|
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: 1176.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEFT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVIMGHEELWKVKAERDRIYSLPEMTEDDGMAVAELETEFAEMDGYTAESRAGELLLGLGIGIEQHNGPMSEVSPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 161 KLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 241 MTVATQSREQLLADNAKKKAQISELQSFVSRFSANASKAKQATSRAKQIDKIQLAEVKPSSRVSPFIRFEQTKKLHRQAV 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 321 VVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAHDFEDECT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 401 LFDWMGQWTQGG--EQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLA 478
Cdd:PRK15064 401 LFDWMSQWRQEGddEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1502692530 479 LENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLRSQGV 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: 742.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEFTVLDTV 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMGHEELWKVKAERDRIYSLPEMTEDDGMAVAELETEFAEMDGYTAESRAGELLLGLGIGIEQHNGPMSEVSPGWKLRVL 165
Cdd:COG0488 83 LDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEYMTVAT 245
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 246 QSREQLLADNAKKKAQISELQSFVSRFSANASKAKQATSRAKQIDKIQLAEVKPSSRvSPFIRFEQTKKLHRQAVVVERM 325
Cdd:COG0488 243 ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELEGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 326 AKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAhDFEDECTLFDWM 405
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-ELDPDKTVLDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 GQWTQGG-EQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPG 484
Cdd:COG0488 401 RDGAPGGtEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 1502692530 485 TLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLR 523
Cdd:COG0488 481 TVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-520 |
3.23e-97 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 307.65 E-value: 3.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEFT 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVIMGHEELWKVKAERDRIYSLPEMTEDDGM--AVAELETEFAEMDGYTAESRAGELLLGLGIGIeqhNGPMSEVSP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 239 EYMTvatqSREQLL----ADNA---KKKAQiSEL---QSFVSRFSAN-----ASKAKQaTSRAKQID-----KIQLAEVK 298
Cdd:PRK11147 240 QYLL----EKEEALrveeLQNAefdRKLAQ-EEVwirQGIKARRTRNegrvrALKALR-RERSERREvmgtaKMQVEEAS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 299 PSSRvspfIRFEqtkklhrqavvVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW 378
Cdd:PRK11147 314 RSGK----IVFE-----------MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 379 TESAEIGYYAQdHAHDFEDECTLFDWMGQWTQ-----GGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQ 453
Cdd:PRK11147 379 GTKLEVAYFDQ-HRAELDPEKTVMDNLAEGKQevmvnGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLK 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVID-FSGTYDD 520
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGrYVGGYHD 525
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-521 |
2.62e-88 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 284.37 E-value: 2.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEfT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVIMGHEELWKVKAErdriysLPEMTE-DDGMAVAELETEFAEMDGYTAESRAGELLLGLGIGIEQHNGPMSEVSPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANErNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 160 WKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDE 239
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 240 Y-MTVATQ-SREQLLADNAKKKaqISELQSFVSRFSANASKAKQATSRAKQIDKIQLaeVKPSSRVSPF-IRFEQTKKLH 316
Cdd:PRK10636 234 FeVQRATRlAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 317 RQAVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQdhaHDFE 396
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ---HQLE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 ----DECTLFDWMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESI 472
Cdd:PRK10636 387 flraDESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1502692530 473 EALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDY 521
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-521 |
1.13e-87 |
|
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: 280.28 E-value: 1.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEFTVLDTVIMGHEELW 93
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 KVKAERDRIYSLpEMTEDDGMAV-----AELETEFAEMDGYTAESRAGELLLGLGIGIEqhNGPMSEVSPGWKLRVLLAQ 168
Cdd:TIGR03719 98 DALDRFNEISAK-YAEPDADFDKlaaeqAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 169 ALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPGNYDEYMTVATQSR 248
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 249 EQLLADNAKKKAQISELQSFVsRFSAnasKAKQATSRAKQIDKIQLAEVKPSSRVSPF-IRFEQTKKLHRQAVVVERMAK 327
Cdd:TIGR03719 255 EQEEKEESARQKTLKRELEWV-RQSP---KGRQAKSKARLARYEELLSQEFQKRNETAeIYIPPGPRLGDKVIEAENLTK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAHdFEDECTLFdwmgQ 407
Cdd:TIGR03719 331 AFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDA-LDPNKTVW----E 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 WTQGGEQLV---------RGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLA 478
Cdd:TIGR03719 406 EISGGLDIIklgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1502692530 479 LENYPGTLIFVSHDREFVSSLATRIIELS-PSGVIDFSGTYDDY 521
Cdd:TIGR03719 486 LLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-521 |
1.86e-80 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 261.59 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEEFTVLDTVIMGHEELW 93
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 KVKAERDRI---YSLPEMTEDDGMA-VAELETEFAEMDGYTAESR--------------AgelllglgigieqhngPMSE 155
Cdd:PRK11819 100 AALDRFNEIyaaYAEPDADFDALAAeQGELQEIIDAADAWDLDSQleiamdalrcppwdA----------------KVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 156 VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLFPG 235
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 236 NYDEYMT-----VATQSREqllaDNAKKKAQISELQsFVsRFSAnasKAKQATSRAkqidkiqlaevkpssRVSpfiRFE 310
Cdd:PRK11819 244 NYSSWLEqkakrLAQEEKQ----EAARQKALKRELE-WV-RQSP---KARQAKSKA---------------RLA---RYE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 311 Q------TKKLHRQ-----------AVVVE--RMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTP 371
Cdd:PRK11819 297 EllseeyQKRNETNeifippgprlgDKVIEaeNLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 372 DAGSIKWTESAEIGYYAQDHAHdFEDECTLFDwmgQWTQGGEQLV--------RGTLGRMLFSNDEILKSVKVISGGEQG 443
Cdd:PRK11819 377 DSGTIKIGETVKLAYVDQSRDA-LDPNKTVWE---EISGGLDIIKvgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERN 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 444 RMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRII--ElSPSGVIDFSGTYDDY 521
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILafE-GDSQVEWFEGNFQEY 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-523 |
1.17e-76 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 255.55 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGG---DLEPSGGQVMlepNVRLGKLRQDQFAYEe 78
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaiDGIPKNCQIL---HVEQEVVGDDTTALQ- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 fTVLDTVI----MGHEELWKVKAERDriYSLPEMTEDDGMA-------------VAELETEFAEMDGYTAESRAGELLLG 141
Cdd:PLN03073 254 -CVLNTDIertqLLEEEAQLVAQQRE--LEFETETGKGKGAnkdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 142 LGIGIEQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTH 221
Cdd:PLN03073 331 LSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 222 MADLDYGELRLFPGNYDEY-MTVATQSREQLLADNAKKKAQiSELQSFVSRFSANASKAKQATSRAKQIDKIQLAEVKPS 300
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVN 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 301 srvSPFIRFE-QTKKLHRQAVVVERMAKGF---DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI 376
Cdd:PLN03073 490 ---DPDYKFEfPTPDDRPGPPIISFSDASFgypGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 KWTESAEIGYYAQDHAHDFEDECTLFDWMGQWTQGG-EQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKP 455
Cdd:PLN03073 567 FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKP 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 456 NVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLR 523
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-510 |
5.60e-57 |
|
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: 186.50 E-value: 5.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQdhahdfedec 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 tlfdwmgqwtqggeqlvrgtlgrmlfsndeilksvkvISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLAL 479
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180 190
....*....|....*....|....*....|.
gi 1502692530 480 ENYPGTLIFVSHDREFVSSLATRIIELSPSG 510
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-524 |
3.05e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 193.74 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHahDFEDECTL 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEP--PLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDW-----------------------------------------MGQWTqgGEQLVRGTLGRMLFSNDEILKSVKVISGG 440
Cdd:COG0488 79 LDTvldgdaelraleaeleeleaklaepdedlerlaelqeefeaLGGWE--AEARAEEILSGLGFPEEDLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 441 EQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDD 520
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSA 236
|
....
gi 1502692530 521 YLRS 524
Cdd:COG0488 237 YLEQ 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-229 |
2.17e-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: 147.98 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQdqfayeeftvldtv 85
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 imgheelwkvkaerdriyslpemteddgmavaeletefaemdgytaesragelllglgigieqhngpmseVSPGWKLRVL 165
Cdd:cd03221 71 ----------------------------------------------------------------------LSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-525 |
1.98e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW------TESAEIGYYAQDHA 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 hdfedectlFDW-----------MGQWTQGGeqlvrgtLGRMLFSND-----EILKSVKV----------ISGGEQGRML 446
Cdd:COG1121 86 ---------VDWdfpitvrdvvlMGRYGRRG-------LFRRPSRADreavdEALERVGLedladrpigeLSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 447 FGKLILQKPNVLVMDEPTNHLDMESIEAL-----NLALENypGTLIFVSHDREFVSSLATRIIELSPSGVidFSGTYDDY 521
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALyellrELRREG--KTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEV 225
|
....
gi 1502692530 522 LRSQ 525
Cdd:COG1121 226 LTPE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
6.56e-33 |
|
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: 125.93 E-value: 6.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLR---------- 70
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-GRDLASLSrrelarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 --QDQFAYEEFTVLDTVIMG---HEELWKVKAERDRiyslpEMTEDdgmAVAELE-TEFAEmdgytaesRagelllglgi 144
Cdd:COG1120 80 vpQEPPAPFGLTVRELVALGrypHLGLFGRPSAEDR-----EAVEE---ALERTGlEHLAD--------R---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 145 gieqhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI-NTIRWLENV--LTQRNSLMIIIS-HDrhfLN---S 217
Cdd:COG1120 134 -------PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLELLrrLARERGRTVVMVlHD---LNlaaR 203
|
250
....*....|...
gi 1502692530 218 VCTHMADLDYGEL 230
Cdd:COG1120 204 YADRLVLLKDGRI 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
7.58e-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: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMlepnvrlgklrqdqfayeeftv 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 ldtvIMGHEELWKVKAERDRIYSLPEmteddgmavaeletEFAEMDGYTAESragelllglgigieqhngpMSEVSPGWK 161
Cdd:cd03230 59 ----VLGKDIKKEPEEVKRRIGYLPE--------------EPSLYENLTVRE-------------------NLKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELlreLKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
328-504 |
1.35e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 119.76 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWT--ESA-EIGYYAQDHAHDFe 396
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSrrELArRIAYVPQEPPAPF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 dECTLFD-----------WMGQWTQGGEQLVRGTLGRMlfsndEIL----KSVKVISGGEQGRMLFGKLILQKPNVLVMD 461
Cdd:COG1120 89 -GLTVRElvalgryphlgLFGRPSAEDREAVEEALERT-----GLEhladRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 462 EPTNHLD-------MESIEALNlalENYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1120 163 EPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-504 |
2.04e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 121.55 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF--GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSG---GQVMLEPNVRLG---KLRQD 72
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLElseALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFAY---EEFTVLDTVIMGHEelwkvkaerdriysLPEMTEDDGMAVAEletefaemdgytAESRAGELLLGLGIGIEQH 149
Cdd:COG1123 84 RIGMvfqDPMTQLNPVTVGDQ--------------IAEALENLGLSRAE------------ARARVLELLEAVGLERRLD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 150 NGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADL 225
Cdd:COG1123 138 RYP-HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 226 DYGELrlfpgnydeymtVATQSREQLLADNAKKKAqiselqsfVSRFSANASKAKQATSRAKQIdkIQLAEVKpssrvsp 305
Cdd:COG1123 217 DDGRI------------VEDGPPEEILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL--LEVRNLS------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 306 fIRFEQTKKLHRQAVvvermakgfdgttlfKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------K 377
Cdd:COG1123 268 -KRYPVRGKGGVRAV---------------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltK 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 378 WTESA------EIGYYAQDHAHDFEDECTLFDWMGQW--TQGG------EQLVRgtlgrmlfsndEILKSVKV------- 436
Cdd:COG1123 332 LSRRSlrelrrRVQMVFQDPYSSLNPRMTVGDIIAEPlrLHGLlsraerRERVA-----------ELLERVGLppdladr 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 437 ----ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMeSIEA--LNLALE---NYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1123 401 ypheLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqiLNLLRDlqrELGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
328-506 |
9.13e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.40 E-value: 9.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK------WTESAEIGYYAQDHAHDFEDECTL 401
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDRDFPISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDW--MGQWTQGGEQLVRGTLGRMLFsnDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:cd03235 88 RDVvlMGLYGHKGLFRRLSKADKAKV--DEALERVGLseladrqigeLSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 470 ESIEAL-----NLALENYpgTLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03235 166 KTQEDIyellrELRREGM--TILVVTHDLGLVLEYFDRVLLL 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-231 |
1.36e-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: 113.80 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVM----------LEPNVRLGKLR 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 QDQFAYEEFTVLDtVIMGHEELWKVKAERDRiyslpemteddgMAVAELETEFaEMDGYtAESRAgelllglgigieqhn 150
Cdd:COG4555 81 DERGLYDRLTVRE-NIRYFAELYGLFDEELK------------KRIEELIELL-GLEEF-LDRRV--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 151 gpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ-RNS-LMIIIS-HDRHFLNSVCTHMADLDY 227
Cdd:COG4555 131 ---GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEgKTVLFSsHIMQEVEALCDRVVILHK 207
|
....
gi 1502692530 228 GELR 231
Cdd:COG4555 208 GKVV 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-240 |
2.61e-28 |
|
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: 118.50 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLrqDQFayeeftv 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV--DQS------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 ldtvimgheelwkvkaeRDRIyslpemteDDGMAVAEL---ETEFAEMDGYTAESRAGELLLGLGIGIEQHNgpMSEVSP 158
Cdd:TIGR03719 394 -----------------RDAL--------DPNKTVWEEisgGLDIIKLGKREIPSRAYVGRFNFKGSDQQKK--VGQLSG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMadLDY---GELRLFPG 235
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFegdSHVEWFEG 524
|
....*
gi 1502692530 236 NYDEY 240
Cdd:TIGR03719 525 NFSEY 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
322-508 |
4.12e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.42 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWT----ESAEIGYYAQ----DHAH 393
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 394 DFEDECTLFDWMGQWTQ-GGEQLVRGTLGRMLfsndEIL-------KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTN 465
Cdd:COG4133 85 GLKPELTVRENLRFWAAlYGLRADREAIDEAL----EAVglagladLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 466 HLDMESIEALNLALENYP---GTLIFVSHDREFVssLATRIIELSP 508
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
5.83e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.10 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV-MLEPNVRLGKLRqdqFAY--- 76
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRARRR---IGYvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 -EEF------TVLDTVIMG---HEELWKV--KAERDRIYSLPEMTeddGMAvaeletEFAemdgytaeSRagelllglgi 144
Cdd:COG1121 83 rAEVdwdfpiTVRDVVLMGrygRRGLFRRpsRADREAVDEALERV---GLE------DLA--------DR---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 145 gieqhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNS---LMIIISHDRHFLNSVCTH 221
Cdd:COG1121 136 -------PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDR 208
|
250 260
....*....|....*....|.
gi 1502692530 222 MADLDYGelRLFPGNYDEYMT 242
Cdd:COG1121 209 VLLLNRG--LVAHGPPEEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
322-508 |
1.14e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.29 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESA-----------EIGYYAQd 390
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 hahdfedECTLFD----------WMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVM 460
Cdd:COG4619 82 -------EPALWGgtvrdnlpfpFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 461 DEPTNHLDMESIEALNLALENYP----GTLIFVSHDREFVSSLATRIIELSP 508
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
2.38e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.11 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPNVRLGKLRQDQFAY-- 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngEPIRDAREDYRRRLAYlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 ------EEFTVLDTVIMgHEELWKVKAERDRIYSLPEmteddGMAVAELETEfaemdgytaesragelllglgigieqhn 150
Cdd:COG4133 82 hadglkPELTVRENLRF-WAALYGLRADREAIDEALE-----AVGLAGLADL---------------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 151 gPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVL---TQRNSLMIIISHDRHFLNSV 218
Cdd:COG4133 128 -PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELAAA 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-465 |
2.45e-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: 107.35 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-----------TESAEIGYYAQDHAHD-----FED- 397
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFprltvRENl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 --ECTLFDWMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTN 465
Cdd:pfam00005 81 rlGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-506 |
2.74e-27 |
|
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: 107.87 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK------WTESAE----IGYYAQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEEvkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMgqwtqggeqlvrgtlgrmlfSNDEILKsvkvISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:cd03230 81 EPS--------LYENL--------------------TVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 470 ESIEAL-----NLALENypGTLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03230 129 ESRREFwellrELKKEG--KTILLSSHILEEAERLCDRVAIL 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
328-522 |
3.14e-27 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 115.82 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES-------------------------- 381
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegtvydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 382 AEIGYYAQDH---AHDFEDECT--LFDWMGQW-----TQGGEQL---VRGTLGRMLFSNDEILKSvkvISGGEQGRMLFG 448
Cdd:PRK11147 92 EEQAEYLKRYhdiSHLVETDPSekNLNELAKLqeqldHHNLWQLenrINEVLAQLGLDPDAALSS---LSGGWLRKAALG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 449 KLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYL 522
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
322-520 |
2.25e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 107.64 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--TESAEIGYYAQDHAHDFEDEC 399
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLFDWM-------------GQWTQGGEQLVRGTLGRMLFSNDeILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:COG4555 84 GLYDRLtvreniryfaelyGLFDEELKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 467 LDMESIEALN---LALENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDD 520
Cdd:COG4555 163 LDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLDE 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-253 |
3.12e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.69 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML----------EPNVRLGKLRQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTV-IMGheelwkvkaerdRIYSLPEMTEDDgmAVAELeTEFAEMDGYTaesragelllglgigieqhN 150
Cdd:COG1131 81 EPALYPDLTVRENLrFFA------------RLYGLPRKEARE--RIDEL-LELFGLTDAA-------------------D 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 151 GPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHDRHFLNSVCTHMADLDY 227
Cdd:COG1131 127 RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRElaaEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
250 260
....*....|....*....|....*.
gi 1502692530 228 GELrlfpgnydeymtVATQSREQLLA 253
Cdd:COG1131 207 GRI------------VADGTPDELKA 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-221 |
7.33e-26 |
|
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: 105.31 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLepnvrLGK---LRQDQFAY----EE 78
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV-----FGKpleKERKRIGYvpqrRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 F------TVLDTVIMG---HEELWKV--KAERDRIYSLPEMTeddGMavaeleTEFAEMdgytaesragelllglgigie 147
Cdd:cd03235 79 IdrdfpiSVRDVVLMGlygHKGLFRRlsKADKAKVDEALERV---GL------SELADR--------------------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 148 qhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRW---LENVLTQRNSLMIIISHDrhfLNSVCTH 221
Cdd:cd03235 129 ----QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHD---LGLVLEY 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-229 |
7.76e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.48 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLrqdqfayeeftvldtv 85
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKL---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 imgheelwKVKAERDRIYSLPEMteddgmavaeletefaemdgytaesragelllglgigieqhngpmsevSPGWKLRVL 165
Cdd:cd00267 67 --------PLEELRRRIGYVPQL------------------------------------------------SGGQRQRVA 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd00267 91 LARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
322-506 |
1.43e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.71 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAeigyyaqdhahdfedectl 401
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 fdwmgqWTQGGEQLVRGTLGrMLFSndeilksvkvISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALEN 481
Cdd:cd00267 63 ------IAKLPLEELRRRIG-YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180
....*....|....*....|....*...
gi 1502692530 482 YPG---TLIFVSHDREFVSSLATRIIEL 506
Cdd:cd00267 126 LAEegrTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
322-504 |
4.62e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA---EIGYYAQd 390
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSPKElarKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 hahdfedectlfdWMGQWtqGGEQLVRgtlgrmlfsndeilKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD-- 468
Cdd:cd03214 81 -------------ALELL--GLAHLAD--------------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDia 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1502692530 469 -----MESIEALNlalENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03214 132 hqielLELLRRLA---RERGKTVVMVLHDLNLAARYADRVI 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-502 |
1.14e-24 |
|
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: 107.20 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGG--DLEPSGGQVM-----------LEPNVRLG- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvalcekcgyVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 68 ---------------------KLR-----------QDQFA-YEEFTVLDTVIMGHEEL-WKVKAERDRIYSLPEMT--ED 111
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdKLRrrirkriaimlQRTFAlYGDDTVLDNVLEALEEIgYEGKEAVGRAVDLIEMVqlSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 112 DGMAVAEletefaemdgytaesragelllglgigieqhngpmsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTI 191
Cdd:TIGR03269 161 RITHIAR------------------------------------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 192 RWLENVLTQ----RNSLMIIISHDRHFLNSVCTHMADLDYGELRlfpgnydeymtvatqsreqlladnakkkaQISELQS 267
Cdd:TIGR03269 205 KLVHNALEEavkaSGISMVLTSHWPEVIEDLSDKAIWLENGEIK-----------------------------EEGTPDE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 268 FVSRFSANASKAKQATsrakqidKIQLAEvkpssrvsPFIRFEQTKKLHrqaVVVER-MAKGFDGTtlfkdfSFTVEASE 346
Cdd:TIGR03269 256 VVAVFMEGVSEVEKEC-------EVEVGE--------PIIKVRNVSKRY---ISVDRgVVKAVDNV------SLEVKEGE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 347 RVAIIGPNGIGKTTLLRTLVNELTPDAGSI------KWTESAEIGYYAQDHAHDF----EDECTLF---DWMGQWTQGGE 413
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGPDGRGRAKRYigilHQEYDLYphrTVLDNLTEAIG 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 414 QLVRGTLGRML---------FSND---EIL-KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD----MESIEALN 476
Cdd:TIGR03269 392 LELPDELARMKavitlkmvgFDEEkaeEILdKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSIL 471
|
570 580
....*....|....*....|....*.
gi 1502692530 477 LALENYPGTLIFVSHDREFVSSLATR 502
Cdd:TIGR03269 472 KAREEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
1.50e-24 |
|
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: 97.26 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 223 ADLDYGELRLFPGNYDEYMTVATQSREQLLADNAKKKAQISELQSFVSRFSANASKAKQATSRAKQIDKIQlaEVKPSSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKME--RIEKPER 78
|
....*..
gi 1502692530 303 VSPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-240 |
4.22e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.97 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGqvmlepnvrlgklrqdqfayeEFTVLDTV 85
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG---------------------TIKIGETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMGHeelwkVKAERDRIyslpemteDDGMAVAEL---ETEFAEMDGYTAESRAGELLLGLGIGIEQHngPMSEVSPGWKL 162
Cdd:PRK11819 388 KLAY-----VDQSRDAL--------DPNKTVWEEisgGLDIIKVGNREIPSRAYVGRFNFKGGDQQK--KVGVLSGGERN 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMadLDY---GELRLFPGNYDE 239
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFegdSQVEWFEGNFQE 530
|
.
gi 1502692530 240 Y 240
Cdd:PRK11819 531 Y 531
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-510 |
4.49e-23 |
|
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: 95.68 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNELTPdagsikWTeSAEIGYYaqdhahdfEDECTLFdwMGQWT 409
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWP------WG-SGRIGMP--------EGEDLLF--LPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 410 QggeqLVRGTLGRMLfsndeILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFV 489
Cdd:cd03223 74 Y----LPLGTLREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
170 180
....*....|....*....|.
gi 1502692530 490 SHdREFVSSLATRIIELSPSG 510
Cdd:cd03223 145 GH-RPSLWKFHDRVLDLDGEG 164
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
331-526 |
6.13e-23 |
|
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: 102.54 E-value: 6.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA---EIGYYAQDhAHDF---- 395
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIAVVPQR-PHLFdttl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 ------------EDECT-------LFDWMGQWTQGGEQLVrGTLGRMLfsndeilksvkviSGGEQGRMLFGKLILQKPN 456
Cdd:COG4987 426 renlrlarpdatDEELWaalervgLGDWLAALPDGLDTWL-GEGGRRL-------------SGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 457 VLVMDEPTNHLDMESIEA-LNLALENYPG-TLIFVSHDREFVsSLATRIIELSpSGVIDFSGTYDDYLRSQG 526
Cdd:COG4987 492 ILLLDEPTEGLDAATEQAlLADLLEALAGrTVLLITHRLAGL-ERMDRILVLE-DGRIVEQGTHEELLAQNG 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
330-527 |
7.52e-23 |
|
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: 102.60 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-------------WTESaeIGYYAQDhahdfe 396
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRRQ--IGVVLQD------ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 deCTLFdwmgqwtqggeqlvRGT------LGRMLFSNDEILKSVKV------------------------ISGGEQGRML 446
Cdd:COG2274 558 --VFLF--------------SGTirenitLGDPDATDEEIIEAARLaglhdfiealpmgydtvvgeggsnLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 447 FGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPG--TLIFVSHDREFVsSLATRIIELSpSGVIDFSGTYDDYLRS 524
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLD-KGRIVEDGTHEELLAR 699
|
...
gi 1502692530 525 QGV 527
Cdd:COG2274 700 KGL 702
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-526 |
3.20e-22 |
|
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: 100.22 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--TESAEIgyyaqdhahDFEDECTLFDWMGQ 407
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngVDLSDL---------DPASWRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 wtqgGEQLVRGT------LGRMLFSNDEILKSVK------VISG---------GEQGRMLFG---------KLILQKPNV 457
Cdd:COG4988 419 ----NPYLFAGTirenlrLGRPDASDEELEAALEaagldeFVAAlpdgldtplGEGGRGLSGgqaqrlalaRALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 458 LVMDEPTNHLDMESIEALNLALENYPG--TLIFVSHDREFVsSLATRIIELSpSGVIDFSGTYDDYLRSQG 526
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVLD-DGRIVEQGTHEELLAKNG 563
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-525 |
3.44e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.52 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK------WTESAE----IGYYAQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMgqwTqGGEQL-----VRGTLGRMLFSN-DEIL----------KSVKVISGGEQGRMLFGKLILQ 453
Cdd:COG1131 81 EPA--------LYPDL---T-VRENLrffarLYGLPRKEARERiDELLelfgltdaadRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEAL-----NLALENypGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDyLRSQ 525
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELwellrELAAEG--KTVLLSTHYLEEAERLCDRVAIID-KGRIVADGTPDE-LKAR 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-504 |
3.57e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 93.79 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-------------TESAEIGYYA 388
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAhdfedectLFDWMGqwtqggeqlVRGTLGRMLfsndeilksvkviSGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:cd03229 83 QDFA--------LFPHLT---------VLENIALGL-------------SGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1502692530 469 ME---SIEALNLAL-ENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03229 133 PItrrEVRALLKSLqAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-211 |
4.33e-22 |
|
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: 93.27 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFAyeeftvldtv 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 imgheelwkvkaeRDRIYsLPEMteddgMAVAELEtEFAEmdgytaesRagelllglgigieqhngPMSEVSPGWKLRVL 165
Cdd:cd03214 73 -------------RKIAY-VPQA-----LELLGLA-HLAD--------R-----------------PFNELSGGERQRVL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDI-NTIRWLENV--LTQRNSLMIIIS-HD 211
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIaHQIELLELLrrLARERGKTVVMVlHD 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
330-506 |
4.52e-22 |
|
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: 93.22 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW---------TES--AEIGYYAQDhahdfede 398
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdlrdldLESlrKNIAYVPQD-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 CTLFDwmgqwtqggeqlvrGTLGrmlfsnDEILksvkviSGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLA 478
Cdd:cd03228 85 PFLFS--------------GTIR------ENIL------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|
gi 1502692530 479 LENYPG--TLIFVSHDREFVsSLATRIIEL 506
Cdd:cd03228 139 LRALAKgkTVIVIAHRLSTI-RDADRIIVL 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-504 |
6.53e-22 |
|
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: 99.47 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 31 GLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNvrlgklrqdqfaYEEftVLD----TVImgHEELWKVKAERDR----- 101
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPS------------WDE--VLKrfrgTEL--QDYFKKLANGEIKvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 102 --IYSLPE----------MTEDDGMAVAELETEFaEMDGYTaesragelllglgigieqhNGPMSEVSPGWKLRVLLAQA 169
Cdd:COG1245 167 qyVDLIPKvfkgtvrellEKVDERGKLDELAEKL-GLENIL-------------------DRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 170 LFSDPEVLLLDEPTNHLDIN-------TIRwlEnvLTQRNSLMIIISHDrhflnsvcthMADLD---------YGElrlf 233
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYqrlnvarLIR--E--LAEEGKYVLVVEHD----------LAILDyladyvhilYGE---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 234 PGNYDeymtVATQSReqlladnaKKKAQISE-LQSFVS----RFsanaskakqatsRAKQIDkiqlAEVKPSSRVspfir 308
Cdd:COG1245 289 PGVYG----VVSKPK--------SVRVGINQyLDGYLPeenvRI------------RDEPIE----FEVHAPRRE----- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 309 fEQTKKLhrqaVVVERMAKGFDGttlfkdFSFTVEA-----SERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKwtESAE 383
Cdd:COG1245 336 -KEEETL----VEYPDLTKSYGG------FSLEVEGgeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 384 IGYYAQDHAHDFEDECtlfdwmgqwtqggEQLVRGTLGRMLFS---NDEIL----------KSVKVISGGEQGRMLFGKL 450
Cdd:COG1245 403 ISYKPQYISPDYDGTV-------------EEFLRSANTDDFGSsyyKTEIIkplgleklldKNVKDLSGGELQRVAIAAC 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMEsiEALNLA------LENYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVE--QRLAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
334-522 |
7.25e-22 |
|
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: 98.85 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQ----DHAHD--------------- 394
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQepqlDPTKTvrenveegvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 395 ----------FEDECTLFDWMGQwTQGG-EQLVRGTLGRMLFSNDEI----LK------SVKVISGGEQGRMLFGKLILQ 453
Cdd:TIGR03719 100 ldrfneisakYAEPDADFDKLAA-EQAElQEIIDAADAWDLDSQLEIamdaLRcppwdaDVTKLSGGERRRVALCRLLLS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYL 522
Cdd:TIGR03719 179 KPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 247
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-506 |
8.33e-22 |
|
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: 92.28 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA---EIGYYAQDhahdfeDEctLF 402
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGYLPQD------DE--LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 403 DwmgqwtqggeqlvrGTLgrmlfsNDEILksvkviSGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENY 482
Cdd:cd03246 89 S--------------GSI------AENIL------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL 142
|
170 180
....*....|....*....|....*..
gi 1502692530 483 P---GTLIFVSHDREFVSSlATRIIEL 506
Cdd:cd03246 143 KaagATRIVIAHRPETLAS-ADRILVL 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-526 |
1.01e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 99.09 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQ------------------------ 389
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgdreyrqle 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 ---DHAHDFEDECTL------FDWMGQWT--QGGEQLVRGtLGrmlFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVL 458
Cdd:PRK10636 96 aqlHDANERNDGHAIatihgkLDAIDAWTirSRAASLLHG-LG---FSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 459 VMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLRSQG 526
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-506 |
1.31e-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: 92.71 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI----KWTESAE----IGYYAQDHAHDF-----E 396
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngKPIKAKErrksIGYVMQDVDYQLftdsvR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 DECTLFDwmgQWTQGGEQLVRGTLGRMlfsNDEILKSV--KVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD---MES 471
Cdd:cd03226 91 EELLLGL---KELDAGNEQAETVLKDL---DLYALKERhpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMER 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1502692530 472 IEALNLALENYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-504 |
3.72e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 91.81 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI-----KWT----ESAEIGYYAQD 390
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrDVTgvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 HAhdfedectLFDWMGQWtqggEQLVRGtLGRMLFSNDEILKSVKVI-----------------SGGEQGRMLFGKLILQ 453
Cdd:cd03259 81 YA--------LFPHLTVA----ENIAFG-LKLRGVPKAEIRARVRELlelvglegllnryphelSGGQQQRVALARALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEALNLALENYPG----TLIFVSHDREFVSSLATRII 504
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
6.21e-21 |
|
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: 90.99 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQ----------DQFAYE 77
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdlTKLSLKELRRkvglvfqnpdDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 efTVLDTVIMGHEELwkvkaerdriySLPEmtEDDGMAVAELETEFaEMDGYTAEsragelllglgigieqhngPMSEVS 157
Cdd:cd03225 92 --TVEEEVAFGLENL-----------GLPE--EEIEERVEEALELV-GLEGLRDR-------------------SPFTLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 158 PGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSL---MIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-230 |
1.42e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.88 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGKLRQD--------Q 73
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-----GKPLSAmpppewrrQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 74 FAY---EEFTVLDTVImghEELWKVKAERDRIYSLPEMTEDdgMAVAELETEFAEMdgytaesragelllglgigieqhn 150
Cdd:COG4619 76 VAYvpqEPALWGGTVR---DNLPFPFQLRERKFDRERALEL--LERLGLPPDILDK------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 151 gPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLD 226
Cdd:COG4619 127 -PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
....
gi 1502692530 227 YGEL 230
Cdd:COG4619 206 AGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-523 |
2.02e-20 |
|
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: 90.08 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW----TESAEIGYYAQ---------DHahdfe 396
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkdITKKNLRELRRkvglvfqnpDD----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 dectlfdwmgqwtqggeQLVRGT--------LGRMLFSNDEILKSVKVI-----------------SGGEQGRM-LFGKL 450
Cdd:COG1122 87 -----------------QLFAPTveedvafgPENLGLPREEIRERVEEAlelvglehladrpphelSGGQKQRVaIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 451 ILQkPNVLVMDEPTNHLDMESIEALNLALENYPG---TLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDYLR 523
Cdd:COG1122 150 AME-PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLD-DGRIVADGTPREVFS 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
2.05e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAHDFEDECTLFDW--M 405
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLvaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 GQWTQggeqlvRGTLGRMLFSN----DEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMES 471
Cdd:NF040873 81 GRWAR------RGLWRRLTRDDraavDDALERVGLadlagrqlgeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1502692530 472 IEALNLALENYPG---TLIFVSHDREFVSSlATRIIEL 506
Cdd:NF040873 155 RERIIALLAEEHArgaTVVVVTHDLELVRR-ADPCVLL 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
2.51e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.48 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGP-KPLfENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 ---------YEEFTVLDTVIMGHEE------------LWKVKAERDRIyslpemtEDDGMAVAeletEFAEMDGYtAESR 134
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAAHArlgrgllaallrLPRARREEREA-------RERAEELL----ERVGLADR-ADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 135 AgelllglgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPT---NHLD----INTIRWL--ENVLTqrnslM 205
Cdd:COG0411 150 A------------------GNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEEteelAELIRRLrdERGIT-----I 206
|
250 260
....*....|....*....|....*
gi 1502692530 206 IIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:COG0411 207 LLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
2.52e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.80 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 -------YEEFTVLDTVIMGHEElwkvkAERDRIYSLPEMTEDDgmAVAELETEFAEMDGYTAESRAgelllglgigieq 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVAAQA-----RTGSGLLLARARREER--EARERAEELLERVGLADLADR------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 149 hngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPT---NHLDIN-TIRWLENvLTQRNSLMIIISHDRHFLNSVCTHMAD 224
Cdd:cd03219 140 ---PAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHDMDVVMSLADRVTV 215
|
....*.
gi 1502692530 225 LDYGEL 230
Cdd:cd03219 216 LDQGRV 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
2.74e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 11 FGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQ-----DQFAyeeFTVLDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLP---LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMGheeLWKvkaerdRIYSLPEMTEDDGMAVAE-LE----TEFAemdgytaesragelllglgigieqhNGPMSEVSPGW 160
Cdd:NF040873 79 AMG---RWA------RRGLWRRLTRDDRAAVDDaLErvglADLA-------------------------GRQLGELSGGQ 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 161 KLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHDRH 213
Cdd:NF040873 125 RQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEehaRGATVVVVTHDLE 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
332-507 |
3.56e-20 |
|
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: 89.06 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 332 TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE-----------SAEIGYYAQDHAHDF----- 395
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelRRKVGLVFQNPDDQFfgptv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 EDEctLFDWMGQWTQGGEQLVRGTLGRMLFSNDEIL--KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIE 473
Cdd:cd03225 94 EEE--VAFGLENLGLPEEEIEERVEEALELVGLEGLrdRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1502692530 474 AL-----NLALENYpgTLIFVSHDREFVSSLATRIIELS 507
Cdd:cd03225 172 ELlellkKLKAEGK--TIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
3.57e-20 |
|
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: 86.93 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 17 FENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-----------PNVRLGKLRQDQFAYEEFTVLDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMGheelwkvkaerDRIYSLPEMTEDDGMAVAelETEFAEMDgyTAESRAGElllglgigieqhngPMSEVSPGWKLRVL 165
Cdd:pfam00005 81 RLG-----------LLLKGLSKREKDARAEEA--LEKLGLGD--LADRPVGE--------------RPGTLSGGQRQRVA 131
|
170
....*....|....*....
gi 1502692530 166 LAQALFSDPEVLLLDEPTN 184
Cdd:pfam00005 132 IARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-230 |
5.43e-20 |
|
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: 88.93 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQ----------DQFAYE 77
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglvfqnpdDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 efTVLDTVIMGHEELWKVKAE-RDRIyslpemteDDGMAVAELEtEFAEMdgytaesragelllglgigieqhngPMSEV 156
Cdd:COG1122 92 --TVEEDVAFGPENLGLPREEiRERV--------EEALELVGLE-HLADR-------------------------PPHEL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-228 |
5.64e-20 |
|
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: 88.08 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKP-LFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYeeftVLDT 84
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGY----VMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 85 VimgHEELWKVKAERDRIYSLPEMTEDDGMAVAELETefaeMDGYTAESRagelllglgigieqHngPMSeVSPGWKLRV 164
Cdd:cd03226 80 V---DYQLFTDSVREELLLGLKELDAGNEQAETVLKD----LDLYALKER--------------H--PLS-LSGGQKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 165 LLAQALFSDPEVLLLDEPTNHLDintiRW-LENV------LTQRNSLMIIISHDRHFLNSVCT---HMADLDYG 228
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLD----YKnMERVgelireLAAQGKAVIVITHDYEFLAKVCDrvlLLANGAIV 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-504 |
6.31e-20 |
|
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: 88.42 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--TESAE---------IGYYAQDhahdfedectlfdw 404
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgTDIRQldpadlrrnIGYVPQD-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 405 mgqwtqggEQLVRGTL------GRMLFSNDEILKSVKvISG----------------GEQGRMLFG---------KLILQ 453
Cdd:cd03245 87 --------VTLFYGTLrdnitlGAPLADDERILRAAE-LAGvtdfvnkhpngldlqiGERGRGLSGgqrqavalaRALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEALNLALENYPG--TLIFVSHdREFVSSLATRII 504
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRII 209
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-230 |
7.48e-20 |
|
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: 89.10 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 5 ANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----------EPNVRLGKLRQDQ 73
Cdd:TIGR03873 5 SRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLagvdlhglsrrARARRVALVEQDS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 74 FAYEEFTVLDTVIMG---HEELWKVKAERDRiyslpEMTeDDGMAVAELeTEFAEMDgytaesragelllglgigieqhn 150
Cdd:TIGR03873 85 DTAVPLTVRDVVALGripHRSLWAGDSPHDA-----AVV-DRALARTEL-SHLADRD----------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 151 gpMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDIN----TIRWLENVLTQRNSLMIIIsHDRHFLNSVCTHMADLD 226
Cdd:TIGR03873 135 --MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRaqleTLALVRELAATGVTVVAAL-HDLNLAASYCDHVVVLD 211
|
....
gi 1502692530 227 YGEL 230
Cdd:TIGR03873 212 GGRV 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
330-510 |
7.51e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 7.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvneltpdAGsIkWTesaeigyYAQDHAHDFEDECTLFdwMGQwt 409
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AG-L-WP-------YGSGRIARPAGARVLF--LPQ-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 410 qggeqlvR-----GTLGRML--------FSNDEI---LKSV----------------KVISGGEQGRMLFGKLILQKPNV 457
Cdd:COG4178 434 -------RpylplGTLREALlypataeaFSDAELreaLEAVglghlaerldeeadwdQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 458 LVMDEPTNHLDMESIEALnLAL--ENYPG-TLIFVSHdREFVSSLATRIIELSPSG 510
Cdd:COG4178 507 LFLDEATSALDEENEAAL-YQLlrEELPGtTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
434-522 |
1.17e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 92.10 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 434 VKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVID 513
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
....*....
gi 1502692530 514 FSGTYDDYL 522
Cdd:PRK11819 241 WEGNYSSWL 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-504 |
1.19e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.18 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 31 GLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNvrlgklrqdqfaYEEftVLD----TVImgHEELWKVKAERDRIYSLP 106
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPS------------WDE--VLKrfrgTEL--QNYFKKLYNGEIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 107 EMTED-----DGMAVAELETefaemdgyTAESRAGELLLGLGIGIEQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDE 181
Cdd:PRK13409 167 QYVDLipkvfKGKVRELLKK--------VDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 182 PTNHLDI-------NTIRWLenvltQRNSLMIIISHDrhflnsvcthMADLD---------YGElrlfPGNYDeymtVAT 245
Cdd:PRK13409 239 PTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHD----------LAVLDyladnvhiaYGE----PGAYG----VVS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 246 QSReqlladnaKKKAQISE-LQSFVS----RFsanaskakqatsrakqidkiqlaevkpssRVSPfIRFEqtKKLHRQAV 320
Cdd:PRK13409 296 KPK--------GVRVGINEyLKGYLPeenmRI-----------------------------RPEP-IEFE--ERPPRDES 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 321 VVERMAKGFDGTTLFKDFSFTVEA-----SERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTEsaEIGYYAQDHAHDF 395
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KISYKPQYIKPDY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 EDECTLF------DWMGQWTQggEQLVRGtlgrmlFSNDEIL-KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:PRK13409 414 DGTVEDLlrsitdDLGSSYYK--SEIIKP------LQLERLLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1502692530 469 MEsiEALNLA------LENYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK13409 486 VE--QRLAVAkairriAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
322-525 |
1.74e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 87.56 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----WTESAEIGYYA-------- 388
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSEAELYRlrrrmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 -QDHAhdfedectLFD----------WMGQWTQGGE----QLVRGTLGRMLFSNDEILKSVKvISGGEQGRMLFGKLILQ 453
Cdd:cd03261 83 fQSGA--------LFDsltvfenvafPLREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 454 KPNVLVMDEPTNHLD---MESIEALNLAL-ENYPGTLIFVSHDREFVSSLATRIIELSPSGVIdFSGTYDDYLRSQ 525
Cdd:cd03261 154 DPELLLYDEPTAGLDpiaSGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRASD 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-241 |
1.88e-19 |
|
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: 91.82 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGP--KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQdQFAY--- 76
Cdd:COG2274 478 NVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgidlRQIDPASLRR-QIGVvlq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 EEF----TVLDTVIMGHeelwkvkaerdriyslPEMTEDDGMAVAE---LETEFAEM-DGYtaesragelllglgigieq 148
Cdd:COG2274 557 DVFlfsgTIRENITLGD----------------PDATDEEIIEAARlagLHDFIEALpMGY------------------- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 149 hNGPMSE----VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHDRHFLNsvcthM 222
Cdd:COG2274 602 -DTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR-----L 675
|
250 260
....*....|....*....|...
gi 1502692530 223 AD----LDYGELRLFpGNYDEYM 241
Cdd:COG2274 676 ADriivLDKGRIVED-GTHEELL 697
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
304-494 |
2.03e-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: 87.83 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 304 SPFIRFEQtkklhrqaVVVERmakgfDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAG--------- 374
Cdd:COG1119 1 DPLLELRN--------VTVRR-----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfger 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 375 ----SIkWTESAEIGYYAQDHAHDFEDECT--------LFDWMGQWTQGGE---QLVRGTLGRMlfsndEIL----KSVK 435
Cdd:COG1119 68 rggeDV-WELRKRIGLVSPALQLRFPRDETvldvvlsgFFDSIGLYREPTDeqrERARELLELL-----GLAhladRPFG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 436 VISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALN-----LALENYPgTLIFVSHDRE 494
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLalldkLAAEGAP-TLVLVTHHVE 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
7.15e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----------EPNVRLGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladwspaELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQD---QFAyeeFTVLDTVIMGHEELWKVKAERDRIYslpemteDDGMAVAELeTEFAEMDgYTaesragelllglgigi 146
Cdd:PRK13548 82 PQHsslSFP---FTVEEVVAMGRAPHGLSRAEDDALV-------AAALAQVDL-AHLAGRD-YP---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 147 eqhngpmsEVSPGWKLRVLLAQAL------FSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSLMIIISHDrhfLN 216
Cdd:PRK13548 134 --------QLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LN 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
322-508 |
1.02e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 84.83 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDG----TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------KWTESAEIGYYAQDH 391
Cdd:cd03293 3 VRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 AhdfedectLFDWM-----------GQWTQGGEQLVRGtlgrmlfsnDEILKSV----------KVISGGEQGRMLFGKL 450
Cdd:cd03293 83 A--------LLPWLtvldnvalgleLQGVPKAEARERA---------EELLELVglsgfenaypHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMESIEALNLAL----ENYPGTLIFVSHDREFVSSLATRIIELSP 508
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-289 |
1.06e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.62 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGqvmlepNVRLG-KLRQ---DQFAYE---E 78
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG------RIHCGtKLEVayfDQHRAEldpE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 FTVLDTVIMGHEELwKVKAeRDRiYSLpemteddgmavaeletefaemdGYTAE-----SRAGElllglgigieqhngPM 153
Cdd:PRK11147 398 KTVMDNLAEGKQEV-MVNG-RPR-HVL----------------------GYLQDflfhpKRAMT--------------PV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 154 SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISHDRHFL-NSVCTHMADLDYGELRL 232
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGR 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 233 FPGNYDEymtvATQSREQLLADNAKKKAQISElqsfvsrfsANASKAKQATSRAKQI 289
Cdd:PRK11147 519 YVGGYHD----ARQQQAQYLALKQPAVKKKEE---------AAAPKAETVKRSSKKL 562
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-216 |
1.25e-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: 89.05 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQD----QFAYEE-----F--TVL 82
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPAswrrQIAWVPqnpylFagTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 DTVIMGH-----EELWKVkAER----DRIYSLPemtedDGmavaeLETEFAEmdgytaesragelllglgigieqhNGpm 153
Cdd:COG4988 429 ENLRLGRpdasdEELEAA-LEAagldEFVAALP-----DG-----LDTPLGE------------------------GG-- 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 154 SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHDRHFLN 216
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLALLA 536
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-232 |
1.85e-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: 83.81 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML---------EPNVRLGKLRQD 72
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgksyqkniEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFAYEEFTvldtvimGHEELwKVKAerdRIYSLPEMTEDDGMAVAELETEfaemdgytaESRagelllglgigieqhngP 152
Cdd:cd03268 81 PGFYPNLT-------ARENL-RLLA---RLLGIRKKRIDEVLDVVGLKDS---------AKK-----------------K 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 MSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLEN---VLTQRNSLMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03268 124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
...
gi 1502692530 230 LRL 232
Cdd:cd03268 204 LIE 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
2.51e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 83.71 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFG--PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML----------EPNVRLGKL 69
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysirtdrkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDtvimgHEELWKvkaerdRIYSLPEMTEDDGMAVAELETEFAEmdgytaesragelllglgigieQH 149
Cdd:cd03263 81 PQFDALFDELTVRE-----HLRFYA------RLKGLPKSEIKEEVELLLRVLGLTD----------------------KA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 150 NGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVL--TQRNSLMIIISHDRHFLNSVCTHMADLDY 227
Cdd:cd03263 128 NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLIleVRKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
....
gi 1502692530 228 GELR 231
Cdd:cd03263 208 GKLR 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-254 |
2.57e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.47 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPK----PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 -QFAYEE--------FTVLDTVimgheelwkvkAERDRIYSLPEMTE--DDGMAVAELETEFaeMDGYtaesragelllg 141
Cdd:COG1124 81 vQMVFQDpyaslhprHTVDRIL-----------AEPLRIHGLPDREEriAELLEQVGLPPSF--LDRY------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 142 lgigieqhngpMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRhflnS 217
Cdd:COG1124 136 -----------PHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDL----A 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1502692530 218 VCTHMAD----LDYGELrlfpgnydeymtVATQSREQLLAD 254
Cdd:COG1124 201 VVAHLCDrvavMQNGRI------------VEELTVADLLAG 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-233 |
4.35e-18 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 83.01 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGnRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnvrlgklrqdqfayeeftv 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 ldtVIMGHEELWKVKAERDRIYSLP-EMTEDDGMAVAELETEFAEMDGYTA-ESRAGELLLGLGIGIEQH-NGPMSEVSP 158
Cdd:cd03264 57 ---RIDGQDVLKQPQKLRRRIGYLPqEFGVYPNFTVREFLDYIAWLKGIPSkEVKARVDEVLELVNLGDRaKKKIGSLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDI-NTIRwLENVLTQ--RNSLMIIISHDRHFLNSVCTHMADLDYGELRLF 233
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIR-FRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-503 |
5.66e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 82.80 E-value: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWT-------ESAE----IGYYA 388
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA-TVaghdvvrEPREvrrrIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAHDfeDECTLFD---WMG--------QWTQGGEQLVRGtLGRMLFSNdeilKSVKVISGGEQGRMLFGKLILQKPNV 457
Cdd:cd03265 80 QDLSVD--DELTGWEnlyIHArlygvpgaERRERIDELLDF-VGLLEAAD----RLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 458 LVMDEPTNHLDMES-------IEALNlalENYPGTLIFVSHDREFVSSLATRI 503
Cdd:cd03265 153 LFLDEPTIGLDPQTrahvweyIEKLK---EEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
7.36e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV-----------RLGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTVIMG---HEELWKVKAERDRiyslpeMTEDDGMAVAELeTEFAEMdgytaesragelllglgigi 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWGRLSAEDN------ARVNQAMEQTRI-NHLADR-------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 147 eqhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNS---LMIIISHDrhfLNSV---CT 220
Cdd:PRK11231 135 -----RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHD---LNQAsryCD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1502692530 221 HMADLDYGELrLFPGNYDEYMTvatqsrEQLLADNAKKKAQI 262
Cdd:PRK11231 207 HLVVLANGHV-MAQGTPEEVMT------PGLLRTVFDVEAEI 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-239 |
1.15e-17 |
|
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: 82.16 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQD--------- 72
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 ----QFA--YEEFTVLDTVImgheelwkvkaerdriYSLPEMTEDDGMAVAELETEFAEMDGYTAEsragelllglgigi 146
Cdd:cd03261 80 gmlfQSGalFDSLTVFENVA----------------FPLREHTRLSEEEIREIVLEKLEAVGLRGA-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 147 eQHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTIRWLENVLTQRNSL---MIIISHDRHFLNSVCTHM 222
Cdd:cd03261 130 -EDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSLKKELgltSIMVTHDLDTAFAIADRI 207
|
250
....*....|....*..
gi 1502692530 223 ADLDYGELrLFPGNYDE 239
Cdd:cd03261 208 AVLYDGKI-VAEGTPEE 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-525 |
1.21e-17 |
|
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: 82.33 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--------TESA------EI 384
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglSEKElyelrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 385 GYYAQDHAhdfedectLFDWMgqwtqggeqlvrgTLG-------RMLF--SNDEILKSVKV-----------------IS 438
Cdd:COG1127 85 GMLFQGGA--------LFDSL-------------TVFenvafplREHTdlSEAEIRELVLEklelvglpgaadkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 439 GGEQgrmlfgK-------LILQkPNVLVMDEPTNHLD---MESIEALNLAL-ENYPGTLIFVSHDREFVSSLATRIIELS 507
Cdd:COG1127 144 GGMR------KrvalaraLALD-PEILLYDEPTAGLDpitSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLA 216
|
250
....*....|....*...
gi 1502692530 508 pSGVIDFSGTYDDYLRSQ 525
Cdd:COG1127 217 -DGKIIAEGTPEELLASD 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-512 |
1.48e-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: 82.16 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQ-DHAHDFedectlfdwm 405
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF-DGRPVTRRRRkAFRRRV---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 gqwtqggeQLV----------RGTLGRML--------FSN-----DEILKSVKV-----------ISGGEQGRMLFGKLI 451
Cdd:COG1124 82 --------QMVfqdpyaslhpRHTVDRILaeplrihgLPDreeriAELLEQVGLppsfldryphqLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 452 LQKPNVLVMDEPTNHLDMeSIEALNLAL-----ENYPGTLIFVSHDREFVSSLATRIIELsPSGVI 512
Cdd:COG1124 154 ILEPELLLLDEPTSALDV-SVQAEILNLlkdlrEERGLTYLFVSHDLAVVAHLCDRVAVM-QNGRI 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.51e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.44 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF----GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML------EPNVRLGklr 70
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 qdqFAYEEF------TVLDTVIMGHEELWKVKAERDRIyslpemteddgmAVAELE----TEFAemDGYtaesragelll 140
Cdd:COG1116 84 ---VVFQEPallpwlTVLDNVALGLELRGVPKAERRER------------ARELLElvglAGFE--DAY----------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 141 glgigieqhngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIR----WLENVLTQRNSLMIIISHD 211
Cdd:COG1116 136 -----------P-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRErlqdELLRLWQETGKTVLFVTHD 198
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-509 |
1.80e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.06 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGF----DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE------SAEIGYYA 388
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAhdfedectLFDWM-----------GQWTQGGEQLVRGtlgrmlfsnDEILKSV----------KVISGGEQ----- 442
Cdd:COG1116 87 QEPA--------LLPWLtvldnvalgleLRGVPKAERRERA---------RELLELVglagfedaypHQLSGGMRqrvai 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 443 GRMLfgkliLQKPNVLVMDEPTNHLDMESIEALN---LAL-ENYPGTLIFVSHD-REFVsSLATRIIELSPS 509
Cdd:COG1116 150 ARAL-----ANDPEVLLMDEPFGALDALTRERLQdelLRLwQETGKTVLFVTHDvDEAV-FLADRVVVLSAR 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
2.98e-17 |
|
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: 81.18 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQD-------- 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 -----QFA--YEEFTVLDTVIMGHEELWKV-KAERDRIyslpemteddgmavAELETEFAEMDGytAESRagelllglgi 144
Cdd:COG1127 84 igmlfQGGalFDSLTVFENVAFPLREHTDLsEAEIREL--------------VLEKLELVGLPG--AADK---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 145 gieqhngpM-SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTIRWLENVLTQRNSL---MIIISHDRHFLNSVC 219
Cdd:COG1127 138 --------MpSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSAVIDELIRELRDELgltSVVVTHDLDSAFAIA 209
|
250 260
....*....|....*....|
gi 1502692530 220 THMADLDYGELrLFPGNYDE 239
Cdd:COG1127 210 DRVAVLADGKI-IAEGTPEE 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
3.40e-17 |
|
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: 79.18 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFG--PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFayeef 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNEL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 tvldtvimgheelwkvkaeRDRIYSLPEmteDDgmavaELetefaeMDGYTAESRagelllglgigieqhngpmseVSPG 159
Cdd:cd03246 75 -------------------GDHVGYLPQ---DD-----EL------FSGSIAENI---------------------LSGG 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 160 WKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHDRHFLNSV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAHRPETLASA 162
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
3.77e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.21 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFG----PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML------EPNVRLGKLRQ 71
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTVIMGHEELWKVKAERDRIyslpemteddgmaVAELeTEFAEMDGYtaesragelllglgigieQHNG 151
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARER-------------AEEL-LELVGLSGF------------------ENAY 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 152 PmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHD 211
Cdd:cd03293 129 P-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
322-520 |
4.14e-17 |
|
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: 80.69 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGF-DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES--------------AEIGY 386
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQDHAhdFEDECT-----LFDWMGQWTqggeqLVRGTLGrmLFSNDEILKS----------------VKVISGGEQGRM 445
Cdd:cd03256 83 IFQQFN--LIERLSvlenvLSGRLGRRS-----TWRSLFG--LFPKEEKQRAlaalervglldkayqrADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 446 LFGKLILQKPNVLVMDEPTNHLD-------MESIEALNLALENypgTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTY 518
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLK-DGRIVFDGPP 229
|
..
gi 1502692530 519 DD 520
Cdd:cd03256 230 AE 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
324-504 |
4.41e-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: 80.03 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 324 RMAKGFDGTTLfkDFSFTVEaSERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----WTESAE----------IGYYA 388
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRKkinlppqqrkIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QdhahdfedECTLFDWMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVL 458
Cdd:cd03297 82 Q--------QYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLdhllnrypaqLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 459 VMDEPTNHLDMES----IEALNLALENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03297 154 LLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-197 |
6.65e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----------EPNVRLGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagddvealsarAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTVIMGHeelwkvKAERDRiysLPEMTEDDGMAVaELETEFAEMDGYTAEsragelllglgigieqh 149
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGR------TPHRSR---FDTWTETDRAAV-ERAMERTGVAQFADR----------------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 150 ngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDIN-TIRWLENV 197
Cdd:PRK09536 136 --PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLELV 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-210 |
8.63e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 80.13 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMlepnVRLGK---------LR- 70
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFGErrggedvweLRk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 ---------QDQFAYEEfTVLDTVIMGHE---ELWKvkaerdriyslpEMTEDDGMAVAELETEFaEMDGYTaesragel 138
Cdd:COG1119 79 riglvspalQLRFPRDE-TVLDVVLSGFFdsiGLYR------------EPTDEQRERARELLELL-GLAHLA-------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 139 llglgigieqhNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISH 210
Cdd:COG1119 137 -----------DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-230 |
9.86e-17 |
|
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: 79.68 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnvRLGKL----RQDQFAYEEftvldTVIMGH 89
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------RVAGLvpwkRRKKFLRRI-----GVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 90 -EELWKVKAERD------RIYSLPemtedDGMAVAELEtEFAEMDGYTAESragelllglgigieqhNGPMSEVSPGWKL 162
Cdd:cd03267 103 kTQLWWDLPVIDsfyllaAIYDLP-----PARFKKRLD-ELSELLDLEELL----------------DTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSL----MIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErgttVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-499 |
1.17e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 302 RVSPFIRFEQTKKLHRQAV--------VVERMAKGFDG--TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNEL-- 369
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLdlservaiVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 370 TPDAGSIKWTESaeigyyaqdhahDFEDECTLFDWMGQwtQGGEQLVRGTLGRM-LFSNDEILKSVKVISGGEQGRMLFG 448
Cdd:COG2401 83 TPVAGCVDVPDN------------QFGREASLIDAIGR--KGDFKDAVELLNAVgLSDAVLWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 449 KLILQKPNVLVMDEPTNHLDMES--IEALNLALE--NYPGTLIFVSHDREFVSSL 499
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTakRVARNLQKLarRAGITLVVATHHYDVIDDL 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
329-513 |
1.29e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 329 FDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGS-------IKWTESAEIGYYA----QDHAHDFED 397
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlvagddVEALSARAASRRVasvpQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 ECTLFDWMGQ---------WTQGGEQLVRGTLGRM---LFSNdeilKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTN 465
Cdd:PRK09536 93 DVRQVVEMGRtphrsrfdtWTETDRAAVERAMERTgvaQFAD----RPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 466 HLDM-ESIEALNLA--LENYPGTLIFVSHDREFVSSLATRIIELSPSGVID 513
Cdd:PRK09536 169 SLDInHQVRTLELVrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-218 |
1.36e-16 |
|
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: 78.79 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 13 PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNV---RLGKLRQDQFAYEEfTV 81
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADlrrNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 LDTVIMGHeelwkvkaerdriyslPEMTEDDGMAVAELE--TEFAEM--DGYTAEsragelllglgigiEQHNGpmSEVS 157
Cdd:cd03245 95 RDNITLGA----------------PLADDERILRAAELAgvTDFVNKhpNGLDLQ--------------IGERG--RGLS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 158 PGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHDRHFLNSV 218
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLLDLV 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-512 |
1.48e-16 |
|
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: 78.45 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES--AEIGYYAQDHAHDFED 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 -----ECTLFDWMGQwtqggeqlvrgTLGRMLFSNDEILKSV-----------------KVISGGEQGRMLFGKLILQKP 455
Cdd:cd03301 81 yalypHMTVYDNIAF-----------GLKLRKVPKDEIDERVrevaellqiehlldrkpKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 456 NVLVMDEPTNHLD----MESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSpSGVI 512
Cdd:cd03301 150 KVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMN-DGQI 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
1.54e-16 |
|
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: 78.33 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVM--------LEPNVR-LGKLRQDQFAY 76
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgVPPERRnIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 EEFTVLDTVIMGHEELWKVKAE-RDRIYSLPEMTEDDGMAvaeletefaemdgytaesragelllglgigieqhNGPMSE 155
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPKAEiRARVRELLELVGLEGLL----------------------------------NRYPHE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 156 VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINtIRW-----LENVLTQRNSLMIIISHDR 212
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-504 |
1.73e-16 |
|
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: 78.03 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-WTESAEIGYYAQDHAHDFEDE 398
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 CTLFDWMgqwtQGGEQLVRGTLGRMLFSN--DEIL----------KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:cd03268 81 PGFYPNL----TARENLRLLARLLGIRKKriDEVLdvvglkdsakKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1502692530 467 LDMESIEALN---LALENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03268 157 LDPDGIKELReliLSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
319-504 |
2.14e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.02 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNEL-TPDAGSIKwtesaeIGYYAQDHAHDFED 397
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLeQPEAGTIR------VGDITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 ECTLFDWMGQWT----QG---------------GEQLVRGT-------LGRmlfsndEILKSV----------KVISGGE 441
Cdd:PRK11264 76 QKGLIRQLRQHVgfvfQNfnlfphrtvleniieGPVIVKGEpkeeataRAR------ELLAKVglagketsypRRLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 442 QGRMLFGKLILQKPNVLVMDEPTNHLDMESI-EALN----LALENYpgTLIFVSHDREFVSSLATRII 504
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNtirqLAQEKR--TMVIVTHEMSFARDVADRAI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
322-520 |
2.20e-16 |
|
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: 78.63 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------------------- 376
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglppheiarlgigrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 ------KWT--ESAEIGYYAQDHAHdfedectlfDWMGQWTQGGEQLVRGTlgrmlfsnDEILKSVKV----------IS 438
Cdd:cd03219 83 iprlfpELTvlENVMVAAQARTGSG---------LLLARARREEREARERA--------EELLERVGLadladrpageLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 439 GGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEAL-----NLALENYpgTLIFVSHDREFVSSLATRIIELSpSGVID 513
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELaelirELRERGI--TVLLVEHDMDVVMSLADRVTVLD-QGRVI 222
|
....*..
gi 1502692530 514 FSGTYDD 520
Cdd:cd03219 223 AEGTPDE 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
2.22e-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: 77.92 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFG----PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGKLR 70
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 QDQFAY--------EEFTVLDTVIMGHEELWKVKAER-DRIYSLPEMteddgMAVAELETEFAemdgytaesragelllg 141
Cdd:cd03255 81 RRHIGFvfqsfnllPDLTALENVELPLLLAGVPKKERrERAEELLER-----VGLGDRLNHYP----------------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 142 lgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDR 212
Cdd:cd03255 139 ------------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
315-480 |
2.64e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.40 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 315 LHRQAVVVERmakgfDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--TESAEIGYYAQDHA 392
Cdd:TIGR01189 1 LAARNLACSR-----GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngTPLAEQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 HdfedectlfdWMG---------------QWTQ---GGEQL-VRGTLGRMLFSNDEILkSVKVISGGEQGRMLFGKLILQ 453
Cdd:TIGR01189 76 L----------YLGhlpglkpelsalenlHFWAaihGGAQRtIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLS 144
|
170 180
....*....|....*....|....*..
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEALNLALE 480
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-507 |
3.18e-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: 77.53 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA-------EIGYYAQDH--------- 391
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEKElaafrrrHIGFVFQSFnllpdltal 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 ---------AHDFEDECtlfdwmgqwtqggEQLVRGTLGRM-LfsNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMD 461
Cdd:cd03255 101 envelplllAGVPKKER-------------RERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 462 EPTNHLD-------MESIEALNlalENYPGTLIFVSHDREFVsSLATRIIELS 507
Cdd:cd03255 166 EPTGNLDsetgkevMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIELR 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
331-475 |
3.95e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESA-EIGYYAQD-----HAHDFEDECTLFDW 404
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiDDPDVAEAchylgHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 405 MGQWtqggeqlvRGTLGRMLFSNDEILKSV----------KVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEA 474
Cdd:PRK13539 94 LEFW--------AAFLGGEELDIAAALEAVglaplahlpfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
.
gi 1502692530 475 L 475
Cdd:PRK13539 166 F 166
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
4.87e-16 |
|
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: 77.62 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPK----PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGdLE-PSGGQVMLE-------PNVRLGK 68
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDgtdltllSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 69 LRQD------QFA-YEEFTVLDTVIMGHEeLWKV-KAERDRiyslpemteddgmAVAELeTEFAEMdgytaESRAgelll 140
Cdd:cd03258 80 ARRRigmifqHFNlLSSRTVFENVALPLE-IAGVpKAEIEE-------------RVLEL-LELVGL-----EDKA----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 141 glgigieqHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLN 216
Cdd:cd03258 135 --------DAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVK 205
|
250
....*....|....
gi 1502692530 217 SVCTHMADLDYGEL 230
Cdd:cd03258 206 RICDRVAVMEKGEV 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
5.26e-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: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV----------MLEPNVR--------LGKLRQDQFAYEEF 79
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTKPGPDgrgrakryIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 TVLD--TVIMGHE---ELWKVKAerdrIYSLpemteddgmAVAELETEFAE--MDGYTaesragelllglgigieqhngp 152
Cdd:TIGR03269 381 TVLDnlTEAIGLElpdELARMKA----VITL---------KMVGFDEEKAEeiLDKYP---------------------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 mSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTIRWLENVLTQR---NSLMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:TIGR03269 426 -DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
..
gi 1502692530 229 EL 230
Cdd:TIGR03269 505 KI 506
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-506 |
5.85e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.55 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQDHAHDFEDECTL 401
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWMgqwtQGGEQLVRgtLGRM--------LFSNDEIL----------KSVKVISGGEQGRMLFGKLILQKPNVLVMDEP 463
Cdd:cd03269 82 YPKM----KVIDQLVY--LAQLkglkkeeaRRRIDEWLerlelseyanKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 464 TNHLDMESIEALNLALENYPG---TLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-492 |
5.98e-16 |
|
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: 80.48 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTT-LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE-----------SAEIGYY 387
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 388 AQDhAHDF----------------EDECT-------LFDWMgQWTQGGEQLVRGTLGRMLfsndeilksvkviSGGEQGR 444
Cdd:TIGR02868 415 AQD-AHLFdttvrenlrlarpdatDEELWaalervgLADWL-RALPDGLDTVLGEGGARL-------------SGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 445 MLFGKLILQKPNVLVMDEPTNHLDMES----IEALNLALENYpgTLIFVSHD 492
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR--TVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
330-506 |
7.98e-16 |
|
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: 80.02 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA---EIGYYAQdHAHDFEDe 398
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladADADSwrdQIAWVPQ-HPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 cTLFD--WMGQWTQGGEQLVRG-----------TLGRMLfsNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTN 465
Cdd:TIGR02857 411 -TIAEniRLARPDASDAEIREAleragldefvaALPQGL--DTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1502692530 466 HLDMES----IEALNLALENYpgTLIFVSHDREfVSSLATRIIEL 506
Cdd:TIGR02857 488 HLDAETeaevLEALRALAQGR--TVLLVTHRLA-LAALADRIVVL 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-524 |
9.46e-16 |
|
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: 79.95 E-value: 9.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLvNELTPDAGSIK---------------WTESAEIGYYAQDHAhdfedecT 400
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRISgevlldgrdllelseALRGRRIGMVFQDPM-------T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 401 LFDWMGQWTQGGEQLVRGTLGR--MLFSNDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:COG1123 95 QLNPVTVGDQIAEALENLGLSRaeARARVLELLEAVGLerrldryphqLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 469 M----ESIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPsGVIDFSGTYDDYLRS 524
Cdd:COG1123 175 VttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD-GRIVEDGPPEEILAA 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-527 |
1.45e-15 |
|
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: 76.11 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA---EIGYYAQDhahdfede 398
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirEVTLDSlrrAIGVVPQD-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 CTLFD-------WMGQWTQGGEQLVRGTLGRMLfsNDEILK-----SVKV------ISGGEQGRMLFGKLILQKPNVLVM 460
Cdd:cd03253 84 TVLFNdtigyniRYGRPDATDEEVIEAAKAAQI--HDKIMRfpdgyDTIVgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 461 DEPTNHLD----MESIEALNLALENYpgTLIFVSHDREFVSSlATRIIELSPSGVIDfSGTYDDYLRSQGV 527
Cdd:cd03253 162 DEATSALDthteREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAKGGL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
332-491 |
1.60e-15 |
|
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: 74.66 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 332 TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkwtesaeigYYAQDHAHDFedECTLFDWMGQWTQg 411
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDL--EKALSSLISVLNQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 412 geqlvrgtlgRMLFSNDEILKSV-KVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMES-IEALNLALENYPG-TLIF 488
Cdd:cd03247 83 ----------RPYLFDTTLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIW 152
|
...
gi 1502692530 489 VSH 491
Cdd:cd03247 153 ITH 155
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-233 |
1.70e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.65 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV--------MLEPNVRLGklrqdqfayEEFTVLD 83
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtvrgrvssLLGLGGGFN---------PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 84 TVIMGHEELWKVKAERDRIYslpemteDDGMAVAELEtEFAEMdgytaesragelllglgigieqhngPMSEVSPGWKLR 163
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKI-------DEIIEFSELG-DFIDL-------------------------PVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 164 VLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENvLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLF 233
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFqekcQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-256 |
1.82e-15 |
|
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: 79.04 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQ----FAY--EE---F--T 80
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVDLRDLDEDDlrrrIAVvpQRphlFdtT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVIMG-----HEELWKVkAER----DRIYSLPemtedDGmavaeLETEFAEmDGYTaesragelllglgigieqhng 151
Cdd:COG4987 425 LRENLRLArpdatDEELWAA-LERvglgDWLAALP-----DG-----LDTWLGE-GGRR--------------------- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 152 pmseVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIR-WLENVLTQ-RNSLMIIISHDRHFLNSVcTHMADLDYGE 229
Cdd:COG4987 472 ----LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQaLLADLLEAlAGRTVLLITHRLAGLERM-DRILVLEDGR 546
|
250 260
....*....|....*....|....*..
gi 1502692530 230 LrlfpgnydeymtVATQSREQLLADNA 256
Cdd:COG4987 547 I------------VEQGTHEELLAQNG 561
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-520 |
1.91e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.49 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--------TESAE--IGYYAQ 389
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlftnLPPRErrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMgqwTqggeqlVRG----TLGRMLFSNDEI-------LKSVKV----------ISGGEQGRMLFG 448
Cdd:COG1118 83 HYA--------LFPHM---T------VAEniafGLRVRPPSKAEIrarveelLELVQLegladrypsqLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 449 KLILQKPNVLVMDEPTNHLD------MESiealNLA--LENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDD 520
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDakvrkeLRR----WLRrlHDELGGTTVFVTHDQEEALELADRVVVMN-QGRIEQVGTPDE 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
420-525 |
2.24e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.13 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 420 LGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSHDREFVSSL 499
Cdd:PLN03073 328 LAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
90 100
....*....|....*....|....*.
gi 1502692530 500 ATRIIELSPSGVIDFSGTYDDYLRSQ 525
Cdd:PLN03073 408 VTDILHLHGQKLVTYKGDYDTFERTR 433
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-520 |
2.93e-15 |
|
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: 75.35 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW---------TESAEIGYYAQD 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 HAhdfedectLFDWMGQWTQGGEQLVRGTLGRMLFSN--DEILKSVKV----------ISGGEQGRMLFGKLILQKPNVL 458
Cdd:cd03300 81 YA--------LFPHLTVFENIAFGLRLKKLPKAEIKErvAEALDLVQLegyanrkpsqLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 459 VMDEPTNHLDMESIEALNLALENYPG----TLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDD 520
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMN-KGKIQQIGTPEE 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
3.67e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDqfAYEEFT 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK--LYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVimgheelwkvkaerDRIYSLPEMTEDDGMAVAELETEFAEMdgytaesragelllglgigieqHNGPMSEVSPGW 160
Cdd:PRK09544 82 LPLTV--------------NRFLRLRPGTKKEDILPALKRVQAGHL----------------------IDAPMQKLSGGE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 161 KLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ-RNSL---MIIISHDRHFLnsvcthMADLD 226
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQlRRELdcaVLMVSHDLHLV------MAKTD 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
3.85e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQ--VMLEP--------NVRLGKLRQ 71
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitVLGVPvpararlaRARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTVIMgheelwkvkaeRDRIYslpemteddGMAVAELET------EFAEMdgytaESRAgelllglgig 145
Cdd:PRK13536 122 FDNLDLEFTVRENLLV-----------FGRYF---------GMSTREIEAvipsllEFARL-----ESKA---------- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 146 ieqhNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK13536 167 ----DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-229 |
5.31e-15 |
|
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: 72.99 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE------PNVRLGKLRQD-QFAYEE 78
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdLEDELPPLRRRiGMVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 F------TVLDTVIMGheelwkvkaerdriyslpemteddgmavaeletefaemdgytaesragelllglgigieqhngp 152
Cdd:cd03229 85 FalfphlTVLENIALG---------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 mseVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:cd03229 101 ---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITrrevRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
.
gi 1502692530 229 E 229
Cdd:cd03229 178 K 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-232 |
7.39e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.47 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnvrlgklrqdQFAYEEFTV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV--------------LFDGKPLDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 LDtvimgheelwkvkaeRDRIYSLPemtEDDG----MAVAELETEFAEMDGYT-AESRAGELLLGLGIGIEQH-NGPMSE 155
Cdd:cd03269 67 AA---------------RNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkEEARRRIDEWLERLELSEYaNKRVEE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 156 VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHDRHFLNSVCTHMADLDYGELRL 232
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElarAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
337-524 |
7.39e-15 |
|
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: 75.92 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 337 DFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----WTESAE----------IGYYAQdhahdfedECTL 401
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRKgiflppekrrIGYVFQ--------EARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWMG--QWTQGGEQLVRGTLGRMLFsnDEIL----------KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:TIGR02142 87 FPHLSvrGNLRYGMKRARPSERRISF--ERVIellgighllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 470 ESIEALNLALENYPGTL----IFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDYLRS 524
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFgipiLYVSHSLQEVLRLADRVVVLE-DGRVAAAGPIAEVWAS 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
322-528 |
7.43e-15 |
|
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: 74.30 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQD----------- 390
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DGRDITGLPPHriarlgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 -HAHDFEdECTLFD--WMGQWTQGGEQLVRGTLGRMLFSN---------DEILKSV----------KVISGGEQGRMLFG 448
Cdd:COG0411 86 qNPRLFP-ELTVLEnvLVAAHARLGRGLLAALLRLPRARReereareraEELLERVgladradepaGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 449 KLILQKPNVLVMDEPT---NHLDMESIEALNLALENYPG-TLIFVSHDREFVSSLATRIIelspsgVIDF-----SGTYD 519
Cdd:COG0411 165 RALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV------VLDFgrviaEGTPA 238
|
....*....
gi 1502692530 520 DYLRSQGVV 528
Cdd:COG0411 239 EVRADPRVI 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-254 |
9.36e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.87 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGKLRQD-----QFAYEEF 79
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklSRRSLRELRRRvqmvfQDPYSSL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 ----TVLDTVIMG---HEELWKvKAERDRIYSLpemteddgMAVAELETEFAEMDGYtaesragelllglgigieqhngp 152
Cdd:COG1123 356 nprmTVGDIIAEPlrlHGLLSR-AERRERVAEL--------LERVGLPPDLADRYPH----------------------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 msEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDInTIRW-----LENVLTQRNSLMIIISHDRHFLNSVCTHMADLDY 227
Cdd:COG1123 404 --ELSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqilnlLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250 260
....*....|....*....|....*..
gi 1502692530 228 GELrlfpgnydeymtVATQSREQLLAD 254
Cdd:COG1123 481 GRI------------VEDGPTEEVFAN 495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-504 |
9.39e-15 |
|
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: 73.69 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW--------------TESAEIGYYAQDHAHdfedecTL 401
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdllklsrrlrkIRRKEIQMVFQDPMS------SL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWMGQWTQGGE--QLVRGTLGRMLFSNDEILKSVKV-------------ISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:cd03257 96 NPRMTIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglpeevlnrypheLSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 467 LDMeSIEALNLAL-----ENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03257 176 LDV-SVQAQILDLlkklqEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-211 |
1.00e-14 |
|
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: 73.37 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGG--DL---EPSGGQVMLEP-NV----------- 64
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLipgAPDEGEVLLDGkDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 65 -RLGKLRQDQFAYEeFTVLDTVIMG---HEELWKvKAERDRIYSLPEMteddgmavAELETEFAemdgytaeSRAGElll 140
Cdd:cd03260 81 rRVGMVFQKPNPFP-GSIYDNVAYGlrlHGIKLK-EELDERVEEALRK--------AALWDEVK--------DRLHA--- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 141 glgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHD 211
Cdd:cd03260 140 -------------LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAElkKEYTIVIVTHN 199
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
1.11e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.15 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFG----PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGKL 69
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQD------QFAY--EEFTVLDTVIMGHeELWKVKAERDRIYSLpEMTEDDGMAvaeletefaemdgytaeSRAgelllg 141
Cdd:COG1136 84 RRRhigfvfQFFNllPELTALENVALPL-LLAGVSRKERRERAR-ELLERVGLG-----------------DRL------ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 142 lgigieqHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRH 213
Cdd:COG1136 139 -------DHRP-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPE 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
336-516 |
1.25e-14 |
|
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: 73.17 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGsikwteSAEI-GYyaqDHAHD----------FEDECTLFDW 404
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVdGF---DVVKEpaearrrlgfVSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 405 MGQWT-----------QGGEQLVR-GTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESI 472
Cdd:cd03266 93 LTAREnleyfaglyglKGDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1502692530 473 EALNLALENYPG---TLIFVSHDREFVSSLATRIIELSpSGVIDFSG 516
Cdd:cd03266 173 RALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLH-RGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
336-503 |
1.26e-14 |
|
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: 73.52 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWT---------ESAEIGYYAQDHAhdfedectLFDWMG 406
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQNYA--------LFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 407 QWtqggEQLVRGtLGRMLFSNDEILKSVKVI-----------------SGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:cd03299 88 VY----KNIAYG-LKKRKVDKKEIERKVLEIaemlgidhllnrkpetlSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1502692530 470 ES----IEALNLALENYPGTLIFVSHDREFVSSLATRI 503
Cdd:cd03299 163 RTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-230 |
1.53e-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: 72.56 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE------PNVRLGKLRQD--- 72
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltdDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 ---QFA-YEEFTVLDTVIMGheeLWKVKaerdriyslpemteddGMAVAEletefaemdgytAESRAGELLLGLGIGIEQ 148
Cdd:cd03262 81 vfqQFNlFPHLTVLENITLA---PIKVK----------------GMSKAE------------AEERALELLEKVGLADKA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 149 HNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNSVCTHMADL 225
Cdd:cd03262 130 DAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
....*
gi 1502692530 226 DYGEL 230
Cdd:cd03262 209 DDGRI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-475 |
2.20e-14 |
|
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: 71.76 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESA---EIGYYAQD-----HA--------- 392
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGllylgHApgikttlsv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 -------HDFEDECTLFDWMGQWTQGG-EQLVRGTLgrmlfsndeilksvkviSGGEQGRMLFGKLILQKPNVLVMDEPT 464
Cdd:cd03231 91 lenlrfwHADHSDEQVEEALARVGLNGfEDRPVAQL-----------------SAGQQRRVALARLLLSGRPLWILDEPT 153
|
170
....*....|.
gi 1502692530 465 NHLDMESIEAL 475
Cdd:cd03231 154 TALDKAGVARF 164
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-504 |
2.32e-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: 72.83 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 337 DFSFTVEA-----SERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQDHAHDFEDecTLFDWMGQWTQG 411
Cdd:cd03237 12 EFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEG--TVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 412 geqlvrgtLGRMLFSNDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDME----SIEALNL 477
Cdd:cd03237 89 --------FYTHPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRR 160
|
170 180
....*....|....*....|....*..
gi 1502692530 478 ALENYPGTLIFVSHDREFVSSLATRII 504
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
336-504 |
3.46e-14 |
|
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: 71.98 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK----------------------------WTESAEIGYY 387
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrrkkflrrigvvfgqktqlwWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 388 AQDHAHDFEDEctlfdwmgqwtQGGEQLVRgtLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHL 467
Cdd:cd03267 118 LLAAIYDLPPA-----------RFKKRLDE--LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1502692530 468 DMESIEALNLALENY----PGTLIFVSHDREFVSSLATRII 504
Cdd:cd03267 185 DVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVL 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
3.76e-14 |
|
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: 70.49 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQdQFAY--EEFTVLDTV 85
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvdlRDLDLESLRK-NIAYvpQDPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 ImgheelwkvkaeRDRIYSlpemteddGmavaeletefaemdgytaesragelllglgigieqhngpmsevspGWKLRVL 165
Cdd:cd03228 92 I------------RENILS--------G---------------------------------------------GQRQRIA 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDINT-IRWLENVLTQR-NSLMIIISHDRH 213
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETeALILEALRALAkGKTVIVIAHRLS 156
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
4.39e-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: 70.15 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGKlrqdqfayeEFTV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GK---------EVSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 LDTvimgheelwkVKAERDRIYSLPEMteddgmavaeletefaemdgytaesragelllglgigieqhngpmsevSPGWK 161
Cdd:cd03216 67 ASP----------RDARRAGIAMVYQL------------------------------------------------SVGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISH 140
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-520 |
4.69e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESA----EIGyyaqdhaHDFEDECTlfdwmgqwtq 410
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallELG-------AGFHPELT---------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 411 gGEQLVRgTLGRML-FSNDEILK-----------------SVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDME-- 470
Cdd:COG1134 105 -GRENIY-LNGRLLgLSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfq 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 471 --SIEALNlALENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDD 520
Cdd:COG1134 183 kkCLARIR-ELRESGRTVIFVSHSMGAVRRLCDRAIWLE-KGRLVMDGDPEE 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-230 |
5.73e-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: 71.38 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFAYEE------------- 78
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKeiqmvfqdpmssl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 ---FTVLDTV---IMGHEELWKVKAERDRIYSLpemteddgMAVAELETEFAEMdgYtaesragelllglgigieqhngP 152
Cdd:cd03257 96 nprMTIGEQIaepLRIHGKLSKKEARKEAVLLL--------LVGVGLPEEVLNR--Y----------------------P 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 mSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYG 228
Cdd:cd03257 144 -HELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
..
gi 1502692530 229 EL 230
Cdd:cd03257 223 KI 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-516 |
6.11e-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: 71.02 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE--SAEIGYyaqdhAHDFEDECTlfdwmgqwtqgG 412
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGL-----GGGFNPELT-----------G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 413 EQLVRgTLGRML-FSNDEILKS-----------------VKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD---ME- 470
Cdd:cd03220 102 RENIY-LNGRLLgLSRKEIDEKideiiefselgdfidlpVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafQEk 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 471 SIEALNLALENyPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSG 516
Cdd:cd03220 181 CQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLE-KGKIRFDG 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-516 |
6.12e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.68 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASeRVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES-----------------A 382
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrigylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 383 EIGYYAQDHAHDFEDECTlfdWMGQWTQGGE-QLVRGTLGRM-LfsNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVM 460
Cdd:cd03264 80 EFGVYPNFTVREFLDYIA---WLKGIPSKEVkARVDEVLELVnL--GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 461 DEPTNHLDMES-IEALNLALENYPGTLIFVS-HDREFVSSLATRIIELSpSGVIDFSG 516
Cdd:cd03264 155 DEPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVAVLN-KGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
327-504 |
8.02e-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: 70.64 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNEL-TPDAGSI------------KWTE-SAEIGYYAQdHA 392
Cdd:cd03262 8 KSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIiidglkltddkkNINElRQKVGMVFQ-QF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 HDFE-----DECTLfdwmgqwtqgGEQLVRG-------TLGRmlfsndEILKSVKV----------ISGGEQGRMLFGKL 450
Cdd:cd03262 86 NLFPhltvlENITL----------APIKVKGmskaeaeERAL------ELLEKVGLadkadaypaqLSGGQQQRVAIARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMESI-EAL----NLALENYpgTLIFVSHDREFVSSLATRII 504
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVgEVLdvmkDLAEEGM--TMVVVTHEMGFAREVADRVI 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-517 |
9.44e-14 |
|
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: 70.67 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTL--VNELTPDAgsikwTESAEIGYYAQDHAHDFED-- 397
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGA-----PDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 -----------ECTLFDW-------MGQWTQG------GEQLVRGTLGRM-LFsnDEILKSVKV--ISGGEQGRMLFGKL 450
Cdd:cd03260 78 elrrrvgmvfqKPNPFPGsiydnvaYGLRLHGiklkeeLDERVEEALRKAaLW--DEVKDRLHAlgLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMES---IEALNLAL-ENYpgTLIFVSHDREFVSSLATRIIELSPSGVIDFSGT 517
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIStakIEELIAELkKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-512 |
1.02e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.46 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA-------EIGYYAQDH 391
Cdd:COG1136 16 TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisSLSERElarlrrrHIGFVFQFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 ahdfedecTLFDW--------MGQWTQGGEQLVRGTLGRmlfsndEILKSVKV----------ISGGEQGRMLFGKLILQ 453
Cdd:COG1136 96 --------NLLPEltalenvaLPLLLAGVSRKERRERAR------ELLERVGLgdrldhrpsqLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 454 KPNVLVMDEPTNHLD-------MESIEALNlalENYPGTLIFVSHDREfVSSLATRIIELSpSGVI 512
Cdd:COG1136 162 RPKLILADEPTGNLDsktgeevLELLRELN---RELGTTIVMVTHDPE-LAARADRVIRLR-DGRI 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.04e-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: 73.55 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----------EPNVRLGKLRQDQ--FAYee 78
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQDAhlFDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 fTVLDTVIMGH-----EELWKVkAERDRIYSLPEMTEDDgmavaeLETEFAEMDgytaesragelllglgigieqhngpm 153
Cdd:TIGR02868 424 -TVRENLRLARpdatdEELWAA-LERVGLADWLRALPDG------LDTVLGEGG-------------------------- 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 154 SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMiiISHD 211
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGRTVVL--ITHH 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-231 |
1.13e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPL----FENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML----------EPNVRL 66
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgfdvvkepaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 67 GKLRQDQFAYEEFTVLDTV--------IMGHEelwkVKAERDRIYSLPEMTEddgmavaeletefaemdgyTAESRAgel 138
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLeyfaglygLKGDE----LTARLEELADRLGMEE-------------------LLDRRV--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 139 llglgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSL---MIIISHDRHFL 215
Cdd:cd03266 135 ---------------GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFSTHIMQEV 199
|
250
....*....|....*.
gi 1502692530 216 NSVCTHMADLDYGELR 231
Cdd:cd03266 200 ERLCDRVVVLHRGRVV 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
1.28e-13 |
|
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: 73.09 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQF-GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLG----KLRQDQFAY 76
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLAdadaDSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 ---EEFTVLDTVimgheelwkvkAERDRIYsLPEMTEDDGMAVAELetefAEMDGYTAESRAGelllglgigieqHNGPM 153
Cdd:TIGR02857 401 vpqHPFLFAGTI-----------AENIRLA-RPDASDAEIREALER----AGLDEFVAALPQG------------LDTPI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 154 SE----VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTirwlENVLTQ------RNSLMIIISHDRHflnsvctHMA 223
Cdd:TIGR02857 453 GEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEalralaQGRTVLLVTHRLA-------LAA 521
|
....
gi 1502692530 224 DLDY 227
Cdd:TIGR02857 522 LADR 525
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-506 |
1.34e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 323 ERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWTESAEIGYYAQDHAHD-----FED 397
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARrigllAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 ECTLFDWMGQ----------------WTQGGEQLVRGTLgRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMD 461
Cdd:PRK10253 90 ATTPGDITVQelvargryphqplftrWRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 462 EPTNHLDM-ESIEALNL--ALENYPG-TLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK10253 169 EPTTWLDIsHQIDLLELlsELNREKGyTLAAVLHDLNQACRYASHLIAL 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-464 |
1.41e-13 |
|
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: 70.16 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-------TESAE-----IGYYAQDHAhdfedectLFD 403
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditgLPPHEraragIGYVPEGRR--------IFP 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 404 --------WMGQWTQGGEQlVRGTLGRM--LFSN-DEILKS-VKVISGGEQgRML-FGKLILQKPNVLVMDEPT 464
Cdd:cd03224 89 eltveenlLLGAYARRRAK-RKARLERVyeLFPRlKERRKQlAGTLSGGEQ-QMLaIARALMSRPKLLLLDEPS 160
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
336-507 |
1.49e-13 |
|
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: 69.97 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA------EIGYYAQDHAhdFEDECTL 401
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRiagedvnrLRGRQlpllrrRIGVVFQDFR--LLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWM-------GQWTQGGEQLVRGTLgRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD---MES 471
Cdd:TIGR02673 97 YENValplevrGKKEREIQRRVGAAL-RQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDpdlSER 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1502692530 472 IEALNLALENYPGTLIFVSHDREFVSSLATRIIELS 507
Cdd:TIGR02673 176 ILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-503 |
1.57e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--PNVRLGKLRQDQFA--- 75
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnPCARLTPAKAHQLGiyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 -------YEEFTVLDTVIMGheeLWKVKAERDRIYSLpemteddgmaVAELETEFA-EMDGYTAEsragelllglgIGIE 147
Cdd:PRK15439 91 vpqepllFPNLSVKENILFG---LPKRQASMQKMKQL----------LAALGCQLDlDSSAGSLE-----------VADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 148 QhngpMSEVSPGwklrvllaqaLFSDPEVLLLDEPTNHLdinTIRWLENVLTQRNSL------MIIISHDRHFLNSVCTH 221
Cdd:PRK15439 147 Q----IVEILRG----------LMRDSRILILDEPTASL---TPAETERLFSRIRELlaqgvgIVFISHKLPEIRQLADR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 222 MADLDYGELRLFpGNYDEYmtvatqSREQLLA--DNAKKKAQISELQSFVSRFSANaskakqatSRAKQIDKiqlaevkp 299
Cdd:PRK15439 210 ISVMRDGTIALS-GKTADL------STDDIIQaiTPAAREKSLSASQKLWLELPGN--------RRQQAAGA-------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 300 ssrvsPFIRfeqtkklhrqavvVERMA-KGfdgttlFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkW 378
Cdd:PRK15439 267 -----PVLT-------------VEDLTgEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-M 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 379 TESAEIGYY------AQDHAHDFEDE---------------CTL-FDWMGQWTQGGEQlvRGTLGR------MLFSNDEi 430
Cdd:PRK15439 322 LNGKEINALstaqrlARGLVYLPEDRqssglyldaplawnvCALtHNRRGFWIKPARE--NAVLERyrralnIKFNHAE- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 431 lKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD----------MESIEALNLAlenypgtLIFVSHDREFVSSLA 500
Cdd:PRK15439 399 -QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlIRSIAAQNVA-------VLFISSDLEEIEQMA 470
|
...
gi 1502692530 501 TRI 503
Cdd:PRK15439 471 DRV 473
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-188 |
1.96e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTVIMGheelwkvkaerdRI-YSLPEMTEDDGMAVAE----LE-TEFAemDGYtaesragelllglg 143
Cdd:COG4604 81 RQENHINSRLTVRELVAFG------------RFpYSKGRLTAEDREIIDEaiayLDlEDLA--DRY-------------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1502692530 144 igieqhngpMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI 188
Cdd:COG4604 133 ---------LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
320-496 |
2.21e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAHDFEDEC 399
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLFDWMgqwtqggeQLVRGTlgrmlfSNDEILKSVKVI-------------SGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:PRK09544 85 TVNRFL--------RLRPGT------KKEDILPALKRVqaghlidapmqklSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|....
gi 1502692530 467 LDMESIEALNLALENYPGTL----IFVSHDREFV 496
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELdcavLMVSHDLHLV 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
320-492 |
2.60e-13 |
|
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: 72.47 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTT--LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA---EIGY 386
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqWDREElgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQDhahdfedeCTLFDwmgqwtqggeqlvrGTLG----RMLFSNDEilksvKVI------------------------- 437
Cdd:COG4618 411 LPQD--------VELFD--------------GTIAeniaRFGDADPE-----KVVaaaklagvhemilrlpdgydtrige 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 438 -----SGGEQ-----GRMLFGklilqKPNVLVMDEPTNHLDMESIEALNLALENY---PGTLIFVSHD 492
Cdd:COG4618 464 ggarlSGGQRqriglARALYG-----DPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
331-512 |
2.74e-13 |
|
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: 68.35 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTP--DAGSI--------KWTESAEIGYYAQ-DHAHdfedec 399
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKIIGYVPQdDILH------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 tlfdwmgqwtqgGEQLVRGTLgrmLFSNDeiLKSvkvISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDmeSIEALNL-- 477
Cdd:cd03213 95 ------------PTLTVRETL---MFAAK--LRG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLD--SSSALQVms 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1502692530 478 ---ALENYPGTLIFVSHD-REFVSSLATRIIELSPSGVI 512
Cdd:cd03213 153 llrRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
319-504 |
2.85e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.28 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW------TESAE---IGYYAQ 389
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtGLPPEkrnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMGqwtqggeqlVR-----GtLGRMLFSNDEILKSVK-----V------------ISGGEQgrmlf 447
Cdd:COG3842 85 DYA--------LFPHLT---------VAenvafG-LRMRGVPKAEIRARVAellelVglegladryphqLSGGQQ----- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 448 gklilQ----------KPNVLVMDEPTNHLDMESIEAL-----NLaLENYPGTLIFVSHDREFVSSLATRII 504
Cdd:COG3842 142 -----QrvalaralapEPRVLLLDEPLSALDAKLREEMreelrRL-QRELGITFIYVTHDQEEALALADRIA 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-508 |
3.31e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE---SAEIGYYAQD-----HAHDFEDECTL 401
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHQDllylgHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FD----WMGQWTQGGEQLVRGTLGRMLFSNDEILkSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNL 477
Cdd:PRK13538 92 LEnlrfYQRLHGPGDDEALWEALAQVGLAGFEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180 190
....*....|....*....|....*....|....
gi 1502692530 478 ALENYP---GTLIFVSHDREFVSSLATRIIELSP 508
Cdd:PRK13538 171 LLAQHAeqgGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
3.40e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 69.29 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE------PNVR---LGKLRQD 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdVPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFAYEEFTVLDTVIMGHEElwKVKAERDriyslPEMTEDDgmAVAELeTEFAEMDGYtaESRAgelllglgigieqhngP 152
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRV--KPRSERP-----PEAEIRA--KVHEL-LKLVQLDWL--ADRY----------------P 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 153 mSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHD 211
Cdd:cd03296 135 -AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVrkelRRWLRRLHDELHVTTVFVTHD 196
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
322-507 |
3.91e-13 |
|
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: 69.46 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESAEIGYYAQ-DHA 392
Cdd:TIGR03873 4 LSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARARRVALvEQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 HDFEDECTLFD------------WMGQwTQGGEQLVRGTLGRMLFSnDEILKSVKVISGGEQGRMLFGKLILQKPNVLVM 460
Cdd:TIGR03873 84 SDTAVPLTVRDvvalgriphrslWAGD-SPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 461 DEPTNHLDMES-IEALNLALE-NYPGTLIFVS-HDREFVSSLATRIIELS 507
Cdd:TIGR03873 162 DEPTNHLDVRAqLETLALVRElAATGVTVVAAlHDLNLAASYCDHVVVLD 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
4.03e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMK-------ILGGDLePSGGQVMLEPNVRLGKLRQD- 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDL-IVDGLKVNDPKVDERLIRQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 -----QF-AYEEFTVLDTVIMGheelwkvkaerdriyslPEMTEddGMAVAELETEFAEMDGYTA-ESRAgelllglgig 145
Cdd:PRK09493 80 gmvfqQFyLFPHLTALENVMFG-----------------PLRVR--GASKEEAEKQARELLAKVGlAERA---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 146 ieqHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDiNTIRwlENVLTQRNSL------MIIISHDRHFLNSVC 219
Cdd:PRK09493 131 ---HHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALD-PELR--HEVLKVMQDLaeegmtMVIVTHEIGFAEKVA 203
|
....*....
gi 1502692530 220 THMADLDYG 228
Cdd:PRK09493 204 SRLIFIDKG 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
331-492 |
5.83e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.03 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKwtesaeigYYAQDhahdfedectLFDW------ 404
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRP----------LADWspaela 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 405 -----MGQWTQGG-----EQLVRgtLGRMLFSN---------DEILKSVKV----------ISGGEQGRMLFGKLILQ-- 453
Cdd:PRK13548 76 rrravLPQHSSLSfpftvEEVVA--MGRAPHGLsraeddalvAAALAQVDLahlagrdypqLSGGEQQRVQLARVLAQlw 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1502692530 454 ----KPNVLVMDEPTNHLD----MESIEAL-NLALENyPGTLIFVSHD 492
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDlahqHHVLRLArQLAHER-GLAVIVVLHD 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-520 |
6.09e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 68.52 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI---------KWTESAEIGYYAQ 389
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHA---HdfedeCTLFDWMG-------QWTQGGEQLVRGTLgrmlfsnDEILKSVKV----------ISGGEQGRMLFGK 449
Cdd:cd03296 82 HYAlfrH-----MTVFDNVAfglrvkpRSERPPEAEIRAKV-------HELLKLVQLdwladrypaqLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 450 LILQKPNVLVMDEPTNHLDMESIEALNLAL----ENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDD 520
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLrrlhDELHVTTVFVTHDQEEALEVADRVVVMN-KGRIEQVGTPDE 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
320-478 |
6.14e-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: 67.67 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDA---GSIKW----------TESAEIGY 386
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYngipykefaeKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQDHAHdfedectlfdwMGQWTqggeqlVRGTLGrmlFS----NDEIlksVKVISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:cd03233 88 VSEEDVH-----------FPTLT------VRETLD---FAlrckGNEF---VRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170
....*....|....*.
gi 1502692530 463 PTNHLDmeSIEALNLA 478
Cdd:cd03233 145 STRGLD--SSTALEIL 158
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-504 |
7.29e-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: 66.30 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQDHAHDfedec 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFASPRDARR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 tlfdwMG-----QWTQGGEQLVrgtlgrmlfsndEILKSvkvisggeqgrmlfgklILQKPNVLVMDEPTNHLDMESIEA 474
Cdd:cd03216 75 -----AGiamvyQLSVGERQMV------------EIARA-----------------LARNARLLILDEPTAALTPAEVER 120
|
170 180 190
....*....|....*....|....*....|....*
gi 1502692530 475 L-----NLALENypGTLIFVSHDREFVSSLATRII 504
Cdd:cd03216 121 LfkvirRLRAQG--VAVIFISHRLDEVFEIADRVT 153
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-187 |
1.03e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EP--------NVRLGKLRQ 71
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTV-IMGHEELWKVKAERDRIYSLpemteddgmavaeleTEFAEMdgytaESRAgelllglgigieqhN 150
Cdd:PRK13537 88 FDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPL---------------LEFAKL-----ENKA--------------D 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 1502692530 151 GPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK13537 134 AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-510 |
1.04e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 21 SVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQvmlepnvrlgklRQDQF---AYEEFTVLDTVImghEELWKvka 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE------------RQSQFshiTRLSFEQLQKLV---SDEWQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 98 eRDRIYSLPEMTEDDGMAVAE---LET-------EFAEMDGYTAE-SRagelllglgigieqhngPMSEVSPGWKLRVLL 166
Cdd:PRK10938 85 -RNNTDMLSPGEDDTGRTTAEiiqDEVkdparceQLAQQFGITALlDR-----------------RFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 167 AQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNS----LMIIIS--HDrhfLNSVCTHMADLDYGELrlfpgnydey 240
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgitLVLVLNrfDE---IPDFVQFAGVLADCTL---------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 241 mtVATQSREQLLADnakkkAQISELqsfvsrfsanaskakqatSRAKQIDKIQLAEV-KPSSRvsPFIRFEQTKKLHRQA 319
Cdd:PRK10938 214 --AETGEREEILQQ-----ALVAQL------------------AHSEQLEGVQLPEPdEPSAR--HALPANEPRIVLNNG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVvermakGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLrTLV---------NELT-----PDAGSIKWTESAEIG 385
Cdd:PRK10938 267 VV------SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLItgdhpqgysNDLTlfgrrRGSGETIWDIKKHIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 386 YYAQDHAHDFEDECTL--------FDWMGQWTQGGE---QLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQK 454
Cdd:PRK10938 340 YVSSSLHLDYRVSTSVrnvilsgfFDSIGIYQAVSDrqqKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKH 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 455 PNVLVMDEPTNHLDmesieALNLAL---------ENYPGTLIFVSHDREFVSSLATRIIELSPSG 510
Cdd:PRK10938 420 PTLLILDEPLQGLD-----PLNRQLvrrfvdvliSEGETQLLFVSHHAEDAPACITHRLEFVPDG 479
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
1.04e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.80 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV--------MLEPNVrlGklrqdqFaYEEFTVLDTV----- 85
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsaLLELGA--G------F-HPELTGRENIylngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMGHEelwkvKAERDRIYslpemteDDGMAVAELEtEFAEMdgytaesragelllglgigieqhngPMSEVSPGWKLRVL 165
Cdd:COG1134 115 LLGLS-----RKEIDEKF-------DEIVEFAELG-DFIDQ-------------------------PVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 166 LAQALFSDPEVLLLDEPTNHLDIN----TIRWLENVLtQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLF 233
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
330-506 |
1.06e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.38 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI----------KWTESA----EIGYYAQDHahdf 395
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlKRREIPylrrRIGVVFQDF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 edectlfdwmgqwtqggeQL---------------VRGTLGRMLFSN-DEILKSVK----------VISGGEQGRMLFGK 449
Cdd:COG2884 89 ------------------RLlpdrtvyenvalplrVTGKSRKEIRRRvREVLDLVGlsdkakalphELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 450 LILQKPNVLVMDEPTNHLDME-SIEALNLALE-NYPG-TLIFVSHDREFVSSLATRIIEL 506
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPEtSWEIMELLEEiNRRGtTVLIATHDLELVDRMPKRVLEL 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-211 |
1.17e-12 |
|
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: 67.32 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGA-GNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV---------------RLGKL 69
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTVIMGheelWKVKAERDRIYSLPEMTedDGMAVAELEtefaemdgytaesragelllglgigieqh 149
Cdd:cd03297 81 FQQYALFPHLNVRENLAFG----LKRKRNREDRISVDELL--DLLGLDHLL----------------------------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 150 NGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHD 211
Cdd:cd03297 126 NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
327-517 |
1.75e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE------SAEigyyaQDHAHDFEDECT 400
Cdd:PRK09452 22 KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvPAE-----NRHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 401 LFDWMGqwtqggeqlVRGTLG---RML-FSNDEI-------LKSVKV----------ISGGEQGRMLFGKLILQKPNVLV 459
Cdd:PRK09452 97 LFPHMT---------VFENVAfglRMQkTPAAEItprvmeaLRMVQLeefaqrkphqLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 460 MDEPTNHLD------MES-IEALNLALenypG-TLIFVSHDREFVSSLATRIIELSpSGVIDFSGT 517
Cdd:PRK09452 168 LDESLSALDyklrkqMQNeLKALQRKL----GiTFVFVTHDQEEALTMSDRIVVMR-DGRIEQDGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
331-506 |
1.82e-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: 66.66 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESA-------EIGYYAQDHAHDFED-----E 398
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKIGVVFQDfrllpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 CTLFDWMG---QWTQGGEQLVRGTLGRMLfsnDEILKSVKV------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:cd03292 93 RNVYENVAfalEVTGVPPREIRKRVPAAL---ELVGLSHKHralpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1502692530 470 E-SIEALNLALE-NYPGTLIFVS-HDREFVSSLATRIIEL 506
Cdd:cd03292 170 DtTWEIMNLLKKiNKAGTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
330-527 |
2.05e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.42 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW---------TES--AEIGYYAQDHahdfede 398
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltLESlrRQIGVVPQDT------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 cTLFDwmgqwtqggeqlvrGT------LGRMLFSNDEILKSVK------VISG---------GEQGRMLFG----KL--- 450
Cdd:COG1132 424 -FLFS--------------GTirenirYGRPDATDEEVEEAAKaaqaheFIEAlpdgydtvvGERGVNLSGgqrqRIaia 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 451 --ILQKPNVLVMDEPTNHLDMES----IEALNLALENYpgTLIFVSHdRefVSSL--ATRIIELSpSGVIDFSGTYDDYL 522
Cdd:COG1132 489 raLLKDPPILILDEATSALDTETealiQEALERLMKGR--TTIVIAH-R--LSTIrnADRILVLD-DGRIVEQGTHEELL 562
|
....*
gi 1502692530 523 RSQGV 527
Cdd:COG1132 563 ARGGL 567
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-230 |
2.14e-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: 66.28 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPK-PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGKLRQD- 72
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFAYEEFTVLdtvimgheelwkvkaerdriyslPEMTEDDGMAVAeleTEFAEMDGYTAESRAGELLLGLGIGIEQHNGP 152
Cdd:cd03292 81 GVVFQDFRLL-----------------------PDRNVYENVAFA---LEVTGVPPREIRKRVPAALELVGLSHKHRALP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 MsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRN---SLMIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:cd03292 135 A-ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGK 213
|
.
gi 1502692530 230 L 230
Cdd:cd03292 214 L 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
336-464 |
3.22e-12 |
|
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: 66.16 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW------TESAE------IGYYAQDHAhdfedectLFD 403
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditGLPPHriarlgIGYVPEGRR--------IFP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 404 --------WMGQWTQGGEQLVRGTLGRM--LFsndEILKSVK-----VISGGEQgRML-FGKLILQKPNVLVMDEPT 464
Cdd:COG0410 92 sltveenlLLGAYARRDRAEVRADLERVyeLF---PRLKERRrqragTLSGGEQ-QMLaIGRALMSRPKLLLLDEPS 164
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-506 |
3.52e-12 |
|
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: 65.59 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 337 DFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTEsaeigyyaQDHAHD----------FED-----ECTL 401
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--------VDVTAAppadrpvsmlFQEnnlfaHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWMG-------QWTQGGEQLVRGTLGRMLFSNDEiLKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD---MES 471
Cdd:cd03298 88 EQNVGlglspglKLTAEDRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1502692530 472 IEALNLALENYPG-TLIFVSHDREFVSSLATRIIEL 506
Cdd:cd03298 167 MLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
7.76e-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: 65.08 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQ-------VMLEP-NVR--LGKLRQ 71
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPrEVRrrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTVIMgHEELWKVKAE--RDRIyslpemteDDGMAVAELeTEFAemdgytaesragelllglgigieqh 149
Cdd:cd03265 81 DLSVDDELTGWENLYI-HARLYGVPGAerRERI--------DELLDFVGL-LEAA------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 150 NGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADL 225
Cdd:cd03265 126 DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
....*.
gi 1502692530 226 DYGELR 231
Cdd:cd03265 206 DHGRII 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-212 |
8.29e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 66.71 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV----------RLGKLRQ 71
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DqfaYEEF---TVLDTVIMGHEELWKVKAE-RDRIYSLPEMTEDDGMAvaeletefaemDGYtaesragelllglgigie 147
Cdd:COG1118 83 H---YALFphmTVAENIAFGLRVRPPSKAEiRARVEELLELVQLEGLA-----------DRY------------------ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 148 qhngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI---NTIR-WLENVL--TQRNSlmIIISHDR 212
Cdd:COG1118 131 ----P-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHdeLGGTT--VFVTHDQ 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
8.88e-12 |
|
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: 65.28 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 12 GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEP----NVRLGKLRQ--DQFAY--------E 77
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinKLKGKALRQlrRQIGMifqqfnliE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 EFTVLDTVIMG---HEELWKV------KAERDRiyslpemteddgmAVAELETefAEMDGYtAESRAgelllglgigieq 148
Cdd:cd03256 92 RLSVLENVLSGrlgRRSTWRSlfglfpKEEKQR-------------ALAALER--VGLLDK-AYQRA------------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 149 hngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNS---LMIIIS-HD 211
Cdd:cd03256 143 -----DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegITVIVSlHQ 204
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-230 |
9.07e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-PNVRLGKLRQDQ---FAYE 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgQTINLVRDKDGQlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 EFTVLDT---VIMGHEELWKVKAERDRIYSLPemTEDDGMAVAEletefaemdgytAESRAGELLLGLGIGIEQHNGPMS 154
Cdd:PRK10619 86 QLRLLRTrltMVFQHFNLWSHMTVLENVMEAP--IQVLGLSKQE------------ARERAVKYLAKVGIDERAQGKYPV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD---INTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
330-510 |
9.42e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW------TESAE-----IGYYAQDHAHdFED- 397
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFegedisTLKPEiyrqqVSYCAQTPTL-FGDt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 --ECTLFDWMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMlfgKLI--LQ-KPNVLVMDEPTNHLDMESI 472
Cdd:PRK10247 97 vyDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRI---SLIrnLQfMPKVLLLDEITSALDESNK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 473 EALNLALENYPG----TLIFVSHDREFVSSlATRIIELSPSG 510
Cdd:PRK10247 174 HNVNEIIHRYVReqniAVLWVTHDKDEINH-ADKVITLQPHA 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-230 |
9.89e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVM-----LEPNVR-LGKLRQdQF 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpLDYSKRgLLALRQ-QV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AyeefTVLDTvimGHEELWKVKAERDRIYSLPEMteddGMAVAELETEFAEmdgytaesragelllGLGIGIEQH--NGP 152
Cdd:PRK13638 80 A----TVFQD---PEQQIFYTDIDSDIAFSLRNL----GVPEAEITRRVDE---------------ALTLVDAQHfrHQP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 MSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLmIIISHDRHFLNSVCTHMADLDYG 228
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQG 212
|
..
gi 1502692530 229 EL 230
Cdd:PRK13638 213 QI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-211 |
1.16e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 64.57 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNVR-LGKLRQD 72
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFAYEEFTVLDTVIMGHEELWKVKAERDRiyslpemteddgmAVAELeTEFAEMDGYtaesragelllglgigieQHNGP 152
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKE-------------RVAEA-LDLVQLEGY------------------ANRKP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 153 mSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLT--QRN--SLMIIISHD 211
Cdd:cd03300 129 -SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKrlQKElgITFVFVTHD 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
322-508 |
1.31e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE------SAEIGYYAQDHAhdf 395
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpGAERGVVFQNEG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 edectLFDW--------MGQWTQGGEQLVRGTLGRmlfsndEILKSVKV----------ISGGEQGRMLFGKLILQKPNV 457
Cdd:PRK11248 81 -----LLPWrnvqdnvaFGLQLAGVEKMQRLEIAH------QMLKKVGLegaekryiwqLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 458 LVMDEPTNHLDM---ESIEALNLALENYPGTLIF-VSHDREFVSSLATRIIELSP 508
Cdd:PRK11248 150 LLLDEPFGALDAftrEQMQTLLLKLWQETGKQVLlITHDIEEAVFMATELVLLSP 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-504 |
2.15e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.65 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----------WTESAEIGYYAQDHAHDF-----EDEC 399
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQVGMVFQNPDNQFvgatvQDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLfdwmGQWTQG--GEQLVRgtlgRMlfsnDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHL 467
Cdd:PRK13635 104 AF----GLENIGvpREEMVE----RV----DQALRQVGMedflnrephrLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1502692530 468 D-------MESIEALNlalENYPGTLIFVSHDREFVSSlATRII 504
Cdd:PRK13635 172 DprgrrevLETVRQLK---EQKGITVLSITHDLDEAAQ-ADRVI 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-468 |
2.15e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 305 PFIRFEQTKKLHRQAVVVErmakgfdgttlfkDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES--- 381
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVD-------------GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 382 -------AEIGYYAQ-DHAH-DF---EDECTLFDWMGQWTQGGEQLVRGTLGrmlFSNDEILKSVKV--ISGGEQGRMLF 447
Cdd:PRK13537 73 srarharQRVGVVPQfDNLDpDFtvrENLLVFGRYFGLSAAAARALVPPLLE---FAKLENKADAKVgeLSGGMKRRLTL 149
|
170 180
....*....|....*....|.
gi 1502692530 448 GKLILQKPNVLVMDEPTNHLD 468
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
307-525 |
2.70e-11 |
|
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: 63.86 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 307 IRFEQTKKLHRqavvvermakgfDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRtLVNEL-TPDAGSIK-------- 377
Cdd:cd03295 1 IEFENVTKRYG------------GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFidgedire 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 378 WTESA---EIGYYAQdhahdfedECTLFDWMGQWTQGGeqLVRGTLG----RMLFSNDEILKSVKV------------IS 438
Cdd:cd03295 68 QDPVElrrKIGYVIQ--------QIGLFPHMTVEENIA--LVPKLLKwpkeKIRERADELLALVGLdpaefadrypheLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 439 GGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALN---LALENYPG-TLIFVSHDREFVSSLATRIIELSPSGVIDF 514
Cdd:cd03295 138 GGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGkTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
250
....*....|.
gi 1502692530 515 sGTYDDYLRSQ 525
Cdd:cd03295 218 -GTPDEILRSP 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-377 |
2.81e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPnVRLGKLRQDQ-----FAYEE 78
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgEP-VRFRSPRDAQaagiaIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 F------TVLDTVIMGHEelwkvkAERDRIYSLPEMTEDdgmAVAELETEFAEMDGYTaesragelllglgigieqhngP 152
Cdd:COG1129 88 LnlvpnlSVAENIFLGRE------PRRGGLIDWRAMRRR---ARELLARLGLDIDPDT---------------------P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 153 MSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHdrhflnsvcthmadldyge 229
Cdd:COG1129 138 VGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIirrLKAQGVAIIYISH------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 230 lRLfpgnyDEYMTVatqsreqllADnakkkaQISELQ--SFVsrfsanASKAKQATSRAKQIDKI---QLAEVKPSSRVS 304
Cdd:COG1129 199 -RL-----DEVFEI---------AD------RVTVLRdgRLV------GTGPVAELTEDELVRLMvgrELEDLFPKRAAA 251
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 305 PfirfeqtkklhrQAVVVErmAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK 377
Cdd:COG1129 252 P------------GEVVLE--VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-503 |
2.86e-11 |
|
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: 63.29 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI----------KWTESAEIGYYAQdhaHDfedecTLFDWM 405
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQ---FD-----ALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 gqwTqgGEQ------LVRGTLGRMLFSNDEIL-----------KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:cd03263 91 ---T--VREhlrfyaRLKGLPKSEIKEEVELLlrvlgltdkanKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1502692530 469 MESIEAL-NLALENYPG-TLIFVSHDREFVSSLATRI 503
Cdd:cd03263 166 PASRRAIwDLILEVRKGrSIILTTHSMDEAEALCDRI 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-183 |
3.36e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPkplF---ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----EPN-----VRLGKLRQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGdiatrRRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 QFA-YEEFTV---LDTvimgHeelwkvkAerdRIYSLPEmtEDDGMAVAELETEFAEMDgyTAESRAgelllglgigieq 148
Cdd:NF033858 347 AFSlYGELTVrqnLEL----H-------A---RLFHLPA--AEIAARVAEMLERFDLAD--VADALP------------- 395
|
170 180 190
....*....|....*....|....*....|....*
gi 1502692530 149 hngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPT 183
Cdd:NF033858 396 -----DSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-517 |
3.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.91 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------KWTE-SAEIGYYAQDHAHD-FEDecTL 401
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvKLSDiRKKVGLVFQYPEYQlFEE--TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FdwmgqwtqggEQLVRGTLGRMLfSNDEILKSVKV-------------------ISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:PRK13637 102 E----------KDIAFGPINLGL-SEEEIENRVKRamnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 463 PTNHLD-------MESIEALNlalENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGT 517
Cdd:PRK13637 171 PTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHSMEDVAKLADRIIVMN-KGKCELQGT 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
319-526 |
4.10e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.37 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTL-FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA---EIGY 386
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtVTRASlrrNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQD-------------------------------HAHDF-EDECTLFDwmgqwTQGGEQlvrgtlGRMLfsndeilksv 434
Cdd:PRK13657 414 VFQDaglfnrsiednirvgrpdatdeemraaaeraQAHDFiERKPDGYD-----TVVGER------GRQL---------- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 435 kviSGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALENypgtlifVSHDR-EFV-----SSL--ATRIIEL 506
Cdd:PRK13657 473 ---SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-------LMKGRtTFIiahrlSTVrnADRILVF 542
|
250 260
....*....|....*....|
gi 1502692530 507 SPSGVIDfSGTYDDYLRSQG 526
Cdd:PRK13657 543 DNGRVVE-SGSFDELVARGG 561
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-492 |
4.12e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHA--------- 392
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLArrlallpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 HDFEDECTLFD--------WMGQW---TQGGEQLVRGTLGRMlfsndEIL----KSVKVISGGEQGRMLFGKLILQKPNV 457
Cdd:PRK11231 85 HLTPEGITVRElvaygrspWLSLWgrlSAEDNARVNQAMEQT-----RINhladRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1502692530 458 LVMDEPTNHLDM-ESIEALNL--ALENYPGTLIFVSHD 492
Cdd:PRK11231 160 VLLDEPTTYLDInHQVELMRLmrELNTQGKTVVTVLHD 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
338-523 |
4.30e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 338 FSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTEsaeigyyaQDHAHD----------FEDEcTLFDWMGQ 407
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG--------QDLTALppaerpvsmlFQEN-NLFPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 WTQGGeqlvrgtLG---RMLFSNDE------ILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:COG3840 89 AQNIG-------LGlrpGLKLTAEQraqveqALERVGLaglldrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 469 ------MesiealnLAL-----ENYPGTLIFVSHDREFVSSLATRIIeLSPSGVIDFSGTYDDYLR 523
Cdd:COG3840 162 palrqeM-------LDLvdelcRERGLTVLMVTHDPEDAARIADRVL-LVADGRIAADGPTAALLD 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-513 |
4.51e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK------WTESAEigyyaqdHAHDFedecTLFdwMGQWT 409
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpFKRRKE-------FARRI----GVV--FGQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 410 Q-------------------GGEQLVRGTLGRM--LFSNDEILKS-VKVISGGEqgRMLfGKLI---LQKPNVLVMDEPT 464
Cdd:COG4586 106 QlwwdlpaidsfrllkaiyrIPDAEYKKRLDELveLLDLGELLDTpVRQLSLGQ--RMR-CELAaalLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 465 NHLDMES-------IEALNlalENYPGTLIFVSHDREFVSSLATRIIelspsgVID 513
Cdd:COG4586 183 IGLDVVSkeairefLKEYN---RERGTTILLTSHDMDDIEALCDRVI------VID 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
4.72e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE------PNVRLGKLRQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AYEEFTVLDTVIMGHEELWKVKAERdriyslpEMTEDDGMAVAELEtefaemdgyTAESRagelllglgigieqhngPMS 154
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQR-------LEIAHQMLKKVGLE---------GAEKR-----------------YIW 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ----RNSLMIIISHD 211
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwqeTGKQVLLITHD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
5.80e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML-----------EPNVRLGKLRQDQF 74
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AYEEFTVLDTVIMG---HEELWKVKAERDriyslpemteDDGMAVAELETEFAEMDGYTAESragelllglgigieqhng 151
Cdd:PRK10253 92 TPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKAMQATGITHLADQSVDT------------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 152 pmseVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNS----LMIIISHDrhfLNSVC---THMAD 224
Cdd:PRK10253 144 ----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD---LNQACryaSHLIA 216
|
....*.
gi 1502692530 225 LDYGEL 230
Cdd:PRK10253 217 LREGKI 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
336-471 |
6.42e-11 |
|
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: 62.04 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----------WTESAEIGYYAQDHahdfedecTLFdw 404
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTIIPQDP--------TLF-- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 405 MGQwtqggeqlVRGTLGRM-LFSNDEILKSVKVISGGE---QGR---MLFGKLILQKPNVLVMDEPTNHLDMES 471
Cdd:cd03369 95 SGT--------IRSNLDPFdEYSDEEIYGALRVSEGGLnlsQGQrqlLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-230 |
6.85e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV-----------RLGKLRQDQF 74
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AYEEFTVLDTVIMG----HEELWKVKAE-RDRIyslpemteDDGMAVAELeTEFAemdgytaesragelllglgigieqh 149
Cdd:PRK10575 96 AAEGMTVRELVAIGrypwHGALGRFGAAdREKV--------EEAISLVGL-KPLA------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 150 NGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADL 225
Cdd:PRK10575 142 HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
....*
gi 1502692530 226 DYGEL 230
Cdd:PRK10575 222 RGGEM 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-210 |
6.90e-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: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPK--PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEP-NVR---LGKLRQdQFA 75
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVRdytLASLRR-QIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 Y---EEFTVLDTVimgheelwkvkaeRDRI-YSLPEMTEDDGMAVAELE--TEFAEM--DGYTAEsragelllglgigiE 147
Cdd:cd03251 80 LvsqDVFLFNDTV-------------AENIaYGRPGATREEVEEAARAAnaHEFIMElpEGYDTV--------------I 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 148 QHNGpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLT--QRNSLMIIISH 210
Cdd:cd03251 133 GERG--VKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALErlMKNRTTFVIAH 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
324-504 |
7.62e-11 |
|
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: 63.58 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 324 RMAKGFDGTTLfkDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----WTESAE----------IGYYA 388
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARgiflpphrrrIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAhdfedectLFDWMGqwtqggeqlVRGTL---------GRMLFSNDEIlksVKV-------------ISGGEQGRML 446
Cdd:COG4148 84 QEAR--------LFPHLS---------VRGNLlygrkraprAERRISFDEV---VELlgighlldrrpatLSGGERQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 447 FGKLILQKPNVLVMDEPTNHLDMES-------IEALNLALeNYPgtLIFVSHDREFVSSLATRII 504
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARkaeilpyLERLRDEL-DIP--ILYVSHSLDEVARLADHVV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-206 |
8.39e-11 |
|
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: 62.25 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGP-KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLR-------QDq 73
Cdd:cd03253 5 NVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRraigvvpQD- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 74 fayeefTVL--DTVimgheelwkvkaeRDRI-YSLPEMTEDDGMA---VAELETEFAEM-DGYTAE--SRagelllglgi 144
Cdd:cd03253 84 ------TVLfnDTI-------------GYNIrYGRPDATDEEVIEaakAAQIHDKIMRFpDGYDTIvgER---------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 145 gieqhnGPMseVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRW----LENVLTQRNSLMI 206
Cdd:cd03253 135 ------GLK--LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREiqaaLRDVSKGRTTIVI 192
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-525 |
1.12e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.82 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-------TESAEIGY-------YAQdha 392
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYlpeerglYPK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 hdfedectlfdwMgqwtQGGEQLVRgtLGR---MlfSNDEILKS-----------------VKVISGGEQGRMLFGKLIL 452
Cdd:COG4152 86 ------------M----KVGEQLVY--LARlkgL--SKAEAKRRadewlerlglgdrankkVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 453 QKPNVLVMDEPTNHLDMESIEALNLALENY--PG-TLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDyLRSQ 525
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIIN-KGRKVLSGSVDE-IRRQ 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
346-504 |
1.72e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 59.31 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 346 ERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDhahdfedectlfdwmgqwtqggeqlvrgtlgrmLF 425
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLD---------------------------------QL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 426 SNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALEN---------YPGTLIFVSHDREFV 496
Cdd:smart00382 50 LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllkseKNLTVILTTNDEKDL 129
|
....*...
gi 1502692530 497 SSLATRII 504
Cdd:smart00382 130 GPALLRRR 137
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
322-503 |
1.78e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--KWTESAEIGYYAQDHAHDFEDEc 399
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImlDGVDLSHVPPYQRPINMMFQSY- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLFDWMGQwtqggEQLVRGTLGRMLFSNDEILKSVK-----------------VISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:PRK11607 101 ALFPHMTV-----EQNIAFGLKQDKLPKAEIASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1502692530 463 PTNHLDMESIEALNLA----LENYPGTLIFVSHDREFVSSLATRI 503
Cdd:PRK11607 176 PMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
1.97e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEP---SGGQVMLEPNV---------RLGK 68
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltalpaeqrRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 69 LRQDQFAYEEFTVLDTVIMGHEELWKVKAERDRIYslpEMTEDDGMAvaeletEFAEMDgytaesragelllglgigieq 148
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVE---QALEEAGLA------GFADRD--------------------- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 149 hngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISHD 211
Cdd:COG4136 131 ---P-ATLSGGQRARVALLRALLAEPRALLLDEPFSKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-210 |
2.23e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEP-NVRLGKLRQdQFAY--- 76
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgDIDDPDVAE-ACHYlgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 -----EEFTVLDTVimgheELW-KVKAERDRiySLPEMTEDDGMA-VAELetefaemdgytaesragelllglgigieqh 149
Cdd:PRK13539 81 rnamkPALTVAENL-----EFWaAFLGGEEL--DIAAALEAVGLApLAHL------------------------------ 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 150 ngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLT---QRNSLMIIISH 210
Cdd:PRK13539 124 --PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRahlAQGGIVIAATH 185
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-187 |
3.11e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNVR-LGKLRQDQFAY 76
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvpPYQRpINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 EEFTVLDTVIMGHEElwkvkaerdriyslpemtedDGMAVAELETEFAEMDGYTaesragelLLGLGIGIEQHngpmsEV 156
Cdd:PRK11607 104 PHMTVEQNIAFGLKQ--------------------DKLPKAEIASRVNEMLGLV--------HMQEFAKRKPH-----QL 150
|
170 180 190
....*....|....*....|....*....|.
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-211 |
3.23e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQvMLEPNVRLGKLRQD-QFAYEEF----- 79
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDtRLMFQDArllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 -TVLDTVIMGHEELWKVKAErdriyslpEMTEDDGMAvaeletefaemdgytaeSRAgelllglgigieqHNGPmSEVSP 158
Cdd:PRK11247 96 kKVIDNVGLGLKGQWRDAAL--------QALAAVGLA-----------------DRA-------------NEWP-AALSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISHD 211
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-506 |
3.38e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------KWTESaEIGYYAQDhAHDFED 397
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRS-KVGLVFQD-PDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 ECTLFD--WMGQWTQG--GEQLVRGTlgrmlfsnDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEP 463
Cdd:PRK13647 94 SSTVWDdvAFGPVNMGldKDEVERRV--------EEALKAVRMwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 464 TNHLD---MESIEALNLALENYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK13647 166 MAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVL 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-503 |
3.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGS-------IKWTESAEIGYYAQDHAHDFEDEctLFDW---- 404
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepITKENIREVRKFVGLVFQNPDDQ--IFSPtveq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 405 --------MGQWTQGGEQLVRGTLgRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEAL- 475
Cdd:PRK13652 99 diafgpinLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELi 177
|
170 180 190
....*....|....*....|....*....|.
gi 1502692530 476 ---NLALENYPGTLIFVSHDREFVSSLATRI 503
Cdd:PRK13652 178 dflNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
330-517 |
3.59e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKwTESAEIGYyaqdhahdfeDECTLFDwmgqwt 409
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-IKGEPIKY----------DKKSLLE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 410 qggeqlVRGTLG------------------------RMLFSNDEILKSVKV-----------------ISGGEQGRMLFG 448
Cdd:PRK13639 76 ------VRKTVGivfqnpddqlfaptveedvafgplNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 449 KLILQKPNVLVMDEPTNHLD-MESIEALNLALE-NYPG-TLIFVSHDREFVSSLATRIIELSpSGVIDFSGT 517
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDlNKEGiTIIISTHDVDLVPVYADKVYVMS-DGKIIKEGT 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
3.99e-10 |
|
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: 60.04 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNVR-LGKLRQDQFAYEEFTVLDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 89 HEELWKVKAERDRiySLPEMTEDdgMAVAELetefaemdgytaesragelllglgigieQHNGPMSeVSPGWKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAEM--LGIDHL----------------------------LNRKPET-LSGGEQQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1502692530 169 ALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
322-523 |
4.06e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.64 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvneltpdAGsIKWTESAEIGYYAQD----HAHD--- 394
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRII-------AG-LEHQTSGHIRFHGTDvsrlHARDrkv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 395 ---FEdECTLFDWMGQWtqggEQLVRG--TLGRMLFSNDEILKSvKV-------------------ISGGEQGRMLFGKL 450
Cdd:PRK10851 77 gfvFQ-HYALFRHMTVF----DNIAFGltVLPRRERPNAAAIKA-KVtqllemvqlahladrypaqLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMESIEALNLAL----ENYPGTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDYLR 523
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMS-QGNIEQAGTPDQVWR 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
319-504 |
4.90e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 61.24 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-------TESAE--IGYYAQ 389
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdLPPKDrnIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMgqwTqggeqlVRGTLG---RML-FSNDEILKSVKVI-----------------SGGEQ-----G 443
Cdd:COG3839 83 SYA--------LYPHM---T------VYENIAfplKLRkVPKAEIDRRVREAaellgledlldrkpkqlSGGQRqrvalG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 444 RMlfgklILQKPNVLVMDEPTNHLD------MES-IEALNLALENypgTLIFVSHDREFVSSLATRII 504
Cdd:COG3839 146 RA-----LVREPKVFLLDEPLSNLDaklrveMRAeIKRLHRRLGT---TTIYVTHDQVEAMTLADRIA 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-527 |
5.10e-10 |
|
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: 59.94 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-----------TESAEIGYYAQD-------- 390
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaSLRRQIGLVSQDvflfndtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 -----------------------HAHDFEDECTLfdwmGQWTQGGEqlvRGtlgrmlfsndeilksVKvISGGEQGRMLF 447
Cdd:cd03251 93 aeniaygrpgatreeveeaaraaNAHEFIMELPE----GYDTVIGE---RG---------------VK-LSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 448 GKLILQKPNVLVMDEPTNHLDMESIEALNLALENYPG--TLIFVSHDREFVSSlATRIIELSPSGVIDfSGTYDDYLRSQ 525
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIEN-ADRIVVLEDGKIVE-RGTHEELLAQG 227
|
..
gi 1502692530 526 GV 527
Cdd:cd03251 228 GV 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-187 |
5.25e-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: 61.27 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlgklrqdqfayeeft 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 vlDTVIMGheelwkVKAERDRI------YSL-PEMT---------EDDGMAVAELETEFAEM------DGYtAESRAgel 138
Cdd:COG3842 66 --GRDVTG------LPPEKRNVgmvfqdYALfPHLTvaenvafglRMRGVPKAEIRARVAELlelvglEGL-ADRYP--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 139 llglgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:COG3842 134 ---------------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-513 |
5.55e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK----------WTESAEIGYYA 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAHDFE----DECTLFD-WMGQWTQGGEQLVRGTLGrmlFSNDEILKSVKV--ISGGEQGRMLFGKLILQKPNVLVMD 461
Cdd:PRK13536 121 QFDNLDLEftvrENLLVFGrYFGMSTREIEAVIPSLLE---FARLESKADARVsdLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 462 EPTN-------HLDMESIEALnLALENypgTLIFVSH---------DREFVSSLATRIIELSPSGVID 513
Cdd:PRK13536 198 EPTTgldpharHLIWERLRSL-LARGK---TILLTTHfmeeaerlcDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-232 |
6.44e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG------GDLEPSG-----GQVMLEPNVRLGKL- 69
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGrveffNQNIYERRVNLNRLr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEE-----FTVLDTVIMGHEEL-WKVKAERDRIYslpemteDDGMAVAELETEFAEmdgytaesragelllglg 143
Cdd:PRK14258 88 RQVSMVHPKpnlfpMSVYDNVAYGVKIVgWRPKLEIDDIV-------ESALKDADLWDEIKH------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 144 igiEQHNGPMsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSL-MIIISHDRHFLNSVC 219
Cdd:PRK14258 143 ---KIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLiqsLRLRSELtMVIVSHNLHQVSRLS 218
|
250
....*....|...
gi 1502692530 220 THMADLDYGELRL 232
Cdd:PRK14258 219 DFTAFFKGNENRI 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-211 |
7.27e-10 |
|
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: 59.40 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--PNVRLGKLRQdqfayeeftvldtVIMGHEELWKV 95
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkQITEPGPDRM-------------VVFQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 96 KAERDRIY-----SLPEMTEDDGMAVAEletEFAEMDGYTAesragelllglgigiEQHNGPmSEVSPGWKLRVLLAQAL 170
Cdd:TIGR01184 69 LTVRENIAlavdrVLPDLSKSERRAIVE---EHIALVGLTE---------------AADKRP-GQLSGGMKQRVAIARAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1502692530 171 FSDPEVLLLDEPTNHLDINTIRWLENVLTQ----RNSLMIIISHD 211
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELMQiweeHRVTVLMVTHD 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-504 |
7.68e-10 |
|
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: 58.21 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVErmAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWT------------ESAEIGY 386
Cdd:cd03215 2 EPVLE--VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQDHAHDfedecTLFDWMGqwtqggeqlVRG--TLGRMLfsndeilksvkviSGGEQGRMLFGKLILQKPNVLVMDEPT 464
Cdd:cd03215 80 VPEDRKRE-----GLVLDLS---------VAEniALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1502692530 465 NHLDMESIEA-----LNLALENypGTLIFVSHDREFVSSLATRII 504
Cdd:cd03215 133 RGVDVGAKAEiyrliRELADAG--KAVLLISSELDELLGLCDRIL 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-210 |
8.01e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.33 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQdQFAY---EEF----TVL 82
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTLESLRR-QIGVvpqDTFlfsgTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 DTVIMGH-----EELWKVkAER----DRIYSLPemtedDGmavaeLETEFAEmdgytaesragelllglgigieqhNGpm 153
Cdd:COG1132 432 ENIRYGRpdatdEEVEEA-AKAaqahEFIEALP-----DG-----YDTVVGE------------------------RG-- 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 154 SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRW-LENVLTQRNSlmIIISH 210
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealIQEaLERLMKGRTT--IVIAH 533
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-230 |
8.50e-10 |
|
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: 58.82 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 16 LFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSG---GQVML--EPNVR------LGKLRQDQFAYEEFTVldt 84
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFngQPRKPdqfqkcVAYVRQDDILLPGLTV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 85 vimghEELWKVKAerdrIYSLPEMTEDdgmAVAELETEFAEMdGYTAESRAGelllglgigieqhNGPMSEVSPGWKLRV 164
Cdd:cd03234 99 -----RETLTYTA----ILRLPRKSSD---AIRKKRVEDVLL-RDLALTRIG-------------GNLVKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 165 LLAQALFSDPEVLLLDEPTNHLD----INTIRWLENvLTQRNSLMIIISHD-RHFLNSVCTHMADLDYGEL 230
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQ-LARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
335-491 |
8.57e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK--------WTESA--------------------EIGY 386
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqpiadYSEAAlrqaisvvsqrvhlfsatlrDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YAQDHAHD---------------FEDECTLFDWMGqwtQGGEQLvrgtlgrmlfsndeilksvkviSGGEQGRMLFGKLI 451
Cdd:PRK11160 436 LAAPNASDealievlqqvgleklLEDDKGLNAWLG---EGGRQL----------------------SGGEQRRLGIARAL 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 452 LQKPNVLVMDEPTNHLDMES-IEALNLALENYPG-TLIFVSH 491
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITH 532
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-210 |
8.94e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQF-GPKPLfENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGKLRQDQFAYEEFTVLDT 84
Cdd:PRK11288 9 GIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-----GQEMRFASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 85 VImgHEELWKVkaerdriyslPEMTeddgmaVAE------LETEFAEMDGYTAESRAgelllglgIGIEQHNGpmSEVSP 158
Cdd:PRK11288 83 II--YQELHLV----------PEMT------VAEnlylgqLPHKGGIVNRRLLNYEA--------REQLEHLG--VDIDP 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 159 GWKLRVL---------LAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISH 210
Cdd:PRK11288 135 DTPLKYLsigqrqmveIAKALARNARVIAFDEPTSSLSAREIEQLFRVireLRAEGRVILYVSH 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
9.57e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFAY--EE 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLDPEDRRRIGYlpEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 ------FTVLDTVI-MGheELWkvkaerdriyslpemteddGMAVAELETEFAE-MDGYTAESRAgelllglgigieqhN 150
Cdd:COG4152 80 rglypkMKVGEQLVyLA--RLK-------------------GLSKAEAKRRADEwLERLGLGDRA--------------N 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 151 GPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTiRWLENVLT-QRNSLMIII--SHDrhfLNSV---CTHMA 223
Cdd:COG4152 125 KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNV-ELLKDVIReLAAKGTTVIfsSHQ---MELVeelCDRIV 200
|
....*....
gi 1502692530 224 DLDYGELRL 232
Cdd:COG4152 201 IINKGRKVL 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-210 |
9.79e-10 |
|
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: 58.64 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGK-LRQDQFAYEEFTVldtVIMGHEELW 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD-----GKpISQYEHKYLHSKV---SLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 KVKAERDRI-YslpemteddGMAVAELETEFAEMDGYTAESRAGELLLGLGIGIEQHNgpmSEVSPGWKLRVLLAQALFS 172
Cdd:cd03248 100 FARSLQDNIaY---------GLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKG---SQLSGGQKQRVAIARALIR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1502692530 173 DPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISH 210
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAH 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
9.97e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVM---LEPNvrlgkLRQDQFAYEEftvldTVIMGH-EELW 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPF-----KRRKEFARRI-----GVVFGQrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 ---------KVKAErdrIYSLPEmteddgmavAELET---EFAEM---DGYTaesragelllglgigieqhNGPMSEVSP 158
Cdd:COG4586 109 wdlpaidsfRLLKA---IYRIPD---------AEYKKrldELVELldlGELL-------------------DTPVRQLSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IR-WLENVLTQRNSLMIIISHD 211
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeaIReFLKEYNRERGTTILLTSHD 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
324-504 |
1.52e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 324 RMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTlVN--------ELTPDAGSIKwTESAEIGYYAQDHAHDF 395
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-INkleeitsgDLIVDGLKVN-DPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 EdECTLFDWM--------------GQWTQGGEQLVRGTLG------RMLFSNDEIlksvkviSGGEQGRMLFGKLILQKP 455
Cdd:PRK09493 84 Q-QFYLFPHLtalenvmfgplrvrGASKEEAEKQARELLAkvglaeRAHHYPSEL-------SGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 456 NVLVMDEPTNHLDME-SIEAL----NLALENYpgTLIFVSHDREFVSSLATRII 504
Cdd:PRK09493 156 KLMLFDEPTSALDPElRHEVLkvmqDLAEEGM--TMVIVTHEIGFAEKVASRLI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-514 |
1.55e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLvNEL-TPDAGSIkwtesaEIGyyaqDHAHDFEDECTlfdwmgqwtQGGEQ 414
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLeTPDSGQL------NIA----GHQFDFSQKPS---------EKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 415 LVRGTLGrMLFSN--------------------------------DEILKSVKV----------ISGGEQGRMLFGKLIL 452
Cdd:COG4161 79 LLRQKVG-MVFQQynlwphltvmenlieapckvlglskeqarekaMKLLARLRLtdkadrfplhLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 453 QKPNVLVMDEPTNHLDME---SIEALNLALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDF 514
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-211 |
1.55e-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: 58.81 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 3 STANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRLGKLRQDQFA 75
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamSRKELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 --YEEF------TVLDTVIMGHEELWKVKAERdriyslpemteddgmavaeletefaemdgytaESRAGELLLGLGIGIE 147
Cdd:cd03294 106 mvFQSFallphrTVLENVAFGLEVQGVPRAER--------------------------------EERAAEALELVGLEGW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 148 QHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLT--QRNS--LMIIISHD 211
Cdd:cd03294 154 EHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLrlQAELqkTIVFITHD 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-210 |
1.60e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLgklRQDQFAYEEFTVldtVIMGHEELW 93
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPL---VQYDHHYLHRQV---ALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 KVKAERDRI-YSLPEMTEDDGMAVAEL---ETEFAEM-DGYTAESragelllglgigieqhnGPM-SEVSPGWKLRVLLA 167
Cdd:TIGR00958 567 FSGSVRENIaYGLTDTPDEEIMAAAKAanaHDFIMEFpNGYDTEV-----------------GEKgSQLSGGQKQRIAIA 629
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 168 QALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIIISH 210
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-503 |
1.63e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 58.59 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 329 FDGttlFK---DFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEIGYYAQdhaHD----------- 394
Cdd:COG4674 20 FDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLF-GGTDLTGLDE---HEiarlgigrkfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 395 ----FEdECTLFDWMgQWTQGGEQLVRGTLGRMLFSN-----DEILKSVK----------VISGGEQGRMLFGKLILQKP 455
Cdd:COG4674 93 kptvFE-ELTVFENL-ELALKGDRGVFASLFARLTAEerdriEEVLETIGltdkadrlagLLSHGQKQWLEIGMLLAQDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 456 NVLVMDEPTNHLDMESIEA-----LNLALENypgTLIFVSHDREFVSSLATRI 503
Cdd:COG4674 171 KLLLLDEPVAGMTDAETERtaellKSLAGKH---SVVVVEHDMEFVRQIARKV 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
336-481 |
1.76e-09 |
|
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: 58.01 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA---EIGYYAQDhAHDFEDecTLFD- 403
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirDISRKSlrsMIGVVLQD-TFLFSG--TIMEn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 404 -WMGQWTQGGEQLVRgtLGRMLFSNDEILKSVK-----------VISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMES 471
Cdd:cd03254 97 iRLGRPNATDEEVIE--AAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170
....*....|
gi 1502692530 472 IEALNLALEN 481
Cdd:cd03254 175 EKLIQEALEK 184
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-491 |
1.77e-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: 58.25 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 332 TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------KWTESA----------------- 382
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyehKYLHSKvslvgqepvlfarslqd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 383 EIGYYAQD-------------HAHDFEDECTLfdwmGQWTQGGEqlvRGTLgrmlfsndeilksvkvISGGEQGRMLFGK 449
Cdd:cd03248 107 NIAYGLQScsfecvkeaaqkaHAHSFISELAS----GYDTEVGE---KGSQ----------------LSGGQKQRVAIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1502692530 450 LILQKPNVLVMDEPTNHLDMESIEALNLALENYPG--TLIFVSH 491
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-491 |
2.03e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELtPDAGSIK--WTESAEIgyyaqdhahDFEDECTLFDWMGQ 407
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKinGIELREL---------DPESWRKHLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 wtqgGEQLVRGT------LGRMLFSNDEI---LKSVKV---------------------ISGGEQGRMLFGKLILQKPNV 457
Cdd:PRK11174 431 ----NPQLPHGTlrdnvlLGNPDASDEQLqqaLENAWVseflpllpqgldtpigdqaagLSVGQAQRLALARALLQPCQL 506
|
170 180 190
....*....|....*....|....*....|....*.
gi 1502692530 458 LVMDEPTNHLDMESIEALNLALENYPG--TLIFVSH 491
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTH 542
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-230 |
2.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV-RLGKlrqDQFAYEEFTVLDTVIMGHEE- 91
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlYFGK---DIFQIDAIKLRKEVGMVFQQp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 92 --LWKVKAERDRIYSLPEMTEDDGMAVAELETEFAEMDGYTAEsragelllglgiGIEQHNGPMSEVSPGWKLRVLLAQA 169
Cdd:PRK14246 100 npFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE------------VYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 170 LFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLM--IIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIaiVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-224 |
2.23e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 20 VSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnVRLGKlrqdqfayeeftvlDTVIMGHEELWKVKAE- 98
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV-----AWLGK--------------DLLGMKDDEWRAVRSDi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 99 ----RDRIYSL-PEMTEDDgmAVAE-LETEFAEMDGYTAESRAGELLLGLGIGIEQHNGPMSEVSPGWKLRVLLAQALFS 172
Cdd:PRK15079 101 qmifQDPLASLnPRMTIGE--IIAEpLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 173 DPEVLLLDEPTNHLDINTIRWLENVLTQRNSLM----IIISHDRhflnSVCTHMAD 224
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglslIFIAHDL----AVVKHISD 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
318-506 |
2.36e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 318 QAVV-VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPD--------------------AGSI 376
Cdd:PRK09984 2 QTIIrVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqregrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 KwTESAEIGYYAQDH------------------AHDFEDECtlFDWMG--QWTQGGEQLVRgtLGRMLFSNdeilKSVKV 436
Cdd:PRK09984 82 R-KSRANTGYIFQQFnlvnrlsvlenvligalgSTPFWRTC--FSWFTreQKQRALQALTR--VGMVHFAH----QRVST 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 437 ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMES----IEALNLALENYPGTLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESarivMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
322-520 |
2.48e-09 |
|
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: 59.82 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTL--VNELTPDAGSIKWTES--AEIGY-----YAQDHA 392
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVAlcEKCGYverpsKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 393 HDFEDECTLFD---W----------------MGQWTQG--GEQLV---------------RGTLGRMLfsndEILKSVKV 436
Cdd:TIGR03269 83 PVCGGTLEPEEvdfWnlsdklrrrirkriaiMLQRTFAlyGDDTVldnvlealeeigyegKEAVGRAV----DLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 ----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESI----EALNLALENYPGTLIFVSHDREFVSSLATR 502
Cdd:TIGR03269 159 shrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*...
gi 1502692530 503 IIELSpSGVIDFSGTYDD 520
Cdd:TIGR03269 239 AIWLE-NGEIKEEGTPDE 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
2.48e-09 |
|
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: 56.55 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGP--KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPNVRLGKLRQDQFAY- 76
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLdgVPVSDLEKALSSLISVl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 -EEFTVLDTVIMGHeelwkvkaerdriyslpemteddgmavaeLETEFaemdgytaesragelllglgigieqhngpmse 155
Cdd:cd03247 81 nQRPYLFDTTLRNN-----------------------------LGRRF-------------------------------- 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 156 vSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISH 210
Cdd:cd03247 100 -SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITH 155
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-294 |
3.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFE-----NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlEPNVRLGKLRQDQFAY 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI--EWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 EEftVLDTVIMG---HEELWKVKAERDRI--------YSLPEMT-EDD--------GMAVAE---LETEFAEMDG----Y 129
Cdd:PRK13651 81 EK--VLEKLVIQktrFKKIKKIKEIRRRVgvvfqfaeYQLFEQTiEKDiifgpvsmGVSKEEakkRAAKYIELVGldesY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 130 TAESragelllglgigieqhngPMsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTIRWLE--NVLTQRNSLMI 206
Cdd:PRK13651 159 LQRS------------------PF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTII 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 207 IISHDrhfLNSVcthmadLDYGELRLFPGN----YDEyMTVATQSREQLLADNakkKAQISELQSFVSRFSANASKAKQA 282
Cdd:PRK13651 220 LVTHD---LDNV------LEWTKRTIFFKDgkiiKDG-DTYDILSDNKFLIEN---NMEPPKLLNFVNKLEKKGIDVPKV 286
|
330
....*....|..
gi 1502692530 283 TSRAKQIDKIQL 294
Cdd:PRK13651 287 TSIEELASEINM 298
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
3.68e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE---------------PNVRLGKLRQDQFAYEEFTVLD 83
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 84 TVIMgheelwkvkaerdriyslPEMTedDGMAVAELETEFAEM-DGYTAESRAgelllglgigieqHNGPmSEVSPGWKL 162
Cdd:PRK11629 107 NVAM------------------PLLI--GKKKPAEINSRALEMlAAVGLEHRA-------------NHRP-SELSGGERQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRN----SLMIIISHD 211
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHD 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-228 |
4.09e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.35 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 4 TANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPnvrlGKLRQDQFAYEEftvlD 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIAR----G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 84 TVIMGHEELWK-VKAERDRIYSLPEMTEDDGmavaeLETEFAEMDGYTAESRagelllglgigieqhngPMSEVSPGWKL 162
Cdd:cd03231 75 LLYLGHAPGIKtTLSVLENLRFWHADHSDEQ-----VEEALARVGLNGFEDR-----------------PVAQLSAGQQR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVL---TQRNSLMIIISHdrHFLNSVCTHMADLDYG 228
Cdd:cd03231 133 RVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaghCARGGMVVLTTH--QDLGLSEAGARELDLG 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-187 |
4.10e-09 |
|
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: 56.88 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV--------MLEPNVR-LGKLRQDQFAY 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRdIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 EEFTVLDTVIMGheeLWKVKAERDRIyslpemteddgmavAELETEFAEMDGYTAEsragelllglgigieQHNGPmSEV 156
Cdd:cd03301 85 PHMTVYDNIAFG---LKLRKVPKDEI--------------DERVREVAELLQIEHL---------------LDRKP-KQL 131
|
170 180 190
....*....|....*....|....*....|.
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-527 |
4.59e-09 |
|
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: 57.16 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------KWTESaEIGY---------------- 386
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlRWLRS-QIGLvsqepvlfdgtiaeni 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 -YAQDHAHDFEDE-----CTLFDWMGQWTQGGEQLVrGTLGRMLfsndeilksvkviSGGEQGRMLFGKLILQKPNVLVM 460
Cdd:cd03249 98 rYGKPDATDEEVEeaakkANIHDFIMSLPDGYDTLV-GERGSQL-------------SGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 461 DEPTNHLDMES----IEALNLALENYpgTLIFVSHdRefVSSL--ATRIIELSPSGVIDfSGTYDDYLRSQGV 527
Cdd:cd03249 164 DEATSALDAESeklvQEALDRAMKGR--TTIVIAH-R--LSTIrnADLIAVLQNGQVVE-QGTHDELMAQKGV 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-219 |
4.75e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGdLEPSG---------GQVMLEPNVR------LGKLR 70
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdgeiywsGSPLKASNIRdteragIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 QDQFAYEEFTVLDTVIMGHEelwkvkaerdriyslpeMTEDDGMavaeleTEFAEMdgytaESRAGELLLGLGIGIEQHN 150
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNE-----------------ITLPGGR------MAYNAM-----YLRAKNLLRELQLDADNVT 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 151 GPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNSVC 219
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVC 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-187 |
5.09e-09 |
|
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: 56.93 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQF-GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-------PNVRL----GKL 69
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgedireqDPVELrrkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTV-IMGHEELWKVKAERDRIYSLPEMTeddGMAVAELetefaeMDGYTaesragelllglgigieq 148
Cdd:cd03295 81 IQQIGLFPHMTVEENIaLVPKLLKWPKEKIRERADELLALV---GLDPAEF------ADRYP------------------ 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1502692530 149 hngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:cd03295 134 -----HELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
334-500 |
5.92e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWTESAEIGYYAQDHAHD--------------FEDeC 399
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTvrkrmsmlfqsgalFTD-M 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLFD---W-MGQWTQGGEQLVRGTLgrMLfsndeILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEP-- 463
Cdd:PRK11831 100 NVFDnvaYpLREHTQLPAPLLHSTV--MM-----KLEAVGLrgaaklmpseLSGGMARRAALARAIALEPDLIMFDEPfv 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 464 -----TNHLDMESIEALNLALenypG-TLIFVSHDREFVSSLA 500
Cdd:PRK11831 173 gqdpiTMGVLVKLISELNSAL----GvTCVVVSHDVPEVLSIA 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
6.30e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.95 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQF--GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPS------GGQVMLEPNV-----RLGK 68
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEagtitvGGMVLSEETVwdvrrQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 69 LRQ---DQFAYEefTVLDTVIMGHEelwKVKAERDriyslpEMTEDDGMAVAELE-TEFAemdgytaesragelllglgi 144
Cdd:PRK13635 86 VFQnpdNQFVGA--TVQDDVAFGLE---NIGVPRE------EMVERVDQALRQVGmEDFL-------------------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 145 gieqHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRWLENvltQRNSLMIIISHD 211
Cdd:PRK13635 135 ----NREP-HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-516 |
6.64e-09 |
|
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: 56.51 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELtpDAGSIKwteSAEIGYYAQD-HAHDFEDECTLFDWMGQWTQGg 412
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTT---SGQILFNGQPrKPDQFQKCVAYVRQDDILLPG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 413 eqL-VRGTL-------GRMLFSNDEILKSVKV------------------ISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:cd03234 96 --LtVRETLtytailrLPRKSSDAIRKKRVEDvllrdlaltriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 467 LDmeSIEALNLA--LENYP--GTLIFVS-HD-REFVSSLATRIIELSpSGVIDFSG 516
Cdd:cd03234 174 LD--SFTALNLVstLSQLArrNRIVILTiHQpRSDLFRLFDRILLLS-SGEIVYSG 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-210 |
7.11e-09 |
|
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: 56.39 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRqDQFAY--EEFTVLDTVImg 88
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDgvdiRDLNLRWLR-SQIGLvsQEPVLFDGTI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 89 heelwkvkaeRDRI-YSLPEMTEDDGMAVAELE--TEFAEM--DGYTAESragelllglgigieqhnGPM-SEVSPGWKL 162
Cdd:cd03249 94 ----------AENIrYGKPDATDEEVEEAAKKAniHDFIMSlpDGYDTLV-----------------GERgSQLSGGQKQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISH 210
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRamKGRTTIVIAH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-183 |
7.22e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNV--RLG--- 67
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaiALGigm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 68 -----KLrqdqfaYEEFTVLDTVIMGHEELWKVKAERDRiyslpemteddgmAVAELEtEFAEMDGYTAESRAgelllgl 142
Cdd:COG3845 85 vhqhfML------VPNLTVAENIVLGLEPTKGGRLDRKA-------------ARARIR-ELSERYGLDVDPDA------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1502692530 143 gigieqhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPT 183
Cdd:COG3845 138 ---------KVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-226 |
8.42e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.90 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-----------PNVRLGKLRQDQFAY-EEF--- 79
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaSPREILALRRRTIGYvSQFlrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 ----TVLDTVimgheelwkvkAErdriySLPEMTEDDGMAVAELETEFAEMdgytaesragelllglgigieqhNGPMS- 154
Cdd:COG4778 105 iprvSALDVV-----------AE-----PLLERGVDREEARARARELLARL-----------------------NLPERl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 -EVSP-----GWKLRVLLAQALFSDPEVLLLDEPTNHLD-INTIRWLE--NVLTQRNSLMIIISHDRHFLNSVCTHMADL 225
Cdd:COG4778 146 wDLPPatfsgGEQQRVNIARGFIADPPLLLLDEPTASLDaANRAVVVEliEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
.
gi 1502692530 226 D 226
Cdd:COG4778 226 T 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
320-493 |
8.51e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRtLVNEL-TPDAGSI-----KWTESA----EIGYYAQ 389
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLeKPTEGQIfidgeDVTHRSiqqrDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 390 DHAhdfedectLFDWMGQwtqgGEQLVRGTlgRML-FSNDEILKSVK-----------------VISGGEQGRMLFGKLI 451
Cdd:PRK11432 86 SYA--------LFPHMSL----GENVGYGL--KMLgVPKEERKQRVKealelvdlagfedryvdQISGGQQQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 452 LQKPNVLVMDEPTNHLD------M-ESIEALNlalENYPGTLIFVSHDR 493
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDanlrrsMrEKIRELQ---QQFNITSLYVTHDQ 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
8.83e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFA----- 75
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAqlgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 --YEEFTVLDtvimgheelwkvkaerdriyslpEMTEDDGMAVAELET---------EFAEMDGYTAEsragelLLGLGI 144
Cdd:PRK09700 84 iiYQELSVID-----------------------ELTVLENLYIGRHLTkkvcgvniiDWREMRVRAAM------MLLRVG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 145 GIEQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWL---ENVLTQRNSLMIIISHDRHFLNSVC 219
Cdd:PRK09700 135 LKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRIC 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-507 |
9.42e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 307 IRFEQTKKLH---RQAVvvermaKGFDgttlfkdfsFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------- 376
Cdd:PRK10908 2 IRFEHVSKAYlggRQAL------QGVT---------FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 ---KWTE----SAEIGYYAQDHaHDFEDEcTLFDWMGQ----WTQGGEQLVRgtlgRMLFSNDEI-----LKSVKV-ISG 439
Cdd:PRK10908 67 trlKNREvpflRRQIGMIFQDH-HLLMDR-TVYDNVAIpliiAGASGDDIRR----RVSAALDKVglldkAKNFPIqLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 440 GEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEALNLALE--NYPG-TLIFVSHDREFVSSLATRIIELS 507
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEefNRVGvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
1.14e-08 |
|
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: 55.17 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 13 PKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVrlgklrqdqfAY---EEF----TVLDTV 85
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI----------AYvsqEPWiqngTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 IMG----HEELWKVkaerdriyslpemteddgMAVAELETEFAEMDGytaesragelllglgigieqhnGPMSEV----- 156
Cdd:cd03250 87 LFGkpfdEERYEKV------------------IKACALEPDLEILPD----------------------GDLTEIgekgi 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 157 --SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWL-ENVLT---QRNSLMIIISHDRHFL 215
Cdd:cd03250 127 nlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILgllLNNKTRILVTHQLQLL 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.38e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV-----MLEPNVRLGK------- 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 69 LRQD-QFAYEEF------TVLDTVIMGHEelwKVKAE-RDRIYSLP-EMTEDDGMAVAEletefaemDGYTaesragell 139
Cdd:PRK11264 83 LRQHvGFVFQNFnlfphrTVLENIIEGPV---IVKGEpKEEATARArELLAKVGLAGKE--------TSYP--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 140 lglgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRwlenVLTQRNSLMIIISHDR 212
Cdd:PRK11264 143 --------------RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEM 204
|
250
....*....|....*.
gi 1502692530 213 HFLNSVCTHMADLDYG 228
Cdd:PRK11264 205 SFARDVADRAIFMDQG 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-504 |
2.23e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 334 LFkDFSFTVEASERVAIIGPNGIGKTTLLRTLvNEL-TPDAGSIkwtesaEIgyyAQDHahdfedectlFDWMGQWTQGG 412
Cdd:PRK11124 18 LF-DITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLeMPRSGTL------NI---AGNH----------FDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 413 EQLVRGTLGrMLFSN--------------------------------DEILKSVKV----------ISGGEQGRMLFGKL 450
Cdd:PRK11124 77 IRELRRNVG-MVFQQynlwphltvqqnlieapcrvlglskdqalaraEKLLERLRLkpyadrfplhLSGGQQQRVAIARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 451 ILQKPNVLVMDEPTNHLDME---SIEALNLALENYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRVV 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-504 |
2.48e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.59 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 338 FSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWTESaeigyyaQDHAHD----------FEdECTLFDWMGQ 407
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG-------QDHTTTppsrrpvsmlFQ-ENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 WTQGG-------------EQLVRGTLGRMLFSND-EILKSvkVISGGEQGRMLFGK-LILQKPnVLVMDEPTNHLD---- 468
Cdd:PRK10771 89 AQNIGlglnpglklnaaqREKLHAIARQMGIEDLlARLPG--QLSGGQRQRVALARcLVREQP-ILLLDEPFSALDpalr 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1502692530 469 MESIEALNLALENYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSL 201
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
330-476 |
3.08e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI----KWTESAE----IGYYAQ--------DHAH 393
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDrsrfMAYLGHlpglkadlSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 394 DFEDECTLFDWMGQWTQGGEQLVRGtlgrmLFSNDEILksVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIE 473
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPGSALAIVG-----LAGYEDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
|
...
gi 1502692530 474 ALN 476
Cdd:PRK13543 175 LVN 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-517 |
3.52e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI---------------KWTESAEIGYYAQDH--- 391
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRESVGMVFQDPDNqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 -AHDFEDECTLFDWMGQWTQGGEQLVRGTLGRMLFSNDEIlKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDME 470
Cdd:PRK13636 97 sASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 471 SI-EALNLALENYPG---TLIFVSHDREFVSSLATRIIELSPSGVIdFSGT 517
Cdd:PRK13636 176 GVsEIMKLLVEMQKElglTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
321-377 |
3.89e-08 |
|
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: 54.20 E-value: 3.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 321 VVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK 377
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL 59
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
4.10e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-PNV-RL-GKLRQDQFAYEE 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgTDVsRLhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 F------TVLDTVIMGheelwkvkaerdrIYSLPEMTEDDGMAVAELETEFAEMD--GYTAESRAgelllglgigieqhn 150
Cdd:PRK10851 83 YalfrhmTVFDNIAFG-------------LTVLPRRERPNAAAIKAKVTQLLEMVqlAHLADRYP--------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 151 gpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDR 212
Cdd:PRK10851 135 ---AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
321-376 |
4.20e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 54.26 E-value: 4.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 321 VVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI 376
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI 60
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-212 |
4.62e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE-PNVRLGKLRQDQF-----AYEEF 79
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgEDVTHRSIQQRDIcmvfqSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 80 ---TVLDTVIMGHEELWKVKAER-DRIYSLPEMTEDDGMAvaeletefaemDGYtaesragelllglgigieqhngpMSE 155
Cdd:PRK11432 91 phmSLGENVGYGLKMLGVPKEERkQRVKEALELVDLAGFE-----------DRY-----------------------VDQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 156 VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDIN-------TIRWLEnvlTQRNSLMIIISHDR 212
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANlrrsmreKIRELQ---QQFNITSLYVTHDQ 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-389 |
4.76e-08 |
|
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: 53.24 E-value: 4.76e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWteSAEIGYYAQ 389
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQ 73
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
4.87e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF-GPKPLFE---NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFA- 75
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALSEKELRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 --------YEEF------TVLDTVimgheelwkvkaerdriySLPemTEDDGMAVAELE---TEFAEMDGYTAesragel 138
Cdd:PRK11153 80 arrqigmiFQHFnllssrTVFDNV------------------ALP--LELAGTPKAEIKarvTELLELVGLSD------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 139 llglgigieQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRN---SLMII-ISHDRHF 214
Cdd:PRK11153 133 ---------KADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINrelGLTIVlITHEMDV 203
|
250
....*....|....*.
gi 1502692530 215 LNSVCTHMADLDYGEL 230
Cdd:PRK11153 204 VKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
4.89e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.23 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGP--KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV----RLGKLRQ--- 71
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskeNLKEIRKkig 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 -------DQFAyeEFTVLDTVIMGHEelwkvkaerDRIYSLPEMTEddgmAVAELETEfAEMDGYTAESragelllglgi 144
Cdd:PRK13632 87 iifqnpdNQFI--GATVEDDIAFGLE---------NKKVPPKKMKD----IIDDLAKK-VGMEDYLDKE----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 145 gieqhngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRWLENvltQRNSLMIIISHD 211
Cdd:PRK13632 140 -------P-QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreiKKIMVDLRK---TRKKTLISITHD 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-210 |
7.64e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFE-----NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML------EPNVRLGKLR 70
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 QD---QFAYEEFTVLDTVImgheelwkvkaERDRIYSLPEMTEDDG---MAVAE-LETEFAEMDGYTAESragelllglg 143
Cdd:PRK13637 83 KKvglVFQYPEYQLFEETI-----------EKDIAFGPINLGLSEEeieNRVKRaMNIVGLDYEDYKDKS---------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 144 igieqhngPMsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRWLENvltQRNSLMIIISH 210
Cdd:PRK13637 142 --------PF-ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSH 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
8.27e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGdLEPSG---GQVMLEpnvrlGKLRQDQfayeefTVL 82
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFE-----GEELQAS------NIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 DT-----VIMgHEELWKVkaerdriyslPEMTEDDGMAVAELETEFAEMDgYTAESRAGELLLGLGIGIEQHNGPMSEVS 157
Cdd:PRK13549 78 DTeragiAII-HQELALV----------KELSVLENIFLGNEITPGGIMD-YDAMYLRAQKLLAQLKLDINPATPVGNLG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 158 PGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDrhfLNSV 218
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISHK---LNEV 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
336-519 |
8.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGYYAQDHAHDFEDECT--------------L 401
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLViqktrfkkikkikeI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 FDWMGQWTQGGE-QLVRGTLGR--------MLFSNDEILKSVKVI------------------SGGEQGRMLFGKLILQK 454
Cdd:PRK13651 104 RRRVGVVFQFAEyQLFEQTIEKdiifgpvsMGVSKEEAKKRAAKYielvgldesylqrspfelSGGQKRRVALAGILAME 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 455 PNVLVMDEPTNHLDME-SIEALNL--ALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYD 519
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQgVKEILEIfdNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-526 |
9.78e-08 |
|
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: 52.87 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI------------KWTEsAEIGYYAQDH------ 391
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpAWLR-RQVGVVLQENvlfnrs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 -------------------------AHDFedectlfdwMGQWTQGGEQLVrGTLGRMLfsndeilksvkviSGGEQGRML 446
Cdd:cd03252 92 irdnialadpgmsmervieaaklagAHDF---------ISELPEGYDTIV-GEQGAGL-------------SGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 447 FGKLILQKPNVLVMDEPTNHLDMESIEAL--NLALENYPGTLIFVSHDREFVSSlATRIIELSpSGVIDFSGTYDDYLRS 524
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAImrNMHDICAGRTVIIIAHRLSTVKN-ADRIIVME-KGRIVEQGSHDELLAE 226
|
..
gi 1502692530 525 QG 526
Cdd:cd03252 227 NG 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-187 |
1.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNV--------RLGKLRQD-----QFA----YEEfTV 81
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkKLKPLRKKvgivfQFPehqlFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 LDTVIMGheelwkvkaerdriyslPE---MTEDDGMAVAEletEFAEMDGYTAESRagelllglgigieqHNGPMsEVSP 158
Cdd:PRK13634 104 EKDICFG-----------------PMnfgVSEEDAKQKAR---EMIELVGLPEELL--------------ARSPF-ELSG 148
|
170 180
....*....|....*....|....*....
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
335-491 |
1.23e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 335 FKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI-------------------------------------- 376
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydhhylhrqvalvgqepvlfsgsvrenia 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 ---KWTESAEIGYYAQD-HAHDFEDECTlfdwMGQWTQGGEqlvRGTLgrmlfsndeilksvkvISGGEQGRMLFGKLIL 452
Cdd:TIGR00958 577 yglTDTPDEEIMAAAKAaNAHDFIMEFP----NGYDTEVGE---KGSQ----------------LSGGQKQRIAIARALV 633
|
170 180 190
....*....|....*....|....*....|....*....
gi 1502692530 453 QKPNVLVMDEPTNHLDMESIEALNLALENYPGTLIFVSH 491
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-210 |
1.27e-07 |
|
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: 52.41 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPK--PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLR----- 70
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidiSTIPLEDLRsslti 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 --QDQfayeeftvldTVIMGheelwKVKAERDRiyslpemteddgmavaelETEFAEMDGYTAESRAgelllglgigieq 148
Cdd:cd03369 87 ipQDP----------TLFSG-----TIRSNLDP------------------FDEYSDEEIYGALRVS------------- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 149 hnGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISH 210
Cdd:cd03369 121 --EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAH 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-210 |
1.28e-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: 52.61 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPN----VRLGKLR-------QDQFAYEEfTVL 82
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdISRKSLRsmigvvlQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 DTVIMGHeelwkvkaerdriyslPEMTEDDGMAVAELE--TEFAEM--DGYTAESRagelllglgigieqHNGpmSEVSP 158
Cdd:cd03254 95 ENIRLGR----------------PNATDEEVIEAAKEAgaHDFIMKlpNGYDTVLG--------------ENG--GNLSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSlmIIISH 210
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGRTS--IIIAH 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
1.38e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKIL------------GGDLEPSGGQV-----MLEPNV 64
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDVLLGGRSIfnyrdVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 65 RLGKLRQDQFAYeEFTVLDTVIMGHeelwkvkaerdRIYSLPEMTEDDGMAVAELeTEFAEMDGytAESRAGelllglgi 144
Cdd:PRK14271 102 RVGMLFQRPNPF-PMSIMDNVLAGV-----------RAHKLVPRKEFRGVAQARL-TEVGLWDA--VKDRLS-------- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 145 gieqhNGPMsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT-------IRWLENVLTqrnslMIIISHD 211
Cdd:PRK14271 159 -----DSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTtekieefIRSLADRLT-----VIIVTHN 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-508 |
1.51e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF----GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQdqfay 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 77 eeftVLDTVIMGHEELWKVK-AERDRIYSLPeMTEDD-----GMAVAE---LETEFAEMDGYTAESRAGELLLGLGIGIE 147
Cdd:PRK10261 87 ----VIELSEQSAAQMRHVRgADMAMIFQEP-MTSLNpvftvGEQIAEsirLHQGASREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 148 QHNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDIN---TIRWLENVLTQRNSL-MIIISHDRhflnSVCTHMA 223
Cdd:PRK10261 162 LSRYP-HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMgVIFITHDM----GVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 224 DLdygELRLFPGNydeymTVATQSREQLLADNAKKK-----AQISEL-----QSFVSRFSANAskAKQATSRAKQIDKIQ 293
Cdd:PRK10261 237 DR---VLVMYQGE-----AVETGSVEQIFHAPQHPYtrallAAVPQLgamkgLDYPRRFPLIS--LEHPAKQEPPIEQDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 294 LAEVKPSSRVSPFI-RFEQT----KKLHRQAVVVERMakgfdgttlfkdfSFTVEASERVAIIGPNGIGKTTLLRTLVNE 368
Cdd:PRK10261 307 VVDGEPILQVRNLVtRFPLRsgllNRVTREVHAVEKV-------------SFDLWPGETLSLVGESGSGKSTTGRALLRL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 369 LTPDAGSIKW------TESA--------EIGYYAQDHAHDFEDECTLFDWMGQ------WTQGGEQLVRGT--LGRMLFS 426
Cdd:PRK10261 374 VESQGGEIIFngqridTLSPgklqalrrDIQFIFQDPYASLDPRQTVGDSIMEplrvhgLLPGKAAAARVAwlLERVGLL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 427 NDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMeSIEA--LNLALE---NYPGTLIFVSHDREFVSSLAT 501
Cdd:PRK10261 454 PEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDlqrDFGIAYLFISHDMAVVERISH 532
|
570
....*....|....*
gi 1502692530 502 R--------IIELSP 508
Cdd:PRK10261 533 RvavmylgqIVEIGP 547
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
2.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 11 FGPKPLFEnVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKLRQDQFA--------------- 75
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvrkkvgvvfqfpes 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 --YEEfTVLDTVIMGHEELWKVKAERDRIYSlpemtedDGMAVAELETEFAEMDGYtaesragelllglgigieqhngpm 153
Cdd:PRK13643 96 qlFEE-TVLKDVAFGPQNFGIPKEKAEKIAA-------EKLEMVGLADEFWEKSPF------------------------ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 154 sEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVlTQRNSLMIIISH 210
Cdd:PRK13643 144 -ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESI-HQSGQTVVLVTH 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
320-511 |
2.29e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.11 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLR-----------------TLVNELTPdagsikwtESA 382
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiagleditsgdlfigeKRMNDVPP--------AER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 383 EIGYYAQDHA---HdfedeCTLFDWMgqwtqggeqlvrgTLGRMLFSND--EILKSV-----------------KVISGG 440
Cdd:PRK11000 76 GVGMVFQSYAlypH-----LSVAENM-------------SFGLKLAGAKkeEINQRVnqvaevlqlahlldrkpKALSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 441 EQGRMLFGKLILQKPNVLVMDEPTNHLD------MES-IEALNLALENypgTLIFVSHDREFVSSLATRIIELSPSGV 511
Cdd:PRK11000 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-523 |
2.35e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 338 FSFTVEASERVAIIGPNGIGKTTLLRTLVNeLTPDAGSIKWTESAEIGYYAQDHAH---------------DFEDECTLF 402
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARhraylsqqqtppfamPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 403 DWMGQWTQGGEQLVRgTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQ-----KPN--VLVMDEPTNHLDMESIEAL 475
Cdd:PRK03695 94 QPDKTRTEAVASALN-EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 476 NLALENYP---GTLIFVSHDREFVSSLATRIIELSpSGVIDFSGTYDDYLR 523
Cdd:PRK03695 173 DRLLSELCqqgIAVVMSSHDLNHTLRHADRVWLLK-QGKLLASGRRDEVLT 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-504 |
2.59e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI-----------KWTESAEIGYYAQ-------------DH 391
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHKIGMVFQnpdnqfvgatvedDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 392 AHDFEDECTLFDWMGQWTQGGEQLVrgtlGRMLFSNDEILKsvkvISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD--- 468
Cdd:PRK13650 104 AFGLENKGIPHEEMKERVNEALELV----GMQDFKEREPAR----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpeg 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1502692530 469 -MESIEALNLALENYPGTLIFVSHDREFVsSLATRII 504
Cdd:PRK13650 176 rLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
2.73e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.39 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 17 FENVSVKFGAGNR-----------------YGLIGANGCGKSTFMKILGGdLE-PSGGQVMLE-------PNVRLGKLRQ 71
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINL-LErPTSGSVLVDgvdltalSERELRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 D------QFA-YEEFTVLDTVimghE---ELWKV-KAERDRIyslpemteddgmaVAELetefAEMDGYTAESRAGelll 140
Cdd:COG1135 83 KigmifqHFNlLSSRTVAENV----AlplEIAGVpKAEIRKR-------------VAEL----LELVGLSDKADAY---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 141 glgigieqhngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLM----IIISHDRHFLN 216
Cdd:COG1135 138 -----------P-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELgltiVLITHEMDVVR 205
|
250
....*....|....
gi 1502692530 217 SVCTHMADLDYGEL 230
Cdd:COG1135 206 RICDRVAVLENGRI 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-217 |
3.28e-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: 51.07 E-value: 3.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPTNHLDINTIRW-----LENVLTQRNSLMIIISHDRHFLNS 217
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
348-468 |
3.63e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 348 VAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAE--IGYYA----QDHahdFEDectLFDwmGQWT-----QGGEQL- 415
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDevLKRFRgtelQNY---FKK---LYN--GEIKvvhkpQYVDLIp 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 416 --VRGTLGRMLFSNDE---------------IL-KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:PRK13409 174 kvFKGKVRELLKKVDErgkldevverlglenILdRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
321-504 |
3.65e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 321 VVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAeiGYYAQDHAHDFEDECT 400
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--GQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 401 LF--DW------------MGQWTQG--GEQL----------VRGT----LGRMLFSNDEILKSVKVISGGEQGRMLFGKL 450
Cdd:PRK11701 86 LLrtEWgfvhqhprdglrMQVSAGGniGERLmavgarhygdIRATagdwLERVEIDAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 451 ILQKPNVLVMDEPTNHLDMeSIEA------------LNLAlenypgtLIFVSHDREFVSSLATRII 504
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDV-SVQArlldllrglvreLGLA-------VVIVTHDLAVARLLAHRLL 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-376 |
3.70e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.63 E-value: 3.70e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1502692530 333 TLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI 376
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
330-491 |
4.31e-07 |
|
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: 50.60 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVN--ELTPDAGSIkwtesaeigyyaqdhahdfedectLFDwmgq 407
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI------------------------LFK---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 408 wtqgGEQLV------RGTLGRML----------FSNDEILKSVKV-ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDME 470
Cdd:cd03217 63 ----GEDITdlppeeRARLGIFLafqyppeipgVKNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180
....*....|....*....|....
gi 1502692530 471 SIEALNLALENY--PGT-LIFVSH 491
Cdd:cd03217 139 ALRLVAEVINKLreEGKsVLIITH 162
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-187 |
5.09e-07 |
|
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: 50.24 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSG--GQVML--------EPNVRLGKLRQDQFAYEEFTVld 83
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLIngrpldkrSFRKIIGYVPQDDILHPTLTV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 84 tvimgHEELWkvkaerdriyslpemteddgmavaeletefaemdgYTAEsragelllglgigieqhngpMSEVSPGWKLR 163
Cdd:cd03213 100 -----RETLM-----------------------------------FAAK--------------------LRGLSGGERKR 119
|
170 180
....*....|....*....|....
gi 1502692530 164 VLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLD 143
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
338-468 |
5.27e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.99 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 338 FSFTVEASERVAIIGPNGIGKTTLLrTLVNELTPDAGSI--------KWT--ESAEI-GYYAQDHAHDFEDECTLFDWMG 406
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLL-ARMAGLLPGQGEIllngrplsDWSaaELARHrAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 407 QWTQGGEQLVRGTLGRM---LFSNDEILKSVKVISGGEQGRMLFGKLILQ-------KPNVLVMDEPTNHLD 468
Cdd:COG4138 94 QPAGASSEAVEQLLAQLaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
332-525 |
5.99e-07 |
|
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: 50.66 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 332 TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRtLVNEL-TPDAGSIKW--------------TESAEIGYYAQdHAHDFE 396
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLeRPTSGSVLVdgtdltllsgkelrKARRRIGMIFQ-HFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 DEcTLFD----WMGQWTQGGEQLVRgtlgRMlfsnDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:cd03258 96 SR-TVFEnvalPLEIAGVPKAEIEE----RV----LELLELVGLedkadaypaqLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 463 PTNHLDME---SIEALNLALENYPG-TLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLRSQ 525
Cdd:cd03258 167 ATSALDPEttqSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-248 |
6.11e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.61 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 20 VSVKFGAGNRYGLIGANGCGKSTFMKILGGdLEPSGGQVMLE-------PNVRLGKLR----QDQ---FAYEEFTVLDTv 85
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwSAAELARHRaylsQQQsppFAMPVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 86 imgHeelwkvkaerdriYSLPEMTEDDGMAVAELETEFAEMDGYtaeSRagelllglgigieqhngPMSEVSPG-WKlRV 164
Cdd:COG4138 93 ---H-------------QPAGASSEAVEQLLAQLAEALGLEDKL---SR-----------------PLTQLSGGeWQ-RV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 165 LLAQALFS-DPEV------LLLDEPTNHLDIN----TIRWLENVLTQRNSlmIIIS-HDrhfLNSVCTHmAD----LDYG 228
Cdd:COG4138 136 RLAAVLLQvWPTInpegqlLLLDEPMNSLDVAqqaaLDRLLRELCQQGIT--VVMSsHD---LNHTLRH-ADrvwlLKQG 209
|
250 260
....*....|....*....|
gi 1502692530 229 ELrLFPGNYDEYMTVATQSR 248
Cdd:COG4138 210 KL-VASGETAEVMTPENLSE 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-231 |
6.18e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPN---VRLGKLRQDQFAYEEFTVLDTVIMGHEE 91
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsilTNISDVHQNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 92 LWKVKAERdriyslpemteddGMAVAELEtefaEMDGYTAESRAGELLLGLGIgieqhngpmSEVSPGWKLRVLLAQALF 171
Cdd:TIGR01257 2033 LYLYARLR-------------GVPAEEIE----KVANWSIQSLGLSLYADRLA---------GTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 172 SDPEVLLLDEPTNHLDINTIRWLENVLT---QRNSLMIIISHDRHFLNSVCTHMADLDYGELR 231
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVsiiREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
6.23e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF-GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPNVRLGKLRQDQFAYE 77
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 EFTVLDtvimgheelwkvkaerDRIYSlPEMTEDDGMAVAELetefaEMDGYTAESRAGELLLGLGIGIEQHNGPmSEVS 157
Cdd:PRK13652 83 VFQNPD----------------DQIFS-PTVEQDIAFGPINL-----GLDEETVAHRVSSALHMLGLEELRDRVP-HHLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 158 PGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWL---ENVLTQRNSLMIIIShdRHFLNSVcTHMADLDY 227
Cdd:PRK13652 140 GGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELidfLNDLPETYGMTVIFS--THQLDLV-PEMADYIY 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
7.26e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQ-------VMLEPNVRLGKLRQDQFAYeeftvldtvIMghe 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLRREHFGF---------IF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 91 elwkvkaerDRIYSLPEMTEDDGMavaELETEFAEMDGYTAESRAGELLLGLGIGIEQHNGPmSEVSPGWKLRVLLAQAL 170
Cdd:PRK10535 93 ---------QRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1502692530 171 FSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHD 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQlrdRGHTVIIVTHD 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-504 |
7.36e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.45 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWTESAEIGYYAQDHAHDFEDeC 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQD-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 400 TLFDW-----------MGQWTQGGEQLVRgTLGRMLFSNDeilkSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:PRK11247 91 RLLPWkkvidnvglglKGQWRDAALQALA-AVGLADRANE----WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 469 ------MES-IEALnlaLENYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK11247 166 altrieMQDlIESL---WQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
154-229 |
7.50e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 154 SEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRWLENVLTQRNSL-MIIISHDRHFLNSVCTHMADLDYGE 229
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLQQKHQLaYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
331-491 |
8.55e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNELTPD-AGSIKWTESAEIGYYAQ----------------DHAH 393
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQrpymtlgtlrdqiiypDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 394 DFEDEctlfdwmGQWTQGGEQ-LVRGTLGRMLFSN---DEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM 469
Cdd:TIGR00954 543 DMKRR-------GLSDKDLEQiLDNVQLTHILEREggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|..
gi 1502692530 470 ESIEALNLALENYPGTLIFVSH 491
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
9.09e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF-GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----------PNVR--LG 67
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklQGIRklVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 68 KLRQD---QFAYEefTVLDTVIMGHEELwkvkaerdriySLP--EMTEDDGMAVAELETEfaemdgytaesragelllgl 142
Cdd:PRK13644 81 IVFQNpetQFVGR--TVEEDLAFGPENL-----------CLPpiEIRKRVDRALAEIGLE-------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 143 gigIEQHNGPMSeVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT-IRWLENV--LTQRNSLMIIISHDRHFLnsvc 219
Cdd:PRK13644 128 ---KYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITHNLEEL---- 199
|
250
....*....|....*..
gi 1502692530 220 tHMAD----LDYGELRL 232
Cdd:PRK13644 200 -HDADriivMDRGKIVL 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-291 |
9.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 10 QFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNvrlgklrqdqFAYEEftvldtvimgh 89
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS----------IAYVP----------- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 90 EELWKVKAE-RDRI-YSLPEMTED--DGMAVAELETEFAEMDGytaesragelllglgigieqhnGPMSEV-------SP 158
Cdd:PTZ00243 728 QQAWIMNATvRGNIlFFDEEDAARlaDAVRVSQLEADLAQLGG----------------------GLETEIgekgvnlSG 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 159 GWKLRVLLAQALFSDPEVLLLDEPTNHLDINT-IRWLENVLTQR--NSLMIIISHDRHFLnSVCTHMADLDYGELRlFPG 235
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGAlaGKTRVLATHQVHVV-PRADYVVALGDGRVE-FSG 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 236 NYDEYM------TVATQSREQLLADNAKKKAQISELQSFVSRFSANASKAKQATSRAKQIDK 291
Cdd:PTZ00243 864 SSADFMrtslyaTLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDG 925
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
330-468 |
9.93e-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: 51.83 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDA----GSIKWtesaeigyyaqdhahdfeDECTLFDWM 405
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqiDGVSW------------------NSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 GQWTQGGEQ--LVRGTLGRML-----FSNDEI--------LKSV----------------KVISGGEQGRMLFGKLILQK 454
Cdd:TIGR01271 1292 KAFGVIPQKvfIFSGTFRKNLdpyeqWSDEEIwkvaeevgLKSVieqfpdkldfvlvdggYVLSNGHKQLMCLARSILSK 1371
|
170
....*....|....
gi 1502692530 455 PNVLVMDEPTNHLD 468
Cdd:TIGR01271 1372 AKILLLDEPSAHLD 1385
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-472 |
1.04e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTES------------AEIGYY 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 388 AQDhAHDFEdECTLFDWMGQWTQGGEQLvrgTLGRMLFSNDEILKSVKV----------ISGGEQGRMLFGKLILQKPNV 457
Cdd:PRK10895 84 PQE-ASIFR-RLSVYDNLMAVLQIRDDL---SAEQREDRANELMEEFHIehlrdsmgqsLSGGERRRVEIARALAANPKF 158
|
170
....*....|....*
gi 1502692530 458 LVMDEPTNHLDMESI 472
Cdd:PRK10895 159 ILLDEPFAGVDPISV 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-183 |
1.09e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMlepnvrlgklrqdqFAYEEFT 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV--------------FDGKDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 81 VLDTVIMGHEELWKVKAERdRIYSlpEMTEDDGMAVAELeteFAEMDGYTAE-SRAGELLLGLGIGIEQHNGPMSEvspG 159
Cdd:PRK11614 71 DWQTAKIMREAVAIVPEGR-RVFS--RMTVEENLAMGGF---FAERDQFQERiKWVYELFPRLHERRIQRAGTMSG---G 141
|
170 180
....*....|....*....|....
gi 1502692530 160 WKLRVLLAQALFSDPEVLLLDEPT 183
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
155-513 |
1.23e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRWLENVLTQR-NSLMIIISHDrhfLNSVcthmadldygel 230
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQElNMGLLFITHN---LSIV------------ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 231 rlfpgnydeymtvatqsreQLLADNAK--KKAQISELQSFVSRFSANASKAKQatsrakqidkiQLAEVKPSSRVSPFIr 308
Cdd:PRK15134 221 -------------------RKLADRVAvmQNGRCVEQNRAATLFSAPTHPYTQ-----------KLLNSEPSGDPVPLP- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 309 fEQTKKLHRqavvVERMAKGF-----------DGTTLFKDFSFTVEASERVAIIGPNGIGKTT----LLRtlvneLTPDA 373
Cdd:PRK15134 270 -EPASPLLD----VEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 374 GSI--------KWTESAEIGYYAQDHAHdFEDECTLFD---WMGQWTQGGEQLVRGTLGRMLFSNDEILKSVKV------ 436
Cdd:PRK15134 340 GEIwfdgqplhNLNRRQLLPVRHRIQVV-FQDPNSSLNprlNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVgldpet 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 -------ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDmESIEALNLAL-----ENYPGTLIFVSHDREFVSSLATRII 504
Cdd:PRK15134 419 rhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALlkslqQKHQLAYLFISHDLHVVRALCHQVI 497
|
....*....
gi 1502692530 505 ELSPSGVID 513
Cdd:PRK15134 498 VLRQGEVVE 506
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-517 |
1.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkwtesaeigyYAQDHahDFEDECTLFDwmgqwtqggeql 415
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----------YVDGL--DTSDEENLWD------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 416 VRGTLGrMLFSN--------------------------------DEILKSVK----------VISGGEQGRMLFGKLILQ 453
Cdd:PRK13633 83 IRNKAG-MVFQNpdnqivativeedvafgpenlgippeeirervDESLKKVGmyeyrrhaphLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 454 KPNVLVMDEPTNHLD-------MESIEALNlalENYPGTLIFVSHDREFVSSlATRIIELSpSGVIDFSGT 517
Cdd:PRK13633 162 RPECIIFDEPTAMLDpsgrrevVNTIKELN---KKYGITIILITHYMEEAVE-ADRIIVMD-SGKVVMEGT 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
329-523 |
1.36e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 329 FDGTTLFkDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE---------------SAEIGYYAQDHAH 393
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 394 DFEDECTLFDW------MGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHL 467
Cdd:PRK13643 96 QLFEETVLKDVafgpqnFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 468 DMES-IEALNL--ALENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDfSGTYDDYLR 523
Cdd:PRK13643 176 DPKArIEMMQLfeSIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS-CGTPSDVFQ 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-78 |
1.48e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 1.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNvrlgKLRQDQFAYEE 78
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ----SIKKDLCTYQK 74
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
330-523 |
1.65e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 330 DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIGY---------------------YA 388
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLngeplaaidaprlarlravlpQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QDHAHDFE-DECTLFDWMGQWTQGGEQLVR--GTLGRMLFSNDE---ILKSVKVISGGEQGRMLFGKLILQ--------- 453
Cdd:PRK13547 92 AQPAFAFSaREIVLLGRYPHARRAGALTHRdgEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 454 KPNVLVMDEPTNHLDMESIEAL-----NLALENYPGTLIFVsHDREFVSSLATRIIELSpSGVIDFSGTYDDYLR 523
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRIAMLA-DGAIVAHGAPADVLT 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-183 |
1.67e-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: 48.97 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPnVRLGKLRQDQFA-------------YEEFTVLDT 84
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-RDITGLPPHERAragigyvpegrriFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 85 VIMGHEELWK--VKAERDRIYSL-PemteddgmavaeletEFAEMdgytAESRAgelllglgigieqhngpmSEVSPGWK 161
Cdd:cd03224 96 LLLGAYARRRakRKARLERVYELfP---------------RLKER----RKQLA------------------GTLSGGEQ 138
|
170 180
....*....|....*....|..
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPT 183
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-182 |
1.73e-06 |
|
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: 49.08 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPN----------VRLG--KL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrARLGigYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEEFTVLDTVIMGHEELWKVKAERDRIysLPEMTEDDGMAvaeletefaemdgYTAESRAgelllglgigieqh 149
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEK--LEELLEEFHIT-------------HLRKSKA-------------- 131
|
170 180 190
....*....|....*....|....*....|...
gi 1502692530 150 ngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEP 182
Cdd:cd03218 132 ----SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
336-491 |
1.77e-06 |
|
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: 49.03 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI-------------KWTESaeIGYYAQDhahdfedeCTLF 402
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhDLRSR--ISIIPQD--------PVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 403 --------DWMGQWTQGG--EQLVRGTLGRMLFSNDEILKSvKVISGGE---QG-RMLF--GKLILQKPNVLVMDEPTNH 466
Cdd:cd03244 91 sgtirsnlDPFGEYSDEElwQALERVGLKEFVESLPGGLDT-VVEEGGEnlsVGqRQLLclARALLRKSKILVLDEATAS 169
|
170 180
....*....|....*....|....*..
gi 1502692530 467 LDMESIEALNLAL-ENYPG-TLIFVSH 491
Cdd:cd03244 170 VDPETDALIQKTIrEAFKDcTVLTIAH 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
2.70e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EP----NVRLGKLRQ----------DQ-FAYeefTV 81
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPikydKKSLLEVRKtvgivfqnpdDQlFAP---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 82 LDTVIMGHEELwkvkaerdriyslpemteddGMAVAELETEFAE------MDGYtaesragelllglgigieqHNGPMSE 155
Cdd:PRK13639 97 EEDVAFGPLNL--------------------GLSKEEVEKRVKEalkavgMEGF-------------------ENKPPHH 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 156 VSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRN--SLMIIIS-HD 211
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHD 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-210 |
3.15e-06 |
|
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: 48.64 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKP--LFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPN----VRLGKLR-QDQF 74
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlalADPAWLRrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AYEEFTVLDTVImgheelwkvkaeRDRIYSlpemtEDDGMAVAELEtEFAEMDGYTAESRageLLLGLGIGIEQHNGpmS 154
Cdd:cd03252 81 VLQENVLFNRSI------------RDNIAL-----ADPGMSMERVI-EAAKLAGAHDFIS---ELPEGYDTIVGEQG--A 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNslMIIISH 210
Cdd:cd03252 138 GLSGGQRQRIAIARALIHNPRILIFDEATSALDYesehAIMRNMHDICAGRT--VIIIAH 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
348-468 |
3.58e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 348 VAIIGPNGIGKTTLLRTLVNELTPDAGSIK----WTESaeIGYYA----QDHahdFEDectLFDwmgqwtqgGE------ 413
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDeepsWDEV--LKRFRgtelQDY---FKK---LAN--------GEikvahk 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 414 --------QLVRGTLGRMLFSNDE---------------IL-KSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:COG1245 166 pqyvdlipKVFKGTVRELLEKVDErgkldelaeklglenILdRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
332-506 |
3.59e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 332 TTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESA-------EIGYYAQDHaHDFE 396
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSAAkaelrnqKLGFIYQFH-HLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 DECTLFDWMGQWTQGGEQlvRGTLGRMLFsndEILKSVKV----------ISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:PRK11629 101 DFTALENVAMPLLIGKKK--PAEINSRAL---EMLAAVGLehranhrpseLSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1502692530 467 LDM---ESIEALNLALENYPGT-LIFVSHDREFVSSLaTRIIEL 506
Cdd:PRK11629 176 LDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEM 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-503 |
3.73e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW-------TESAE-----IGY 386
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvriRSPRDaialgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 387 YaqdHAHdFedecTLFD--------WMGQwtqggEQLVRGTLGRmlfsnDEILKSVKVISG-----------------GE 441
Cdd:COG3845 85 V---HQH-F----MLVPnltvaeniVLGL-----EPTKGGRLDR-----KAARARIRELSErygldvdpdakvedlsvGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 442 QGR--MLfgKLILQKPNVLVMDEPTNHLDMESIEAL-----NLALENYpgTLIFVSHD-REfVSSLATRI 503
Cdd:COG3845 147 QQRveIL--KALYRGARILILDEPTAVLTPQEADELfeilrRLAAEGK--SIIFITHKlRE-VMAIADRV 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-230 |
4.11e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.53 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPnvrLGKL-RQDQFAYEEftvlDTVIMGHE 90
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgEP---LAKLnRAQRKAFRR----DIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 91 ELWKVKAERD--RIYSLPeMTEDDGMAVAELETEFAEMdgytaeSRAGELLLGLGIGIEQhngpmsEVSPGWKLRVLLAQ 168
Cdd:PRK10419 98 SISAVNPRKTvrEIIREP-LRHLLSLDKAERLARASEM------LRAVDLDDSVLDKRPP------QLSGGQLQRVCLAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 169 ALFSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
328-506 |
4.23e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 328 GFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTL-----------------VNELTPDAGSIKWTEsaEIGYYAQD 390
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptsgtyrvagqdVATLDADALAQLRRE--HFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 H--------AHDFEDECTlfdWMGQWTQGGEQLVRGTLGRMLFSnDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:PRK10535 95 YhllshltaAQNVEVPAV---YAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1502692530 463 PTNHLDMESIE---ALNLALENYPGTLIFVSHDREfVSSLATRIIEL 506
Cdd:PRK10535 171 PTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEI 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-500 |
5.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 319 AVVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNELTPDAGSIKWTESAEigYYAQD-------- 390
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVE--FFNQNiyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 ----------HAHDFEDECTLFDWMGQ------WTQGGEqlVRGTLGRMLFSND-------EILKSVKVISGGEQGRMLF 447
Cdd:PRK14258 84 nrlrrqvsmvHPKPNLFPMSVYDNVAYgvkivgWRPKLE--IDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 448 GKLILQKPNVLVMDEPTNHLDMES---IEAL--NLALENyPGTLIFVSHDREFVSSLA 500
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIAsmkVESLiqSLRLRS-ELTMVIVSHNLHQVSRLS 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-187 |
5.50e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 48.53 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGKLRQD-------- 72
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-----GRDVTDlppkdrni 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 73 -----QFA-YEEFTVLDTV-----IMGHEelwkvKAERDRiyslpemteddgmAVAELetefAEM---DGYtAESRAgel 138
Cdd:COG3839 78 amvfqSYAlYPHMTVYENIafplkLRKVP-----KAEIDR-------------RVREA----AELlglEDL-LDRKP--- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 139 llglgigieqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:COG3839 132 ---------------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-211 |
5.51e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 20 VSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnvrlgklrqdqfayeefTVLDTVIMGHEELW---KV- 95
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---------------------KVMGREVNAENEKWvrsKVg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 96 ---KAERDRIYSlpeMTEDDGMAVAELETEfaeMDGYTAESRAGELLLGLGIGIEQHNGPMsEVSPGWKLRVLLAQALFS 172
Cdd:PRK13647 83 lvfQDPDDQVFS---STVWDDVAFGPVNMG---LDKDEVERRVEEALKAVRMWDFRDKPPY-HLSYGQKKRVAIAGVLAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1502692530 173 DPEVLLLDEPTNHLD---INTIRWLENVLTQRNSLMIIISHD 211
Cdd:PRK13647 156 DPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
333-504 |
5.79e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 333 TLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWT-------ESAEIGYYAQDHAHDFEDECTLFDwm 405
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQRKAFRRDIQMVFQDSISAVN-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 gqwtqgGEQLVRGTLG---RMLFSND---------EILKSVKV-----------ISGGEQGRMLFGKLILQKPNVLVMDE 462
Cdd:PRK10419 104 ------PRKTVREIIReplRHLLSLDkaerlarasEMLRAVDLddsvldkrppqLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 463 PTNHLD-MESIEALNL--ALENYPGT-LIFVSHDREFVSSLATRII 504
Cdd:PRK10419 178 AVSNLDlVLQAGVIRLlkKLQQQFGTaCLFITHDLRLVERFCQRVM 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
7.27e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG--GDLEPS---------GGQVMLEPNVRLGKL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtitgsivyNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQD------QFAYEEFTVLDTVIMGheelWKVKAERDRiYSLPEMTEdDGMAVAELETEFAEmdgytaesragelllglg 143
Cdd:PRK14239 85 RKEigmvfqQPNPFPMSIYENVVYG----LRLKGIKDK-QVLDEAVE-KSLKGASIWDEVKD------------------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 144 igiEQHNGPMSeVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVL--TQRNSLMIIISH 210
Cdd:PRK14239 141 ---RLHDSALG-LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlgLKDDYTMLLVTR 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-528 |
8.45e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 339 SFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK-----------WTESAEIGYYAQDHAHDF-----EDECTLf 402
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIGMVFQNPDNQFvgatvEDDVAF- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 403 dwmGQWTQG--GEQLVRGTLGRMLFSN--DEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD----MESIEA 474
Cdd:PRK13642 106 ---GMENQGipREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 475 LNLALENYPGTLIFVSHDREFVSSlATRIIELSPSGVIDFSGTYDDYLRSQGVV 528
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
327-377 |
8.74e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 8.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK 377
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL 62
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-468 |
9.11e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 302 RVSPFIRFEQTKKLHRQAVVVERMAKgfdgtTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPD---AGSI-- 376
Cdd:TIGR00955 13 RVAQDGSWKQLVSRLRGCFCRERPRK-----HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 377 ------KWTESAEIGYYAQDHahdfedectLFdwMGQWTqGGEQLV---RGTLGRMLFSN------DEILK--------- 432
Cdd:TIGR00955 88 ngmpidAKEMRAISAYVQQDD---------LF--IPTLT-VREHLMfqaHLRMPRRVTKKekrervDEVLQalglrkcan 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 433 -------SVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD 468
Cdd:TIGR00955 156 trigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-208 |
9.64e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.21 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG------------GDLEPSGGQVMLEPNVRLGKL 69
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielypearvsGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 70 RQDQFAYEE----FTVLDTVIMGHEELWKVKAERDRIYSLPEMTEDdgmavAELETEFAEmdgytaesragelllglgig 145
Cdd:PRK14247 84 VQMVFQIPNpipnLSIFENVALGLKLNRLVKSKKELQERVRWALEK-----AQLWDEVKD-------------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 146 ieQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLMIII 208
Cdd:PRK14247 139 --RLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIV 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-190 |
1.05e-05 |
|
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: 48.37 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKlrqdQFAY-EEFTVLDTVIMGheelw 93
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP----QTSWiMPGTIKDNIIFG----- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 kVKAERDRIYSLpemteddgMAVAELE---TEFAEMDgytaesragelllglgigieqhNGPMSE----VSPGWKLRVLL 166
Cdd:TIGR01271 511 -LSYDEYRYTSV--------IKACQLEediALFPEKD----------------------KTVLGEggitLSGGQRARISL 559
|
170 180
....*....|....*....|....
gi 1502692530 167 AQALFSDPEVLLLDEPTNHLDINT 190
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
348-492 |
1.13e-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: 46.98 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 348 VAIIGPNGIGKTTLLRTLVNELTPDAGSI----KWTESaeIGYYAQDHAHDF-----EDECTLFdwmgQWTQGGEQL--- 415
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEI--LDEFRGSELQNYftkllEGDVKVI----VKPQYVDLIpka 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 416 VRGTLGRMLFSNDEILKSVKVI----------------SGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMEsiEALNLA- 478
Cdd:cd03236 103 VKGKVGELLKKKDERGKLDELVdqlelrhvldrnidqlSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNAAr 180
|
170
....*....|....*...
gi 1502692530 479 ----LENYPGTLIFVSHD 492
Cdd:cd03236 181 lireLAEDDNYVLVVEHD 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
437-520 |
1.15e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESI-EALNL--ALENYPGTLIFVSHDREFVSSLATRIIELSpSGVID 513
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRImqQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIE 231
|
....*..
gi 1502692530 514 FSGTYDD 520
Cdd:PRK10619 232 EEGAPEQ 238
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-510 |
1.36e-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: 46.06 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 349 AIIGPNGIGKTTLLRTLVNELTPD--------AGSIKWTESAEIGYYAQDHahdFEDectlfdwmgqwTQGGEQLVRGTL 420
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGElppnskggAHDPKLIREGEVRAQVKLA---FEN-----------ANGKKYTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 421 gRML----F-----SNDEILKSVKVISGGEqgRMLFGkLILQ---------KPNVLVMDEPTNHLDMESIE-ALNLALEN 481
Cdd:cd03240 92 -AILenviFchqgeSNWPLLDMRGRCSGGE--KVLAS-LIIRlalaetfgsNCGILALDEPTTNLDEENIEeSLAEIIEE 167
|
170 180 190
....*....|....*....|....*....|...
gi 1502692530 482 YPGTLIF----VSHDREFVsSLATRIIELSPSG 510
Cdd:cd03240 168 RKSQKNFqlivITHDEELV-DAADHIYRVEKDG 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-230 |
1.38e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPnvrlgklrqdqfayeeftvLDTVIMGHEELWKVKA 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 98 ER-----DRIYSLPEMTEDDGMAVAeletefAEMDGYTAESRAGELLLGLGIGIEQH--NGPMSEVSPGWKLRVLLAQAL 170
Cdd:PRK10070 106 KKiamvfQSFALMPHMTVLDNTAFG------MELAGINAEERREKALDALRQVGLENyaHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 171 FSDPEVLLLDEPTNHLD--INTIRWLENVLTQ--RNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10070 180 AINPDILLMDEAFSALDplIRTEMQDELVKLQakHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-376 |
1.53e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.57 E-value: 1.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTL--VNELTPDA---GSI 376
Cdd:COG1117 28 KDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGArveGEI 73
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
337-504 |
1.53e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 337 DFSFTVEA-----SERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtesaeigyyaqdhahdfedectlfdwmgqwtqg 411
Cdd:cd03222 12 VFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW--------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 412 geqlvrgtlgrmlfsnDEILKSVK----VISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDME----SIEALNLALENYP 483
Cdd:cd03222 59 ----------------DGITPVYKpqyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK 122
|
170 180
....*....|....*....|.
gi 1502692530 484 GTLIFVSHDREFVSSLATRII 504
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIH 143
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-226 |
1.62e-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: 45.22 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG-------GDLE-PSGGQVML---EPNVRLGKLRqDQFAYeeftvl 82
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsGRIGmPEGEDLLFlpqRPYLPLGTLR-EQLIY------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 dtvimgheeLWkvkaerdriyslpemteddgmavaeletefaemdgytaesragelllglgigieqhngpMSEVSPGWKL 162
Cdd:cd03223 87 ---------PW-----------------------------------------------------------DDVLSGGEQQ 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRnsLMIIIS--HdRHFLNSVCTHMADLD 226
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISvgH-RPSLWKFHDRVLDLD 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
336-525 |
2.03e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.31 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTL--VNELTPD---AGSIKWTES-------------AEIGY-YAQDHAHDF- 395
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlrKEIGMvFQQPNPFPMs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 396 --------------EDECTLfdwmgqwtqggEQLVRGTL-GRMLFS--NDEILKSVKVISGGEQGRMLFGKLILQKPNVL 458
Cdd:PRK14239 102 iyenvvyglrlkgiKDKQVL-----------DEAVEKSLkGASIWDevKDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 459 VMDEPTNHLDMES---IEALNLALEN-YpgTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYDDYLRSQ 525
Cdd:PRK14239 171 LLDEPTSALDPISagkIEETLLGLKDdY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-212 |
2.09e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGnRYGLI-GANGCGKSTFMKILGGDLEPSGGQVMLEpnvrlGK---------LRQdQFA 75
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAG-EFKLItGPSGCGKSTLLKIVASLISPTSGTLLFE-----GEdistlkpeiYRQ-QVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 Y-----EEF--TVLDTVIMGheelWKVKAERdriyslPEMTE-DDGMAVAELETEFAEMdgytaesragelllglgigie 147
Cdd:PRK10247 85 YcaqtpTLFgdTVYDNLIFP----WQIRNQQ------PDPAIfLDDLERFALPDTILTK--------------------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 148 qhngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD------INTIrwLENVLTQRNSLMIIISHDR 212
Cdd:PRK10247 134 ----NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEI--IHRYVREQNIAVLWVTHDK 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
315-479 |
2.16e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 315 LHRQAVVVERMAKGF-DGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWTESAEIG 385
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 386 YYAQDHAHDF------EDECTL-----FDWMGQWTQGGEQLVRGTLGRMLFSnDEILKSVKVISGGEQGRMLFGKLILQK 454
Cdd:PRK15056 82 YVPQSEEVDWsfpvlvEDVVMMgryghMGWLRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180
....*....|....*....|....*
gi 1502692530 455 PNVLVMDEPTNHLDMESiEALNLAL 479
Cdd:PRK15056 161 GQVILLDEPFTGVDVKT-EARIISL 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
320-376 |
2.27e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 45.84 E-value: 2.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI 376
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV 58
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-211 |
2.40e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGP---KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML------EPNV-----RL 66
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdgdlltEENVwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 67 GKLRQ---DQFAYEefTVLDTVIMGHEelwkvkaerDRIYSLPEMTEDDGMAVaeletEFAEMDGYTAESRAgelllglg 143
Cdd:PRK13650 84 GMVFQnpdNQFVGA--TVEDDVAFGLE---------NKGIPHEEMKERVNEAL-----ELVGMQDFKEREPA-------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 144 igieqhngpmsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISHD 211
Cdd:PRK13650 140 -----------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
336-376 |
2.52e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 46.61 E-value: 2.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRtLVNEL-TPDAGSI 376
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIR-CINLLeRPTSGSV 62
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-506 |
2.63e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 349 AIIGPNGIGKTTLLRTLVNELTPDAGSIKW---------------TESAEIGYYAQDHahdfedecTLFDWMGqwtqgge 413
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaekgiclpPEKRRIGYVFQDA--------RLFPHYK------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 414 qlVRGTL--GRMLFSNDEILKSVKVI-------------SGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM----ESIEA 474
Cdd:PRK11144 93 --VRGNLryGMAKSMVAQFDKIVALLgieplldrypgslSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPY 170
|
170 180 190
....*....|....*....|....*....|....
gi 1502692530 475 L-NLALE-NYPgtLIFVSHDREFVSSLATRIIEL 506
Cdd:PRK11144 171 LeRLAREiNIP--ILYVSHSLDEILRLADRVVVL 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
336-480 |
2.80e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI----KWTESAEIGYYAQDHAHDFEDECTLFD---WMGQW 408
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddHPLHFGDYSYRSQRIRMIFQDPSTSLNprqRISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 409 ------------TQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGK-LILQkPNVLVMDEPTNHLDME-SIEA 474
Cdd:PRK15112 110 ldfplrlntdlePEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARaLILR-PKVIIADEALASLDMSmRSQL 188
|
....*.
gi 1502692530 475 LNLALE 480
Cdd:PRK15112 189 INLMLE 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-491 |
2.84e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 2.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 437 ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMES---IEALNLALENyPGTLIFVSH 491
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-200 |
2.88e-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: 46.00 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQF--GPKPLFENVSVKFGAGNRYGLIGANGCGKST----FMKILG--GDLEPSG---------------GQV 58
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNteGDIQIDGvswnsvplqkwrkafGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 59 MLEPNVRLGKLRQDQFAYEEFTvldtvimgHEELWKVkAERDRIYSLPEMTEDdgmavaelETEFAEMDGYTAesragel 138
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWS--------DEEIWKV-AEEVGLKSVIEQFPG--------QLDFVLVDGGCV------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1502692530 139 llglgigieqhngpmseVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ 200
Cdd:cd03289 139 -----------------LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-190 |
3.03e-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: 46.00 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 15 PLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRLGKlrqdQFAY-EEFTVLDTVIMGheelw 93
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS----QFSWiMPGTIKENIIFG----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 kVKAERDRIYSLPEMTEddgmaVAELETEFAEMDgytaesragelllglgigieqhNGPMSE----VSPGWKLRVLLAQA 169
Cdd:cd03291 122 -VSYDEYRYKSVVKACQ-----LEEDITKFPEKD----------------------NTVLGEggitLSGGQRARISLARA 173
|
170 180
....*....|....*....|.
gi 1502692530 170 LFSDPEVLLLDEPTNHLDINT 190
Cdd:cd03291 174 VYKDADLYLLDSPFGYLDVFT 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
322-463 |
3.26e-05 |
|
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: 45.23 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIkWTESAE-------------IGYYA 388
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI-LLDGQDitklpmhkrarlgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 389 QdhahdfedECTLFDWM-----------------GQWTQGGEQLVRgtlgrmLFSNDEILKSVKV-ISGGEQGRMLFGKL 450
Cdd:cd03218 82 Q--------EASIFRKLtveenilavleirglskKEREEKLEELLE------EFHITHLRKSKASsLSGGERRRVEIARA 147
|
170
....*....|...
gi 1502692530 451 ILQKPNVLVMDEP 463
Cdd:cd03218 148 LATNPKFLLLDEP 160
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-519 |
3.93e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 339 SFTVEASERVAIIGPNGIGKTTLLR------------TLVNELTPDAGSIKWTE----SAEIGYYAQDHAHDFEDECTLF 402
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEvkrlRKEIGLVFQFPEYQLFQETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 403 DW------MGQWTQGGEQLVRGTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMESIEA-L 475
Cdd:PRK13645 111 DIafgpvnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDfI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1502692530 476 NLAL---ENYPGTLIFVSHDREFVSSLATRIIELSPSGVIDFSGTYD 519
Cdd:PRK13645 191 NLFErlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
331-469 |
3.95e-05 |
|
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: 46.83 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 331 GTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKwtESAEIGYYAQdhahdfedectlFDWmgqwtq 410
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQ------------TSW------ 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 411 ggeqLVRGTL-GRMLF--SNDE-----ILKSVKV---------------------ISGGEQGRMLFGKLILQKPNVLVMD 461
Cdd:TIGR01271 498 ----IMPGTIkDNIIFglSYDEyrytsVIKACQLeedialfpekdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
....*...
gi 1502692530 462 EPTNHLDM 469
Cdd:TIGR01271 574 SPFTHLDV 581
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-500 |
4.15e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.42 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 322 VERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLvNELTPDAGSiKWTESAEIGYYAQD----HAHDFED 397
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEIYDS-KIKVDGKVLYFGKDifqiDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 398 EC-------------TLFDWMG------------QWTQGGEQLVRgTLGRMLFSNDEILKSVKVISGGEQGRMLFGKLIL 452
Cdd:PRK14246 91 EVgmvfqqpnpfphlSIYDNIAyplkshgikekrEIKKIVEECLR-KVGLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 453 QKPNVLVMDEPTNHLDM---ESIEALNLALENyPGTLIFVSHDREFVSSLA 500
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVA 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
155-211 |
4.28e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 4.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRWLENVLTQR-NSLMIIISHD 211
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREfNTAIIMITHD 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
4.55e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 44.75 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLfeNVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV--------MLEPNVR-LGKLRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltALPPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQ--FAYeeFTVLDTVIMG-HEELWKVKAERDRIyslpemteddgMAVAElETEFAEMDGYTaesragelllglgigieq 148
Cdd:COG3840 79 ENnlFPH--LTVAQNIGLGlRPGLKLTAEQRAQV-----------EQALE-RVGLAGLLDRL------------------ 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1502692530 149 hngPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDIN----TIRWLENVLTQRNSLMIIISHD 211
Cdd:COG3840 127 ---P-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
4.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.54 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVmlepnvrlgklrqdqfayeefTVLDTVIMGHEELWKVKAE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV---------------------TVDDITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 99 RDRI---YSLPE--MTEDDgmavAELETEFA----EMDGYTAESRAGELLLGLGIGIEQHNGPMSEVSPGWKLRVLLAQA 169
Cdd:PRK13646 84 RKRIgmvFQFPEsqLFEDT----VEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1502692530 170 LFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHD 211
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHD 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
155-376 |
4.95e-05 |
|
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: 45.83 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDInTIRW----LENVLTQRNSL-MIIISHDrhfLNSVcTHMAD----L 225
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqildLLKDLQRELGMaLLLITHD---LGVV-RRFADrvavM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 226 DYGEL-------RLF--PGnyDEYmtvaTQsreQLLAdnakkkaqiSElqsfvSRFSANASKAKQATsrakqidkiqLAE 296
Cdd:COG4172 231 RQGEIveqgptaELFaaPQ--HPY----TR---KLLA---------AE-----PRGDPRPVPPDAPP----------LLE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 297 VKpSSRVSPFIR---FEQTKKLHRqAVvvermakgfdgttlfKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNeLTPDA 373
Cdd:COG4172 278 AR-DLKVWFPIKrglFRRTVGHVK-AV---------------DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSE 339
|
...
gi 1502692530 374 GSI 376
Cdd:COG4172 340 GEI 342
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-182 |
5.09e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPN----------VRLGKLR 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpghqiARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 --QDQFAYEEFTVLDTVIMG-HEE--------LWKVKAERDRiyslpemtEDDGMAVAE--LE----TEFAemdgytaes 133
Cdd:PRK11300 85 tfQHVRLFREMTVIENLLVAqHQQlktglfsgLLKTPAFRRA--------ESEALDRAAtwLErvglLEHA--------- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 134 ragelllglgigieqhNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEP 182
Cdd:PRK11300 148 ----------------NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
327-503 |
5.83e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWtESAEigyYAQDHAHDFED--------E 398
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL-DGEP---VRFRSPRDAQAagiaiihqE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 399 CTLFD--------WMGQwtqggEQLVRGTL--GRMLFSNDEILKSVKV----------ISGGEQGRMLFGKLILQKPNVL 458
Cdd:COG1129 88 LNLVPnlsvaeniFLGR-----EPRRGGLIdwRAMRRRARELLARLGLdidpdtpvgdLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 459 VMDEPTNHLDMESIEAL-----NLALEnypG-TLIFVSHDREFVSSLATRI 503
Cdd:COG1129 163 ILDEPTASLTEREVERLfriirRLKAQ---GvAIIYISHRLDEVFEIADRV 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
336-377 |
6.62e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.60 E-value: 6.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK 377
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK 67
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
437-502 |
7.08e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.38 E-value: 7.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDM---ESIEALNLAL-ENYPGTLIFVSHDrefvSSLATR 502
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRqtgDKIADLLFSLnREHGTTLILVTHD----LQLAAR 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
7.29e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQF------GPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPnvrlgklrqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 ayeeftvLDTVIMGHeeLWKVKAERDRIYSLPemteDDGMAVAELETEFA---EMDGYTAE---SRAGELLLGLGIGIEQ 148
Cdd:PRK13633 72 -------LDTSDEEN--LWDIRNKAGMVFQNP----DNQIVATIVEEDVAfgpENLGIPPEeirERVDESLKKVGMYEYR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 149 HNGPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRWLENvltQRNSLMIIISH 210
Cdd:PRK13633 139 RHAP-HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIKELNK---KYGITIILITH 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-217 |
7.31e-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: 43.47 E-value: 7.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 150 NGPMSEVSPGWKLRVLLAQALFSDPE--VLLLDEPTNHLDINTIRWLENV---LTQRNSLMIIISHDRHFLNS 217
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLSS 154
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-504 |
7.81e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 320 VVVERMAKGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAeigYYAQDHAHDFE--- 396
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLAAQlgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 397 ----------DECT-------------------LFDWMGQWTQGGEQLVRGTLGRMLfsnDEilkSVKVISGGEQGRMLF 447
Cdd:PRK09700 83 giiyqelsviDELTvlenlyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDL---DE---KVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 448 GKLILQKPNVLVMDEPTNHLDMESIEALNL---ALENYPGTLIFVSH---------DREFV----SSLATRII 504
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLimnQLRKEGTAIVYISHklaeirricDRYTVmkdgSSVCSGMV 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-228 |
9.31e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 44.23 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG-------GDLEPSGGQVML--EPNVRLG-KLRQ 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLNIAGNHFDFskTPSDKAIrELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DqfayeeftvldtVIMGHEE--LWkvkaerdriyslPEMTEDDGMAvaELETEFAEMDGYTAESRAGELLLGLGIGIEQH 149
Cdd:PRK11124 83 N------------VGMVFQQynLW------------PHLTVQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 150 NGPMsEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD-------INTIRWLENV-LTQrnslmIIISHDRHFLNSVCTH 221
Cdd:PRK11124 137 RFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETgITQ-----VIVTHEVEVARKTASR 210
|
....*..
gi 1502692530 222 MADLDYG 228
Cdd:PRK11124 211 VVYMENG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
336-492 |
9.68e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 336 KDFSFTVEASERVAIIGPNGIGKTTLLRTL--VNELTPDAGSikwteSAEIGYYAQDHAHDFEDECTLFDWMGQWTQGG- 412
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFRV-----EGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 413 -----------------------EQLVRGTLGRMLFSN---DEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPTNH 466
Cdd:PRK14243 102 pfpksiydniaygaringykgdmDELVERSLRQAALWDevkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|
gi 1502692530 467 LDMES---IEALNLAL-ENYpgTLIFVSHD 492
Cdd:PRK14243 182 LDPIStlrIEELMHELkEQY--TIIIVTHN 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
9.69e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGdLEPSG-GQVMLEPNVR-----------LGKLRqDQFAY----E 77
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARPAGARvlflpqrpylpLGTLR-EALLYpataE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 78 EFT------VLDTVIMGH-------EELWkvkaerDRIYSLPEmteddgmavaeletefaemdgytaesragelllglgi 144
Cdd:COG4178 454 AFSdaelreALEAVGLGHlaerldeEADW------DQVLSLGE------------------------------------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 145 gieqhngpmsevspgwKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQR--NSLMIIISHdRHFLNSVCTHM 222
Cdd:COG4178 491 ----------------QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRV 553
|
....
gi 1502692530 223 ADLD 226
Cdd:COG4178 554 LELT 557
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
1.11e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.97 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE----PNVRLGKLRQD-----QFAYEEF---TVLDTVI 86
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaiTDDNFEKLRKHigivfQNPDNQFvgsIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 87 MGHEELWKVKAERDRIysLPEMTEDDGMavaeleTEFAEMDgytaesragelllglgigieqhngPMSeVSPGWKLRVLL 166
Cdd:PRK13648 107 FGLENHAVPYDEMHRR--VSEALKQVDM------LERADYE------------------------PNA-LSGGQKQRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 167 AQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISHD 211
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDpdarQNLLDLVRKVKSEHNITIISITHD 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-208 |
1.23e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 43.87 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGG--DLEPSG---GQVMLE------PNVRLGKLR 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLDgediydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 71 QD-----Q----FAyeeFTVLDTVIMGHeelwKVKAERDRiyslpemteddgmavaeletefAEMDGYTAES--RAgell 139
Cdd:COG1117 92 RRvgmvfQkpnpFP---KSIYDNVAYGL----RLHGIKSK----------------------SELDEIVEESlrKA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 140 lglgigieqhnGPMSEV-----SPGWKL------RVLLAQALFSDPEVLLLDEPTNHLD-INTIRwLENVLTQ-RNSLMI 206
Cdd:COG1117 139 -----------ALWDEVkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElKKDYTI 206
|
..
gi 1502692530 207 II 208
Cdd:COG1117 207 VI 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
157-218 |
1.32e-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: 43.28 E-value: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ---RNSLMIIISHDRHFLNSV 218
Cdd:cd03217 106 SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlreEGKSVLIITHYQRLLDYI 170
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
1.38e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 11 FGPKPLFeNVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNVRLGKLRQD-----QFA-- 75
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstsKNKDIKQIRKKvglvfQFPes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 --YEEfTVLDTVIMGHEELWKVKAERDRIyslpemtEDDGMAVAELETEFAEMDGYtaesragelllglgigieqhngpm 153
Cdd:PRK13649 97 qlFEE-TVLKDVAFGPQNFGVSQEEAEAL-------AREKLALVGISESLFEKNPF------------------------ 144
|
170 180 190
....*....|....*....|....*....|....
gi 1502692530 154 sEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK13649 145 -ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-209 |
1.52e-04 |
|
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: 43.02 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGqvmlePNvrlGKLRQDQFAYEEFtvldtvimgheelw 93
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-----VE---GDIHYNGIPYKEF-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 94 KVKAERDRIYS------LPEMTeddgmaVAELeTEFAemdgytaesragelllglgiGIEQHNGPMSEVSPGWKLRVLLA 167
Cdd:cd03233 78 AEKYPGEIIYVseedvhFPTLT------VRET-LDFA--------------------LRCKGNEFVRGISGGERKRVSIA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1502692530 168 QALFSDPEVLLLDEPTNHLD-------INTIRWLENVLtqRNSLMIIIS 209
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDsstaleiLKCIRTMADVL--KTTTFVSLY 177
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-288 |
1.72e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVRL---GKLRQDQFAYEEFTVLDTVIMGheelwkv 95
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALiaiSSGLNGQLTGIENIELKGLMMG------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 96 kaerdriyslpeMTEDDGMAVAELETEFAEMDGYTaesragelllglgigieqhNGPMSEVSPGWKLRVLLAQALFSDPE 175
Cdd:PRK13545 115 ------------LTKEKIKEIIPEIIEFADIGKFI-------------------YQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 176 VLLLDEPTNHLDIN-TIRWLE--NVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGELRLF------PGNYD----EYMT 242
Cdd:PRK13545 164 ILVIDEALSVGDQTfTKKCLDkmNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDeflkKYNQ 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 243 VATQSREQLladnakKKAQISE-----LQSFVSRFSANASKAKQATSRAKQ 288
Cdd:PRK13545 244 MSVEERKDF------REEQISQfqhglLQEDQTGRERKRKKGKKTSRKFKK 288
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-61 |
1.80e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE 61
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID 73
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-61 |
2.15e-04 |
|
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: 43.17 E-value: 2.15e-04
10 20 30
....*....|....*....|....*....|.
gi 1502692530 31 GLIGANGCGKSTFMKILGGDLEPSGGQVMLE 61
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIE 59
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-183 |
2.31e-04 |
|
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: 42.66 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQ---------------FAyeEFTVLD 83
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRiarlgigyvpegrriFP--SLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 84 TVIMG---HEELWKVKAERDRIYSL-PEMteddgmavaeletefAEMdgytAESRAgelllglgigieqhnGPMSEvspG 159
Cdd:COG0410 98 NLLLGayaRRDRAEVRADLERVYELfPRL---------------KER----RRQRA---------------GTLSG---G 140
|
170 180
....*....|....*....|....
gi 1502692530 160 WKLRVLLAQALFSDPEVLLLDEPT 183
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-60 |
2.48e-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: 43.63 E-value: 2.48e-04
10 20
....*....|....*....|....*....
gi 1502692530 32 LIGANGCGKSTFMKILGGDLEPSGGQVML 60
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-211 |
2.73e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV--------------MLEPNVRL 66
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipamsrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 67 GKLRQDQFAYEEFTVLDTVIMGHEELWKVKAERDRIYSLPEMTEDDGMAVAELETefaemdgytaesragelllglgigi 146
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMP------------------------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 147 eqhngpmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQRNSLM----IIISHD 211
Cdd:PRK11831 142 -------SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
437-516 |
2.99e-04 |
|
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: 41.92 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 ISGGEQGRMLFGKLILQ--KPNVLVMDEPTNHLDMESIEALNLALE---NYPGTLIFVSHDREFVSSlATRIIELSP--- 508
Cdd:cd03238 88 LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSS-ADWIIDFGPgsg 166
|
90
....*....|
gi 1502692530 509 --SGVIDFSG 516
Cdd:cd03238 167 ksGGKVVFSG 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
339-377 |
3.04e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.67 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1502692530 339 SFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIK 377
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL 63
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-187 |
3.40e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.01 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQ------F- 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-GQDITHVPAENrhvntvFq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 75 AYEEF---TVLDTVIMGHeELWKV-KAE-RDRIYslpemtedDGMAVAELEtEFAemdgytaesragelllglgigieQH 149
Cdd:PRK09452 94 SYALFphmTVFENVAFGL-RMQKTpAAEiTPRVM--------EALRMVQLE-EFA-----------------------QR 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 1502692530 150 NgPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PRK09452 141 K-P-HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-491 |
3.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.52 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 349 AIIGPNGIGKTTLLRTL--VNELTPDA---GSIK------WTESA-------EIGYYAQ-----DHAHDFEDECTLFDWM 405
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRlfgrniYSPDVdpievrrEVGMVFQypnpfPHLTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 406 GQWTQGGE--QLVRGTLGRMLFSnDEILKSVK----VISGGEQGRMLFGKLILQKPNVLVMDEPTNHLD---MESIEALN 476
Cdd:PRK14267 114 GLVKSKKEldERVEWALKKAALW-DEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELL 192
|
170
....*....|....*
gi 1502692530 477 LALENyPGTLIFVSH 491
Cdd:PRK14267 193 FELKK-EYTIVLVTH 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
4.63e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 2 ISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILG------------GDLEPSGGQVM------LEPN 63
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneearveGEVRLFGRNIYspdvdpIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 64 VRLGKLRQDQFAYEEFTVLDTVIMG--HEELWKVKAERDRIYSLpemteddGMAVAELETEFAEmdgytaesragelllg 141
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGvkLNGLVKSKKELDERVEW-------ALKKAALWDEVKD---------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 142 lgigieQHNGPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHDRHFLNSVC 219
Cdd:PRK14267 142 ------RLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFElkKEYTIVLVTHSPAQAARVS 215
|
250
....*....|.
gi 1502692530 220 THMADLDYGEL 230
Cdd:PRK14267 216 DYVAFLYLGKL 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
152-233 |
4.71e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.55 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 152 PMSeVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIR----WLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDY 227
Cdd:PRK11144 126 PGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
....*.
gi 1502692530 228 GELRLF 233
Cdd:PRK11144 205 GKVKAF 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-187 |
4.83e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 5 ANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSG--GQVMLEPNV-------RLGKLRQDQFA 75
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKptkqilkRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 76 YEEFTVLDTVIMGheelwkvkaerdRIYSLPE-MTEDDGMAVAEleTEFAEMDGYTAESRAGElllglgigieqhNGPMS 154
Cdd:PLN03211 152 YPHLTVRETLVFC------------SLLRLPKsLTKQEKILVAE--SVISELGLTKCENTIIG------------NSFIR 205
|
170 180 190
....*....|....*....|....*....|...
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:PLN03211 206 GISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
152-209 |
4.85e-04 |
|
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: 42.89 E-value: 4.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 152 PMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRWLENVLTQRNSLMIIIS 209
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVS 460
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-210 |
4.90e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.33 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVML--EPnvrLGKLRqDQFAYee 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqgEP---IRRQR-DEYHQ-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 79 ftvlDTVIMGHeeLWKVKA-----ERDRIY-SLPEMTEDDGMAVAeLET----EFAEMdgytaesragelllglgigieq 148
Cdd:PRK13538 75 ----DLLYLGH--QPGIKTeltalENLRFYqRLHGPGDDEALWEA-LAQvglaGFEDV---------------------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 149 hngPMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVL---TQRNSLMIIISH 210
Cdd:PRK13538 126 ---PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhAEQGGMVILTTH 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
5.80e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.76 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKfgAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMlepnvRLGKlrqdqfayeeftVLDTVIMGHEELWK---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-----FDGK------------PIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 95 VKAERDRIYSLPEMTEDDGMAVAELETEFAEMdgytaESRAGELLLGLGIGIEQHNgPMSEVSPGWKLRVLLAQALFSDP 174
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIEHLKDK-PTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 175 EVLLLDEPTNHLD---INTIRWLENVLTQRNSLMIII-SHDRHFLNSVCTHMADLDYGELrLFPGNYDE 239
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLYCDNVFVMKEGRV-ILQGNPKE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
307-513 |
5.88e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 307 IRFEQTKKLHRQAVVVERMAkgfdgttlFKDFSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKWTE------ 380
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA--------IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 381 ---------SAEIGYYAQ-DHAHDFEDECTLFDWMGQWTQGGE-QLVRGTLGRML----FSNDEILKSVKVISGGEQGRM 445
Cdd:PRK13646 75 tkdkyirpvRKRIGMVFQfPESQLFEDTVEREIIFGPKNFKMNlDEVKNYAHRLLmdlgFSRDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 446 LFGKLILQKPNVLVMDEPTNHLD-------MESIEALNLAlENypGTLIFVSHDREFVSSLATRIIELSPSGVID 513
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDpqskrqvMRLLKSLQTD-EN--KTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-234 |
6.03e-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: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 27 GNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMlepnvrlgklrqdqfayeeftvldtVIMGHEELWKVKAERDRIYSLP 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------YIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 107 EMTEDDGMAvaeletefaemdgytaesragelllglgigieqhngpmsevspgwKLRVLLAQALFSDPEVLLLDEPTNHL 186
Cdd:smart00382 57 KKASGSGEL---------------------------------------------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1502692530 187 DINTIRWLENVLTQRNSLMIIISHDRHFlnsVCTHMADLDYGELRLFP 234
Cdd:smart00382 92 DAEQEALLLLLEELRLLLLLKSEKNLTV---ILTTNDEKDLGPALLRR 136
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-187 |
6.50e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLE--PSGGQVmlepnvrlgKLRQDQFaYEEFTVLDTVimghee 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV---------DVPDNQF-GREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 92 lwkvkaerDRIYSLPEMTE---DDGMAVAELetefaemdgYTAesragelllglgigieqhngPMSEVSPGWKLRVLLAQ 168
Cdd:COG2401 107 --------GRKGDFKDAVEllnAVGLSDAVL---------WLR--------------------RFKELSTGQKFRFRLAL 149
|
170
....*....|....*....
gi 1502692530 169 ALFSDPEVLLLDEPTNHLD 187
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLD 168
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
335-402 |
7.32e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 7.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1502692530 335 FKDFSFTVEASERV-AIIGPNGIGKTTLLRTLVNELTPDAGSIKWTESAEIgyyaQDHAHDFEDECTLF 402
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKL----LIRNGEFGDSAKLI 78
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-227 |
8.46e-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: 41.20 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 31 GLIGANGCGKSTFMKILGGDLEPSGGQVMLEPNVR------LGKLRQDQFAYEEFTVLDTVIMGH-------------EE 91
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeildefRGSELQNYFTKLLEGDVKVIVKPQyvdlipkavkgkvGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 92 LWKVKAERDRIYSLPEMTEDDGMavaeLETEfaemdgytaesragelllglgigieqhngpMSEVSPGWKLRVLLAQALF 171
Cdd:cd03236 110 LLKKKDERGKLDELVDQLELRHV----LDRN------------------------------IDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 172 SDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSlMIIISHDrhflnsvcthMADLDY 227
Cdd:cd03236 156 RDADFYFFDEPSSYLDIkqrlNAARLIRELAEDDNY-VLVVEHD----------LAVLDY 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-49 |
9.18e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 9.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1502692530 6 NITMQF-GPKPLfENVSVKFGAGNRYGLIGANGCGKSTFMKILGG 49
Cdd:NF040905 6 GITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-187 |
9.47e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 14 KPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPS---GGQVML--------EPNVRLGKLRQDQFAYEEFTVL 82
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLngmpidakEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 83 DTVI-MGHEELWKVKAERDRIYSLPEMTEDDGMAVAeletefaemdgytAESRagelllglgigiEQHNGPMSEVSPGWK 161
Cdd:TIGR00955 118 EHLMfQAHLRMPRRVTKKEKRERVDEVLQALGLRKC-------------ANTR------------IGVPGRVKGLSGGER 172
|
170 180
....*....|....*....|....*.
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPTNHLD 187
Cdd:TIGR00955 173 KRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-464 |
1.10e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 40.63 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 339 SFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSI--------KWtESAEIGYYAQDHAHD---------FEDECTL 401
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditDW-QTAKIMREAVAIVPEgrrvfsrmtVEENLAM 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1502692530 402 FDWMGQWTQGGEQLVR--GTLGRMLfsnDEILKSVKVISGGEQGRMLFGKLILQKPNVLVMDEPT 464
Cdd:PRK11614 104 GGFFAERDQFQERIKWvyELFPRLH---ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-211 |
1.16e-03 |
|
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: 41.59 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 19 NVSVKFGAGNRYGLIGANGCGKSTFMK-ILGgdLEPSGGQVMLEpNVRLGKLRQDQFayeeftvldtvimgheelwkvKA 97
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLaLLR--LIPSEGEIRFD-GQDLDGLSRRAL---------------------RP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 98 ERDRI-------Y-SL-PEMTEddGMAVAE-LETEFAEMDGYTAESRAGELllglgigieqhngpMSEV----------- 156
Cdd:COG4172 360 LRRRMqvvfqdpFgSLsPRMTV--GQIIAEgLRVHGPGLSAAERRARVAEA--------------LEEVgldpaarhryp 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 157 ---SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDInTIRW----LENVLTQRNSL-MIIISHD 211
Cdd:COG4172 424 hefSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVQAqildLLRDLQREHGLaYLFISHD 485
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
323-492 |
1.47e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 40.72 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 323 ERMAKGFDGTtlfkdfSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKwtesaeigYYAQDHA-HDFEDECTL 401
Cdd:PRK11308 25 ERLVKALDGV------SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY--------YQGQDLLkADPEAQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 402 -------FdwmgQWTQGG---EQLVRGTLGRMLFSNDEILKS----------VKV-------------ISGGEQGRMLFG 448
Cdd:PRK11308 91 rqkiqivF----QNPYGSlnpRKKVGQILEEPLLINTSLSAAerrekalammAKVglrpehydryphmFSGGQRQRIAIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1502692530 449 K-LILQkPNVLVMDEPTNHLDMeSIEA--LNLAL---ENYPGTLIFVSHD 492
Cdd:PRK11308 167 RaLMLD-PDVVVADEPVSALDV-SVQAqvLNLMMdlqQELGLSYVFISHD 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
157-224 |
1.83e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 40.72 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDInTIRwlENVLtqrNSLM----------IIISHDRhflnSVCTHMAD 224
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQ--AQVL---NLMMdlqqelglsyVFISHDL----SVVEHIAD 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
437-524 |
1.86e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 437 ISGGEQGRMLFGKLILQKPNVLVMDEPTNHLDMeSIEA----LNLAL---ENYpgTLIFVSHDREFVSSLATRIIELSPS 509
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqiieLLLELqqkENM--ALVLITHDLALVAEAAHKIIVMYAG 230
|
90
....*....|....*
gi 1502692530 510 GVIDfSGTYDDYLRS 524
Cdd:PRK11022 231 QVVE-TGKAHDIFRA 244
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
155-253 |
1.90e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT----IRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGEl 230
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ- 236
|
90 100
....*....|....*....|...
gi 1502692530 231 rlfpgnydeymTVATQSREQLLA 253
Cdd:PRK15093 237 -----------TVETAPSKELVT 248
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
1.90e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 39.95 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFENVSVKfgAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE--------PNVR-LGKLRQ 71
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 72 DQFAYEEFTVLDTVIMG-HEELWKVKAERDRIYSLPEMteddgMAVAELETEFaemdgytaesragelllglgigieqhn 150
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlNPGLKLNAAQREKLHAIARQ-----MGIEDLLARL--------------------------- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1502692530 151 gPmSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLD----INTIRWLENVLTQRNSLMIIISH 210
Cdd:PRK10771 127 -P-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-58 |
2.00e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1502692530 18 ENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV 58
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-58 |
2.19e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.91 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 6 NITMQFGPKPLFENVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQV 58
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
155-211 |
3.02e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 3.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSLMIIISHD 211
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHD 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-90 |
3.08e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 1 MISTANITMQFGPKPLFeNVSVKFGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLEpNVRLGKLRQDQFAY---- 76
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-NCNINNIAKPYCTYighn 78
|
90
....*....|....*...
gi 1502692530 77 ----EEFTVLDTVIMGHE 90
Cdd:PRK13541 79 lglkLEMTVFENLKFWSE 96
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
155-230 |
3.57e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.30 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 155 EVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDI----NTIRWLENVLTQRNSLMIIISHDRHFLNSVCTHMADLDYGEL 230
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
157-242 |
3.58e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.19 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 157 SPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLTQ--RNSLMIIISHDRHFLNSVcTHMADLDYGELRLfP 234
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE-Q 554
|
....*...
gi 1502692530 235 GNYDEYMT 242
Cdd:PRK11160 555 GTHQELLA 562
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-61 |
4.04e-03 |
|
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: 38.32 E-value: 4.04e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1502692530 24 FGAGNRYGLIGANGCGKSTFMKILGGDLEPSGGQVMLE 61
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD 59
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
432-524 |
4.26e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 432 KSVKVISGGEQGRMLFGK----------LILQKPNVLVMDEPTNHLdMESIEalnlALENYPGTLIFVSHDREFVsSLAT 501
Cdd:PRK00635 472 RALATLSGGEQERTALAKhlgaeligitYILDEPSIGLHPQDTHKL-INVIK----KLRDQGNTVLLVEHDEQMI-SLAD 545
|
90 100
....*....|....*....|....*...
gi 1502692530 502 RIIELSP-----SGVIDFSGTYDDYLRS 524
Cdd:PRK00635 546 RIIDIGPgagifGGEVLFNGSPREFLAK 573
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
420-510 |
4.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 420 LGRMLFSndeilksvkvISGGEQGRMLFGKLIL---QKPNVLVMDEPTNHLDMESIEALNLALEN--YPG-TLIFVSHDR 493
Cdd:PRK00635 803 LGRPLSS----------LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNM 872
|
90
....*....|....*..
gi 1502692530 494 EFVsSLATRIIELSPSG 510
Cdd:PRK00635 873 HVV-KVADYVLELGPEG 888
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
327-491 |
4.90e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 327 KGFDGTTLFKDFSFTVEASERVAIIGPNGIGKTTLLRTLV----------------NELTpdAGSIKWTESAEIGYYAQd 390
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgtyegeiifegEELQ--ASNIRDTERAGIAIIHQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1502692530 391 hahdfedECTLFDWM---------GQWTQGGeqlvRGTLGRMLFSNDEILKSVKV----------ISGGEQGRMLFGKLI 451
Cdd:PRK13549 90 -------ELALVKELsvleniflgNEITPGG----IMDYDAMYLRAQKLLAQLKLdinpatpvgnLGLGQQQLVEIAKAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1502692530 452 LQKPNVLVMDEPTNHLDMESIEAL-NLA--LENYPGTLIFVSH 491
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLlDIIrdLKAHGIACIYISH 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
5.01e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 5.01e-03
10 20
....*....|....*....|....*
gi 1502692530 164 VLLAQALFSDPEVLLLDEPTNHLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-183 |
5.29e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 39.23 E-value: 5.29e-03
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-216 |
5.39e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 5.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1502692530 162 LRVLLAQALFSDPEVLLLDEPTNHLDINTIRWLENVLT--------QRNSLMIIISHDRHFLN 216
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVeiiksrsqQRNFQLLVITHDEDFVE 1274
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
338-378 |
6.02e-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: 6.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1502692530 338 FSFTVEASERVAIIGPNGIGKTTLLRTLVNELTPDAGSIKW 378
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-192 |
7.95e-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: 37.41 E-value: 7.95e-03
10 20 30
....*....|....*....|....*....|
gi 1502692530 163 RVLLAQALFSDPEVLLLDEPTNHLDINTIR 192
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
152-209 |
9.61e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 9.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1502692530 152 PMSEVSPGWKLRVLLAQALFSDPEVLLLDEPTNHLDINT---IRWLENVLTQRNSLMIIIS 209
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAkyeIYKLINQLVQQGVAIIVIS 462
|
|
| |
