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSYRSQRIRMIFQDpstslnprqrisqi 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 398 -DMSLFDWMAQWTQGGEQLVRGTLGRMLFSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM 469
Cdd:PRK15112 110 lDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
159-218 |
1.76e-04 |
|
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: 42.90 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHDRHFLNSV 218
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-281 |
2.05e-04 |
|
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: 44.17 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVrlGKLRQDQFAYEDfSV 81
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWIQND-SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 IDTVIMGHeelwAVKAERDRiyslpEMSEADGMaVAELEVqFAEFDgytaESRAGELllglGIPLeqhfgpmsavAPGWK 161
Cdd:TIGR00957 716 RENILFGK----ALNEKYYQ-----QVLEACAL-LPDLEI-LPSGD----RTEIGEK----GVNL----------SGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLDINTIRWL-------EGVLtaRNSTMIIISHDRHFL--NSVCTHMADLDYGELrl 232
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVL--KNKTRILVTHGISYLpqVDVIIVMSGGKISEM-- 842
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489202159 233 fpGNYDEYMtAAEQARERLLSDNAKKKAQIAELQSFVSRFSANASKAKQ 281
Cdd:TIGR00957 843 --GSYQELL-QRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKL 888
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
2.07e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 2 ISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGN--DLEPSA---GQVML------EPNV------ 64
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLfgrniySPDVdpievr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 65 -RLGKLRQDQFAYEDFSVIDTVIMGHEELWAVKAERDriysLPEMSE-ADGMAVAELEVQfaefdgytaeSRagelllgl 142
Cdd:PRK14267 85 rEVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKE----LDERVEwALKKAALWDEVK----------DR-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 143 gipLEQHFGPMSAvapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISHDRHFLNSVCT 220
Cdd:PRK14267 143 ---LNDYPSNLSG---GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTHSPAQAARVSD 216
|
250
....*....|
gi 489202159 221 HMADLDYGEL 230
Cdd:PRK14267 217 YVAFLYLGKL 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
331-469 |
2.18e-04 |
|
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: 44.13 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 331 GKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKwtDSADVGYFAQdhaddfaddmslFDWmaqwtq 410
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQ------------TSW------ 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 411 ggeqLVRGTL-GRMLF--SNDEIKKSVKV--------------------------ISGGEQGRMLFGRLILKRPNVLVMD 461
Cdd:TIGR01271 498 ----IMPGTIkDNIIFglSYDEYRYTSVIkacqleedialfpekdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
....*...
gi 489202159 462 EPTNHLDM 469
Cdd:TIGR01271 574 SPFTHLDV 581
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
325-503 |
2.27e-04 |
|
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: 44.23 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 325 ISKGYDG--KPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGevkwtDSADVGYFAQDHADDFADDMSL- 401
Cdd:TIGR01257 1943 LTKVYSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAGKSILTNISDVHQNMGYc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 402 --FDWMAQWTQGGEQL-----VRG---------------TLGRMLFSNdeikKSVKVISGGEQGRMLFGRLILKRPNVLV 459
Cdd:TIGR01257 2018 pqFDAIDDLLTGREHLylyarLRGvpaeeiekvanwsiqSLGLSLYAD----RLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489202159 460 MDEPTNHLDMESIEAL---NLALDNYPGTLIFVSHDREFVSSLATRI 503
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLwntIVSIIREGRAVVLTSHSMEECEALCTRL 2140
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-187 |
2.62e-04 |
|
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: 42.15 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 12 GAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSA--GQVML--------EPNVRLGKLRQDQFAYEDFSV 81
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLIngrpldkrSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 idtvimgHEELWavkaerdriyslpemseadgmavaelevqfaefdgYTAESRagelllglGIPLEQhfgpmsavapgwK 161
Cdd:cd03213 100 -------RETLM-----------------------------------FAAKLR--------GLSGGE------------R 117
|
170 180
....*....|....*....|....*.
gi 489202159 162 LRVLLAQALFSDPDVLLLDEPTNHLD 187
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
337-503 |
3.35e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 337 GLSLQVEAGERVAIIGPNGIGKT----TLLRCL--------VGDLPVDGGEVKWTDSADV-GYFAQDHADDFADDM---- 399
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQTLrGVRGNKIAMIFQEPMvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 400 -------------SLFDWMAQWTQGGEQL-------VRGTLGRMlfsNDEIKKsvkvISGGEQGRMLFGRLILKRPNVLV 459
Cdd:PRK15134 107 plhtlekqlyevlSLHRGMRREAARGEILncldrvgIRQAAKRL---TDYPHQ----LSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489202159 460 MDEPTNHLDMeSIEALNLALDN-----YPGTLIFVSHDREFVSSLATRI 503
Cdd:PRK15134 180 ADEPTTALDV-SVQAQILQLLRelqqeLNMGLLFITHNLSIVRKLADRV 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-227 |
4.08e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.35 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 31 GLIGANGCGKSTFMKILGNDLEPSAGQVMLEPNVR--------------LGKLRQDQFA------YEDfsVIDTVIMGH- 89
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeildefrgselqnyFTKLLEGDVKvivkpqYVD--LIPKAVKGKv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 90 EELWAVKAERDRIYSLPEMSEADGMavaeLEVQFAEFDGytaesraGELllglgipleqhfgpmsavapgwkLRVLLAQA 169
Cdd:cd03236 108 GELLKKKDERGKLDELVDQLELRHV----LDRNIDQLSG-------GEL-----------------------QRVAIAAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489202159 170 LFSDPDVLLLDEPTNHLDI----NTIRWLEGVLTARNStMIIISHDrhflnsvcthMADLDY 227
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIkqrlNAARLIRELAEDDNY-VLVVEHD----------LAVLDY 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
319-468 |
4.54e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK---PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLP--------VDGG-----EVKWTDSA 382
Cdd:PLN03232 614 AISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShaetssvvIRGSvayvpQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 DVG---YFAQDH----------ADDFADDMSLFDwmaqwtqggeqlvrgtlGRMLfsnDEIKKSVKVISGGEQGRMLFGR 449
Cdd:PLN03232 694 TVReniLFGSDFeserywraidVTALQHDLDLLP-----------------GRDL---TEIGERGVNISGGQKQRVSMAR 753
|
170
....*....|....*....
gi 489202159 450 LILKRPNVLVMDEPTNHLD 468
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALD 772
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
134-216 |
4.60e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 134 RAGELLLGLGIplEQHFGPMSA----VAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDINT----IRWLEGVLTARNSTM 205
Cdd:PRK15093 135 RAIELLHRVGI--KDHKDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTI 212
|
90
....*....|.
gi 489202159 206 IIISHDRHFLN 216
Cdd:PRK15093 213 LLISHDLQMLS 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
438-510 |
4.88e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.55 E-value: 4.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 438 SGGEQGRMLFGRLILKRPNVLVMDEPTNHLDM----ESIEAL-NLALD-NYPgtLIFVSHDREFVSSLATRIIELgENG 510
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLeRLAREiNIP--ILYVSHSLDEILRLADRVVVL-EQG 205
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
277-378 |
4.91e-04 |
|
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: 42.86 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 277 SKAKQAtsrARQIDKIQLEEVKPSSRVSPFIRFEQYKklHRQAVTVENISKGY---DGKPLFK-G-LSLQVEAGERVAII 351
Cdd:COG4615 290 SRANVA---LRKIEELELALAAAEPAAADAAAPPAPA--DFQTLELRGVTYRYpgeDGDEGFTlGpIDLTIRRGELVFIV 364
|
90 100
....*....|....*....|....*..
gi 489202159 352 GPNGIGKTTLLRCLVGDLPVDGGEVKW 378
Cdd:COG4615 365 GGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-248 |
5.08e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 42.89 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVL--TARNSTMIIISHDRHFLNSVcTHMADLDYGELRLfPGNYDEY 240
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLaeHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE-QGTHQEL 560
|
....*...
gi 489202159 241 MtaAEQAR 248
Cdd:PRK11160 561 L--AQQGR 566
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-217 |
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: 40.43 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 27 GNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgklrqdqfayedfsvidtVIMGHEELWAVKAERDRIYSLP 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------YIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 107 EMSEADGMAvaelevqfaefdgytaesragelllglgipleqhfgpmsavapgwKLRVLLAQALFSDPDVLLLDEPTNHL 186
Cdd:smart00382 57 KKASGSGEL---------------------------------------------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489202159 187 DINT---------IRWLEGVLTARNSTMIIISHDRHFLNS 217
Cdd:smart00382 92 DAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
322-378 |
6.00e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 6.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKW 378
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY 63
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
322-493 |
6.06e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 322 VENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSA---DVGYFAQD-----HAD 393
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkDLCTYQKQlcfvgHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 DFADDMSL-----FDWMAQWTQGG-EQLVRgtlgrmLFSNDE-IKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNH 466
Cdd:PRK13540 84 GINPYLTLrenclYDIHFSPGAVGiTELCR------LFSLEHlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 489202159 467 LDMESIEALNLALDNYP---GTLIFVSHDR 493
Cdd:PRK13540 158 LDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
319-362 |
6.92e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 6.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489202159 319 AVTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLL 362
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL 44
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
130-269 |
6.99e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 130 TAESRAGELLLGLGIP-----LE----QHFGPMSAvapgwklRVLLAQALFSDPDVLLLDEPTNHLDI----NTIRWLEG 196
Cdd:PRK11022 126 TRRQRAIDLLNQVGIPdpasrLDvyphQLSGGMSQ-------RVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 197 VLTARNSTMIIISHDRHFLNSVCTHMadldygeLRLFPGNYDEYMTAAE----------QARERLLSDNAKKKAQIAELQ 266
Cdd:PRK11022 199 LQQKENMALVLITHDLALVAEAAHKI-------IVMYAGQVVETGKAHDifraprhpytQALLRALPEFAQDKARLASLP 271
|
...
gi 489202159 267 SFV 269
Cdd:PRK11022 272 GVV 274
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
339-475 |
7.32e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 339 SLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV---------------------KWT---------DSADVGYFA 388
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitrlsfeqlqklvsdEWQrnntdmlspGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 389 QDHADDFADDMSLFDWMAQWTQGGEQLVRgtlgrmlfsndeikkSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD 468
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQFGITALLDR---------------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
....*..
gi 489202159 469 MESIEAL 475
Cdd:PRK10938 168 VASRQQL 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
116-229 |
8.32e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 116 VAE-LEVQFAEFDGYTAESRAGELLLGLGI-PLEQHFGPmSAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD------ 187
Cdd:PRK15134 385 IEEgLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaq 463
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489202159 188 INTIrwLEGVLTARNSTMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:PRK15134 464 ILAL--LKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
9.29e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 41.29 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV--------------MLEPNVRL 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipamsrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 67 GKLRQDQFAYEDFSVIDTVIMGHEELWAVKAERDRIYSLPEMsEADGMAVAElEVQFAEFDGytaesragelllglgipl 146
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKL-EAVGLRGAA-KLMPSELSG------------------ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489202159 147 eqhfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGVLTARNS----TMIIISHD 211
Cdd:PRK11831 147 ------------GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-61 |
9.46e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.13 E-value: 9.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489202159 1 MISTANITMQFGAKPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE 61
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR 65
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
9.47e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 41.28 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLF--ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE----PNVRLGKLRQD-- 72
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaiTDDNFEKLRKHig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 73 -------------------QFAYEDFSVidtvimGHEELWAVKAErdriyslpEMSEADGMAVAELEVQfaefdgytaes 133
Cdd:PRK13648 87 ivfqnpdnqfvgsivkydvAFGLENHAV------PYDEMHRRVSE--------ALKQVDMLERADYEPN----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 134 ragelllglgipleqhfgpmsAVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLD----INTIRWLEGVLTARNSTMIIIS 209
Cdd:PRK13648 142 ---------------------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDpdarQNLLDLVRKVKSEHNITIISIT 200
|
..
gi 489202159 210 HD 211
Cdd:PRK13648 201 HD 202
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-58 |
2.11e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489202159 1 MISTANITMQFGAKPLFeNVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV 58
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
323-376 |
2.40e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489202159 323 ENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEV 376
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
437-504 |
2.42e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 437 ISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEA----LNLALDNYPG-TLIFVSHDREFVSSLATRII 504
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqiieLLLELQQKENmALVLITHDLALVAEAAHKII 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
2.69e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 39.35 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 1 MISTANITMQFGAKPLfeNVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQV--------MLEPNVR-LGKLRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltALPPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 72 DQ--FAYedFSVIDTVIMG-HEELWAVKAERDRIyslpemseadgMAVAElEVQFAEFdgytaESRAGELLLGlgipleq 148
Cdd:COG3840 79 ENnlFPH--LTVAQNIGLGlRPGLKLTAEQRAQV-----------EQALE-RVGLAGL-----LDRLPGQLSG------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 149 hfgpmsavapGWKLRVLLAQALFSDPDVLLLDEPTNHLDIN----TIRWLEGVLTARNSTMIIISHD 211
Cdd:COG3840 133 ----------GQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-504 |
2.87e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 320 VTVENISKGYDGKPLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVKWTDSAdvgYFAQDHAD------ 393
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLaaqlgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 394 -------DFADDMS-------------------LFDWMAQWTQGGEQLVRGTLGRMLfsndEIKksVKVISGGEQGRMLF 447
Cdd:PRK09700 83 giiyqelSVIDELTvlenlyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDL----DEK--VANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 448 GRLILKRPNVLVMDEPTNHLDMESIEALNLALDNYPG---TLIFVSH---------DREFV----SSLATRII 504
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHklaeirricDRYTVmkdgSSVCSGMV 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
2.95e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 2.95e-03
10 20
....*....|....*....|....*
gi 489202159 164 VLLAQALFSDPDVLLLDEPTNHLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-468 |
3.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 319 AVTVENISKGYDGK---PLFKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPV--DGG-----------EVKWTDSA 382
Cdd:PLN03130 614 AISIKNGYFSWDSKaerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrsDASvvirgtvayvpQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 383 DV-------------GYFAQDHADDFADDMSLFdwmaqwtQGGEQlvrgtlgrmlfsnDEIKKSVKVISGGEQGRMLFGR 449
Cdd:PLN03130 694 TVrdnilfgspfdpeRYERAIDVTALQHDLDLL-------PGGDL-------------TEIGERGVNISGGQKQRVSMAR 753
|
170
....*....|....*....
gi 489202159 450 LILKRPNVLVMDEPTNHLD 468
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALD 772
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
159-245 |
3.42e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 159 GWKLRVLLAQALFSDPDVLLLDEPTNHLDINT---IRWLEGVLTAR-NSTMIIISHDRHFLNSVCTHMadldygeLRLFP 234
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREfNTAIIMITHDLGVVAGICDKV-------LVMYA 237
|
90
....*....|.
gi 489202159 235 GNYDEYMTAAE 245
Cdd:PRK09473 238 GRTMEYGNARD 248
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-211 |
4.11e-03 |
|
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: 38.57 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 163 RVLLAQALFSDPDVLLLDEPTNHLDINTIRWLEGV---LTARNSTMIIISHD 211
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLireLADAGKAVLLISSE 163
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-261 |
4.12e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 18 ENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMlepnvrlgklrqdqfAYEDFSVIDTVIMGHEELWAVKA 97
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD---------------RNGEVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 98 ERDRIYSLPEMSEadgmAVAELEVQFAEFdgytaeSRAGELLlglgipleqhFGPMSAVAPGWKLRVLLAQALFSDPDVL 177
Cdd:PRK13546 106 IEFKMLCMGFKRK----EIKAMTPKIIEF------SELGEFI----------YQPVKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 178 LLDEPTNHLDIN-TIRWLEGV--LTARNSTMIIISHDRHFLNSVCTHMADLDYGELRLFpGNYDEYMTAAEQarerLLSD 254
Cdd:PRK13546 166 VIDEALSVGDQTfAQKCLDKIyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVLPKYEA----FLND 240
|
....*...
gi 489202159 255 NAKK-KAQ 261
Cdd:PRK13546 241 FKKKsKAE 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
437-504 |
4.16e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.84 E-value: 4.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489202159 437 ISGGEQGRMLFGRLILKRPNVLVMDEPTNHLDMeSIEALNLAL-----DNYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLikvlqKEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
139-188 |
4.49e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.47 E-value: 4.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489202159 139 LLGLGiPLEQHFgPMSaVAPGWKLRVLLAQALFSDPDVLLLDEPTNHLDI 188
Cdd:PRK11144 115 LLGIE-PLLDRY-PGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-210 |
4.87e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 39.70 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 14 KPLFENVSVKFGNGNRYGLIGANGCGKSTFMKILGNDLEPSAGQVMLE--PNVRLGK--LRQDQFAYEDfsviDTVIMGH 89
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrPLSSLSHsvLRQGVAMVQQ----DPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 90 EELWAVKAERDriyslpeMSEADGMAVAELeVQFAEFdgytaesrAGELLLGLGIPLEQHFGPMSAvapGWKLRVLLAQA 169
Cdd:PRK10790 430 TFLANVTLGRD-------ISEEQVWQALET-VQLAEL--------ARSLPDGLYTPLGEQGNNLSV---GQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489202159 170 LFSDPDVLLLDEPTNHLDINTIRWLEGVLTA--RNSTMIIISH 210
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAvrEHTTLVVIAH 533
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-210 |
5.70e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 6 NITMQF-GAKPLfENVSVKFGNGNRYGLIGANGCGKSTFMKILgNDLEPSA---GQVMLEpnvrlGKLRQdqfayedFSV 81
Cdd:NF040905 6 GITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYPHGsyeGEILFD-----GEVCR-------FKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 82 I-DT-----VIMgHEELWAVkaerdriyslPEMSEADGMAVAELEVQFAEFDGYTAESRAGELL--LGLGiplEQHFGPM 153
Cdd:NF040905 72 IrDSealgiVII-HQELALI----------PYLSIAENIFLGNERAKRGVIDWNETNRRARELLakVGLD---ESPDTLV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489202159 154 SAVAPGWKLRVLLAQALFSDPDVLLLDEPT--------NHLdINTIRWL--EGVltarnsTMIIISH 210
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTaalneedsAAL-LDLLLELkaQGI------TSIIISH 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-82 |
5.76e-03 |
|
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: 39.40 E-value: 5.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489202159 32 LIGANGCGKSTFMKILGNDLEPSAGQVMLEpNVRLGKLRQDqfAYED-FSVI 82
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTADNRE--AYRQlFSAV 411
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
425-513 |
8.01e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 38.22 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 425 FSNDEIKKSVKVISGGEQGRMLFGRLILKRPNVLVMDEPTNHLD-------MESIEALNLALDNypgTLIFVSHDREFVS 497
Cdd:PRK13646 134 FSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskrqvMRLLKSLQTDENK---TIILVSHDMNEVA 210
|
90
....*....|....*.
gi 489202159 498 SLATRIIELGENGVTD 513
Cdd:PRK13646 211 RYADEVIVMKEGSIVS 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
287-376 |
8.43e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 38.80 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 287 RQIDKIQLEEVKPSSRVSPfiRFEQYKKLHRQAVTVENISKGYDGKPLfkglSLQVEAGERVAIIGPNGIGKTTLLRCLV 366
Cdd:PRK10522 297 NKLNKLALAPYKAEFPRPQ--AFPDWQTLELRNVTFAYQDNGFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLT 370
|
90
....*....|....*..
gi 489202159 367 -------GDLPVDGGEV 376
Cdd:PRK10522 371 glyqpqsGEILLDGKPV 387
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
437-507 |
9.13e-03 |
|
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: 37.30 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489202159 437 ISGGEQGRM-----LFGRLilkRPNVLVMDEPTNHLDMES----IEALNLALDNyPGTLIFVSHDREFVSSlATRIIELG 507
Cdd:cd03238 88 LSGGELQRVklaseLFSEP---PGTLFILDEPSTGLHQQDinqlLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFG 162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
330-377 |
9.31e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 9.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489202159 330 DGKPL-FKGLSLQVEAGERVAIIGPNGIGKTTLLRCLVGDLPVDGGEVK 377
Cdd:PTZ00243 1320 EGLPLvLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
|
| |
