|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-530 |
0e+00 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 1240.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDTVIMGHKELWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRQNPFIRFEQDKKLFRNAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEFENDLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 VFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMA 480
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 481 LELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLRSKGIE 530
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-525 |
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: 760.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDT 84
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 VIMGHKELWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRV 164
Cdd:COG0488 82 VLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMTAA 244
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 245 TQARERLLADNAKKKAQIAELQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRqNPFIRFEQDKKLFRNALEVEG 324
Cdd:COG0488 242 AERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 325 LTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEyEFENDLTVFEW 404
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-ELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 405 MSQWKqEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELY 484
Cdd:COG0488 400 LRDGA-PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1352184330 485 QGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLR 525
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-523 |
4.33e-97 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 307.48 E-value: 4.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEfT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDTVIMGHKELWEVKQErdriyaLPEMSEE-DGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 160 WKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYD- 238
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 239 -EYMTAATQARERLLADNAKKKaqIAELQSFVSRFSANASKSRQATSRARQIDKIKLeeVKASSRQNPF-IRFEQDKKLF 316
Cdd:PRK10636 234 fEVQRATRLAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQdHEYEF- 395
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ-HQLEFl 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ENDLTVFEWMSQWKQEgDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIE 475
Cdd:PRK10636 389 RADESPLQHLARLAPQ-ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1352184330 476 SLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDY 523
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-523 |
9.97e-93 |
|
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: 293.38 E-value: 9.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDTVIMGHKE 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 92 LWEVKQERDRIYALpeMSEED------GYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQhyGPMSEVAPGWKLRVL 165
Cdd:TIGR03719 96 IKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKLSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMtaaT 245
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL---E 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 246 QARERLL----ADNAKKKAQIAELQsfvsrFSANASKSRQATSRARQidkIKLEEV--KASSRQNPF--IRFEQDKKLFR 317
Cdd:TIGR03719 249 QKQKRLEqeekEESARQKTLKRELE-----WVRQSPKGRQAKSKARL---ARYEELlsQEFQKRNETaeIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEyEFEN 397
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD-ALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 DLTVFEWMSqwkqEGDDEQAV-------RSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:TIGR03719 400 NKTVWEEIS----GGLDIIKLgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 471 MESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPE-RVIDFSGNYEDY 523
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEY 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-522 |
1.30e-91 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 293.01 E-value: 1.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVS-SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFT 80
Cdd:PRK11147 3 LISiHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDTVIMGHKELWEVKQERDRIYAL--PEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQhygPMSEVAP 158
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLveTDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYD 238
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 239 EYMTAATQAReRLLAD-NA---KKKAQiAEL---QSFVSRFSAN-----ASKS-RQATSRARQID---KIKLEEVKASSR 302
Cdd:PRK11147 240 QYLLEKEEAL-RVEELqNAefdRKLAQ-EEVwirQGIKARRTRNegrvrALKAlRRERSERREVMgtaKMQVEEASRSGK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 303 qnpfIRFeqdkklfrnalEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA 382
Cdd:PRK11147 318 ----IVF-----------EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 RIGYYAQdHEYEFENDLTVFEWMSQWKQE----GDDeqavRSILGRL---LFSQDDIKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:PRK11147 383 EVAYFDQ-HRAELDPEKTVMDNLAEGKQEvmvnGRP----RHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLARLFLK 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 456 KPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVID-FSGNYED 522
Cdd:PRK11147 458 PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGrYVGGYHD 525
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-523 |
1.21e-87 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 280.47 E-value: 1.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDTVIMGHKE 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 92 LWEVKQERDRIYAlpEMSEEDGY------KVADLEVKYGEMDGYSAEARagelllgvgipVEQHY---------GPMSEV 156
Cdd:PRK11819 98 VKAALDRFNEIYA--AYAEPDADfdalaaEQGELQEIIDAADAWDLDSQ-----------LEIAMdalrcppwdAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGN 236
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 237 YDEYMtaaTQARERLL----ADNAKKKAQIAELQsFVsRFSAnasKSRQATSRARqidkIK-LEEV--KASSRQNPF--I 307
Cdd:PRK11819 245 YSSWL---EQKAKRLAqeekQEAARQKALKRELE-WV-RQSP---KARQAKSKAR----LArYEELlsEEYQKRNETneI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 308 RFEQDKKLFRNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYY 387
Cdd:PRK11819 313 FIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEyEFENDLTVFEWMSqwkqEGDD-------EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK11819 393 DQSRD-ALDPNKTVWEEIS----GGLDiikvgnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 461 IMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPE-RVIDFSGNYEDY 523
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQVEWFEGNFQEY 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-525 |
2.17e-86 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 281.36 E-value: 2.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGgdLEPTLGnvsLDPNERIGKLRQDQFAfEEFTVLDTV 85
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQEVVG-DDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 IMGHKELWEVKQERDRIYALPEMSEEDGYKVAD----------------LEVKYGEM---DGYSAEARAGELLLGVGIPV 146
Cdd:PLN03073 256 LNTDIERTQLLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavsqrLEEIYKRLeliDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EQHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 227 YGELRVYPGNYDEY-MTAATQARERLLADNAKKKAQiAELQSFVSRFSANASKSRQATSRARQIDKIK-LEEVKassrQN 304
Cdd:PLN03073 416 GQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLGhVDAVV----ND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 305 PFIRFE---QDKKLFRNALEVEGLTKGFDNGP-LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE 380
Cdd:PLN03073 491 PDYKFEfptPDDRPGPPIISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 NARIGYYAQDHEYEFENDLTVFEWMSQWkQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PLN03073 571 KVRMAVFSQHHVDGLDLSSNPLLYMMRC-FPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 461 IMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLR 525
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-527 |
8.89e-60 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 206.07 E-value: 8.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 322 VEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEyeFENDLTV 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP--LDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 402 FEW---------------------MSQWKQEGDD----------------EQAVRSILGRLLFSQDDIKKPAKVLSGGEK 444
Cdd:COG0488 79 LDTvldgdaelraleaeleeleakLAEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 445 GRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYL 524
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
...
gi 1352184330 525 RSK 527
Cdd:COG0488 239 EQR 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-512 |
8.80e-59 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 191.51 E-value: 8.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQdheyefendl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 tvfewmsqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNM 479
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1352184330 480 ALELYQGTLIFVSHDREFVSSLATRILEITPER 512
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-229 |
4.79e-44 |
|
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: 152.60 E-value: 4.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQdqfafeeftvldt 84
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 vimghkelwevkqerdriyalpemseedgykvadlevkygemdgysaearagelllgvgipveqhygpMSevaPGWKLRV 164
Cdd:cd03221 71 --------------------------------------------------------------------LS---GGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-530 |
9.80e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 9.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------SENARIGYYAQDHE 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 393 yeFEND--LTVFEW--MSQWKQEG-------DDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:COG1121 86 --VDWDfpITVRDVvlMGRYGRRGlfrrpsrADREAVDEALERVgL--EDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 461 IMDEPTNHLDMESIESLnMAL--ELYQG--TLIFVSHDREFVSSLATRILEITPERVidFSGNYEDYLRSKGIE 530
Cdd:COG1121 162 LLDEPFAGVDAATEEAL-YELlrELRREgkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTPENLS 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-506 |
7.75e-37 |
|
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: 136.71 E-value: 7.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENA---RIGYY 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYEFenDLTVFE--------WMSQWKQEG-DDEQAVRSILGRLlfsqdDI----KKPAKVLSGGEKGRMLFGKLMM 454
Cdd:COG1120 81 PQEPPAPF--GLTVRElvalgrypHLGLFGRPSaEDREAVEEALERT-----GLehlaDRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 455 QKPNILIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-506 |
1.08e-36 |
|
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: 142.35 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPTLGNVSldpneriGKLRqdqFAFEE 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIS-------GEVL---LDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 79 FTVLDTVIMGhKELWEVKQErdriyalpEMSEEDGYKVAD-----LEVkyGEMDGYSAEARAGELLLGVGIPVEQHYGPm 153
Cdd:COG1123 73 LLELSEALRG-RRIGMVFQD--------PMTQLNPVTVGDqiaeaLEN--LGLSRAEARARVLELLEAVGLERRLDRYP- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:COG1123 141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 230 LrvypgnydeymtAATQARERLLADNAKKKAqiaelqsfVSRFSANASKSRQATSRARQIdkikleevkassrqnpfirf 309
Cdd:COG1123 221 I------------VEDGPPEEILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL-------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 310 eqdkklfrnaLEVEGLTKGFDNG-----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-------- 376
Cdd:COG1123 261 ----------LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdlt 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 377 KWSENA------RIGYYAQDHEYEFENDLTVFEWMSQ------WKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEK 444
Cdd:COG1123 331 KLSRRSlrelrrRVQMVFQDPYSSLNPRMTVGDIIAEplrlhgLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 445 GRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALEL---YQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDV-SVQAqiLNLLRDLqreLGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-508 |
5.13e-35 |
|
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: 130.73 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSENARIGYYAQDHEYE 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 FENDLTVFEW--MSQWKQEG-------DDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDE 464
Cdd:cd03235 81 RDFPISVRDVvlMGLYGHKGlfrrlskADKAKVDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1352184330 465 PTNHLDMESIESLnMAL--ELYQ-G-TLIFVSHDREFVSSLATRILEI 508
Cdd:cd03235 159 PFAGVDPKTQEDI-YELlrELRReGmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-512 |
1.95e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 128.75 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW----SENARIGYYAQ----DH 391
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepIRDAREDYRRRlaylGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 EYEFENDLTVFE----WMSQWKQEGDDEQAVRSI----LGRLLfsqddiKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:COG4133 83 ADGLKPELTVREnlrfWAALYGLRADREAIDEALeavgLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 464 EPTNHLDMESIESLNMALELY---QGTLIFVSHDREFVssLATRILEITPER 512
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-513 |
1.88e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-----------RIGYYA 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QdheyefENDL---TV---FEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:COG4619 81 Q------EPALwggTVrdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 463 DEPTNHLDMESIESLNMALELY----QGTLIFVSHDREFVSSLATRILEITPERV 513
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
324-527 |
2.77e-32 |
|
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: 130.44 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 324 GLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQdhEYEFENDLTVF 402
Cdd:TIGR03719 9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ--EPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 403 ------------------EWMSQWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLS 440
Cdd:TIGR03719 87 enveegvaeikdaldrfnEISAKYAEPDADFDKLAAEQAEL---QEIIDaadawdldsqleiamdalrcppwdADVTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 441 GGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNY 520
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 243
|
....*..
gi 1352184330 521 EDYLRSK 527
Cdd:TIGR03719 244 SSWLEQK 250
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
1.07e-31 |
|
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: 122.84 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVLDTVIMG---HKELWEvkqerdriyalpEMSEEDgykvadlevkygemdgysaEARAGELLLGVGIpv 146
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFG------------RPSAED-------------------REAVEEALERTGL-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 eQHYG--PMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDrhfLNM--- 217
Cdd:COG1120 128 -EHLAdrPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNLaar 203
|
250 260
....*....|....*....|....*...
gi 1352184330 218 VCTHMADLDYGELRVYpGNYDEYMTAAT 245
Cdd:COG1120 204 YADRLVLLKDGRIVAQ-GPPEEVLTPEL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-508 |
1.84e-31 |
|
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: 119.42 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSENA----RIGYYAQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 dhEYEFENDLTVFEWMSqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:cd03230 81 --EPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1352184330 470 DMESIESL-NMALELYQ--GTLIFVSHDREFVSSLATRILEI 508
Cdd:cd03230 127 DPESRREFwELLRELKKegKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-230 |
2.33e-30 |
|
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: 116.34 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNERIGKLRQdqfafeeftv 81
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkDIKKEPEEVKR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 ldtvimghkelwevkqerdRIYALPEmseEDGYkvadlevkYGEMDGYsaearagELLLgvgipveqhygpMSEvapGWK 161
Cdd:cd03230 74 -------------------RIGYLPE---EPSL--------YENLTVR-------ENLK------------LSG---GMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElkkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
324-527 |
4.77e-30 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.69 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 324 GLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQdhEYEFENDLTVF 402
Cdd:PRK11819 11 RVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ--EPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 403 ------------------EWMSQWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLS 440
Cdd:PRK11819 89 enveegvaevkaaldrfnEIYAAYAEPDADFDALAAEQGEL---QEIIDaadawdldsqleiamdalrcppwdAKVTKLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 441 GGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNY 520
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNY 245
|
....*..
gi 1352184330 521 EDYLRSK 527
Cdd:PRK11819 246 SSWLEQK 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-504 |
1.61e-29 |
|
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: 121.83 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNV-----------SLDPNERIG-KLRQ 71
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgYVERPSKVGePCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVlDTVIMGHKELWEVKQER----DRIYALpemSEEDgyKVADLEVKYGEMDGYSAEA---RAGELLLGVGI 144
Cdd:TIGR03269 85 CGGTLEPEEV-DFWNLSDKLRRRIRKRIaimlQRTFAL---YGDD--TVLDNVLEALEEIGYEGKEavgRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 145 pveQHYgpMSEVAP----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRW----LEQVLNERDSTMIIISHDRHFLN 216
Cdd:TIGR03269 159 ---SHR--ITHIARdlsgGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 217 MVCTHMADLDYGELrVYPGNYDEymtaatqarerlladnakkkaqiaelqsFVSRFSANASKSRQATSRARQIDKIKLEE 296
Cdd:TIGR03269 234 DLSDKAIWLENGEI-KEEGTPDE----------------------------VVAVFMEGVSEVEKECEVEVGEPIIKVRN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 297 VKASsrqnpFIRFEQdkklfrnaleveGLTKGFDNgplfknLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV 376
Cdd:TIGR03269 285 VSKR-----YISVDR------------GVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 377 ------KWSENARIG---------YYAQDH-EY------------------EFENDLTVFEWMSQWKQEGDDEQAVRSIL 422
Cdd:TIGR03269 342 nvrvgdEWVDMTKPGpdgrgrakrYIGILHqEYdlyphrtvldnlteaiglELPDELARMKAVITLKMVGFDEEKAEEIL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 423 GRLlfsqddikkPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD-------MESIesLNMALELYQgTLIFVSHDR 495
Cdd:TIGR03269 422 DKY---------PDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSI--LKAREEMEQ-TFIIVSHDM 488
|
....*....
gi 1352184330 496 EFVSSLATR 504
Cdd:TIGR03269 489 DFVLDVCDR 497
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
4.87e-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: 114.17 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP------NERIGKLRQdQFAFE- 77
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 78 EF--TVLDTVIMGhkeLWEvkqerdRIYALPEMSEEDgykvadlevkygemdgysaEARAGELLLGVGIpVEQHYGPMSE 155
Cdd:cd03235 82 DFpiSVRDVVLMG---LYG------HKGLFRRLSKAD-------------------KAKVDEALERVGL-SELADRQIGE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQvLNERDSTMIIISHDrhfLNMVCTH 221
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHD---LGLVLEY 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-506 |
5.82e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSEN----ARIGYYAQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHeyEFENDLTVFEWMSQWKQ-----EGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:COG1131 81 EP--ALYPDLTVRENLRFFARlyglpRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 464 EPTNHLDMESIESL-NMALELYQG--TLIFVSHDREFVSSLATRIL 506
Cdd:COG1131 157 EPTSGLDPEARRELwELLRELAAEgkTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-467 |
6.97e-29 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 111.59 E-value: 6.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 335 FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-----------SENARIGYYAQDHeyEFENDLTVFE 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 404 ------WMSQWKQEGDDEQA--VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTN 467
Cdd:pfam00005 79 nlrlglLLKGLSKREKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
1.34e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQdQF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AFEE---FTVLDTVIMG---HKELWEVKQERDRiyalpemseedgykvadlevkygemdgysaeARAGELLLGVGIpveQ 148
Cdd:COG1121 85 EVDWdfpITVRDVVLMGrygRRGLFRRPSRADR-------------------------------EAVDEALERVGL---E 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 149 HYG--PMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDrhfLNMV---CT 220
Cdd:COG1121 131 DLAdrPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHD---LGAVreyFD 207
|
250 260
....*....|....*....|....*...
gi 1352184330 221 HMADLDYGelRVYPGNYDEYMTAATQAR 248
Cdd:COG1121 208 RVLLLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-239 |
1.84e-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: 113.41 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----------PNERIGKLR 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 QDQFAFEEFTVLDtVIMGHKELWEVKqerdriyalpemSEEDGYKVADLEVKYGeMDGYsAEARAGELllgvgipveqhy 150
Cdd:COG4555 81 DERGLYDRLTVRE-NIRYFAELYGLF------------DEELKKRIEELIELLG-LEEF-LDRRVGEL------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 151 gpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:COG4555 134 ------STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRalkKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
250
....*....|..
gi 1352184330 228 GELrVYPGNYDE 239
Cdd:COG4555 208 GKV-VAQGSLDE 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.93e-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: 112.19 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA----- 75
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRRrlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 ------FEEFTVLDTVIMgHKELWEVKQERDRIYALPEMSEEDGYkvADLEVKYgemdgYSAearagelllgvgipveqh 149
Cdd:COG4133 81 ghadglKPELTVRENLRF-WAALYGLRADREAIDEALEAVGLAGL--ADLPVRQ-----LSA------------------ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 150 ygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRHFL 215
Cdd:COG4133 135 ---------GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhlaRGGAVLLTTHQPLEL 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
2.01e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.41 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRqdqfafeeftvldt 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 vimghkelweVKQERDRIYALPEMSeedgykvadlevkygemdgysaearagelllgvgipveqhygpmsevaPGWKLRV 164
Cdd:cd00267 68 ----------LEELRRRIGYVPQLS------------------------------------------------GGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
328-527 |
4.49e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.51 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 328 GFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEFENdlTVFEWMSQ 407
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEG--TVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 408 WKQE-GDDEQAVRSILGRLLFSQDD--IKKPAKV---------------------------------LSGGEKGRMLFGK 451
Cdd:PRK11147 90 GIEEqAEYLKRYHDISHLVETDPSEknLNELAKLqeqldhhnlwqlenrinevlaqlgldpdaalssLSGGWLRKAALGR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 452 LMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLRSK 527
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEK 245
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-230 |
5.18e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.69 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----------PNERIGKLRQDQFA 75
Cdd:COG1131 5 GLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTVIMghkelwevkqerdriyalpemseedgykVADLevkYGeMDGYSAEARAGELLLGVGIPVEQH--YGPM 153
Cdd:COG1131 85 YPDLTVRENLRF----------------------------FARL---YG-LPRKEARERIDELLELFGLTDAADrkVGTL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 154 SevaPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:COG1131 133 S---GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELlreLAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-506 |
1.20e-27 |
|
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: 111.10 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR--IGYYAQ 389
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREARrqIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHE-YEFendLTVFEWM----SQWKQEGDD-EQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:COG4555 82 ERGlYDR---LTVRENIryfaELYGLFDEElKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 464 EPTNHLDMESIESL-NMALELYQ--GTLIFVSHDREFVSSLATRIL 506
Cdd:COG4555 158 EPTNGLDVMARRLLrEILRALKKegKTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-506 |
1.39e-27 |
|
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: 109.65 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGF-DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN--------ARIGYYAQDH 391
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 EYEFENDlTVF-EWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:cd03226 81 DYQLFTD-SVReELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1352184330 471 MESIESL-NMALELY-QGTLIFV-SHDREFVSSLATRIL 506
Cdd:cd03226 159 YKNMERVgELIRELAaQGKAVIViTHDYEFLAKVCDRVL 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-508 |
1.94e-27 |
|
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: 109.48 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-----------RIGYY 387
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYEFENDlTVFE----WMSQWKQEGDD-EQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:cd03225 81 FQNPDDQFFGP-TVEEevafGLENLGLPEEEiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 463 DEPTNHLDMESIESLnMAL--ELYQG--TLIFVSHDREFVSSLATRILEI 508
Cdd:cd03225 159 DEPTAGLDPAGRREL-LELlkKLKAEgkTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-508 |
3.19e-27 |
|
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: 107.33 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEnarigyyaqdheyefendlt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 vfewmsQWKQEGDDEQAVRSILgrLLFSqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESL-NM 479
Cdd:cd00267 61 ------KDIAKLPLEELRRRIG--YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlEL 122
|
170 180 190
....*....|....*....|....*....|.
gi 1352184330 480 ALELYQG--TLIFVSHDREFVSSLATRILEI 508
Cdd:cd00267 123 LRELAEEgrTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-508 |
1.01e-25 |
|
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: 104.88 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR---- 383
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 ---IGYYAQDHEYefENDLTVFE-----WMSQWKQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMM 454
Cdd:cd03255 81 rrhIGFVFQSFNL--LPDLTALEnvelpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 455 QKPNILIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVsSLATRILEI 508
Cdd:cd03255 157 NDPKIILADEPTGNLDsetgkevMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
1.10e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 328 GFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEFENDLTVFEW--M 405
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLvaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 406 SQWKQEG-------DDEQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLN 478
Cdd:NF040873 81 GRWARRGlwrrltrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|.
gi 1352184330 479 --MALELYQG-TLIFVSHDREFVSSlATRIL 506
Cdd:NF040873 160 alLAEEHARGaTVVVVTHDLELVRR-ADPCV 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-240 |
1.96e-25 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 110.02 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQ-------DQFAFEE 78
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdaldpNKTVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 79 FTV-LDTVIMGHKELwevkQERDRIYALpemseedGYKVADLEVKYGEMDGysaearaGElllgvgipveqhygpmseva 157
Cdd:TIGR03719 407 ISGgLDIIKLGKREI----PSRAYVGRF-------NFKGSDQQKKVGQLSG-------GE-------------------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 158 pgwKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMadLDY-GELRV--YP 234
Cdd:TIGR03719 449 ---RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFeGDSHVewFE 523
|
....*.
gi 1352184330 235 GNYDEY 240
Cdd:TIGR03719 524 GNFSEY 529
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-528 |
2.56e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 109.87 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 334 LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDH--------EYEFENDLTVFEWM 405
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpalpqpalEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 406 SQWKQ--EGDDEQAVRSILGRLL-------------------FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDE 464
Cdd:PRK10636 96 AQLHDanERNDGHAIATIHGKLDaidawtirsraasllhglgFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 465 PTNHLDMESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYEDYLRSKG 528
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
2.80e-25 |
|
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: 104.12 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----WSENARIGYYAQDHE-- 392
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSEAELYRLRRRmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 393 YEFE-----NDLTVFE----WMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILI 461
Cdd:cd03261 81 MLFQsgalfDSLTVFEnvafPLREHTRLSEEEirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 462 MDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVIdFSGNYEDYLRS 526
Cdd:cd03261 160 YDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-230 |
6.38e-25 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 102.80 E-value: 6.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----PNERIGKLRQ--------- 71
Cdd:COG1122 5 NLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglvfqnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 -DQFaFEEfTVLDTVIMGhkelwevkqerdriyalPE---MSEEDgykvadlevkygemdgysAEARAGELLLGVGIpve 147
Cdd:COG1122 85 dDQL-FAP-TVEEDVAFG-----------------PEnlgLPREE------------------IRERVEEALELVGL--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 148 QHYGpmsEVAP-----GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVC 219
Cdd:COG1122 125 EHLA---DRPPhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAELA 201
|
250
....*....|.
gi 1352184330 220 THMADLDYGEL 230
Cdd:COG1122 202 DRVIVLDDGRI 212
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
1.03e-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: 97.64 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 223 ADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKSRQATSRARQIDkiKLEEVKASSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALE--KMERIEKPER 78
|
....*..
gi 1352184330 303 QNPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-230 |
1.15e-24 |
|
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: 102.52 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA--------- 75
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 ----FEEFTVLDTVIMGHKElwevkQERDRIYALPEMSEEDgykvadlevkygemdgySAEARAGELLLGVGIpveQHYG 151
Cdd:cd03219 83 iprlFPELTVLENVMVAAQA-----RTGSGLLLARARREER-----------------EARERAEELLERVGL---ADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 --PMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQvLNERDSTMIIISHDRHFLNMVCTHMADL 225
Cdd:cd03219 138 drPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeeteELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVL 216
|
....*
gi 1352184330 226 DYGEL 230
Cdd:cd03219 217 DQGRV 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-506 |
1.62e-24 |
|
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: 100.20 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWS--ENAR-IGYYAQ 389
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSpkELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 dheyefendltvfeWMSQWKqegddeqaVRSILGRLLFSqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:cd03214 81 --------------ALELLG--------LAHLADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 470 D-------MESIESLNmalELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:cd03214 129 DiahqielLELLRRLA---RERGKTVVMVLHDLNLAARYADRVI 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-528 |
3.23e-24 |
|
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: 106.39 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENA---RIG 385
Cdd:COG4987 333 SLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHeYEF-----ENdLTVFewmsqwKQEGDDEQAVRSI----LGRLLFSQddikkPAKV----------LSGGEKGR 446
Cdd:COG4987 413 VVPQRP-HLFdttlrEN-LRLA------RPDATDEELWAALervgLGDWLAAL-----PDGLdtwlgeggrrLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 447 MLFGKLMMQKPNILIMDEPTNHLDMESIESLnMA--LELYQG-TLIFVSHDREFVsSLATRILEITPERVIDfSGNYEDY 523
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQAL-LAdlLEALAGrTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEEL 556
|
....*
gi 1352184330 524 LRSKG 528
Cdd:COG4987 557 LAQNG 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
316-529 |
3.49e-24 |
|
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: 106.84 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 316 FRNALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-------------WSE 380
Cdd:COG2274 470 LKGDIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpasLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 NarIGYYAQDheyefeNDL---TVFEWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGR 446
Cdd:COG2274 550 Q--IGVVLQD------VFLfsgTIRENITLGDPDATDEEIIEAA--RLAGLHDFIEAlPmgydtvvgegGSNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 447 MLFGKLMMQKPNILIMDEPTNHLDMES----IESLNmalELYQG-TLIFVSHDREFVsSLATRILEITPERVIDfSGNYE 521
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETeaiiLENLR---RLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHE 694
|
....*...
gi 1352184330 522 DYLRSKGI 529
Cdd:COG2274 695 ELLARKGL 702
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-210 |
3.95e-24 |
|
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: 101.31 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNvsldpnerigklrqdqfafeEFTVLDTV 85
Cdd:COG1119 8 NVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN--------------------DVRLFGER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 iMGHKELWEVKQerdRI-YALPEMSE--------ED-----GYKVADLEVKYGEMDgysaEARAGELL--LGVGIPVEQH 149
Cdd:COG1119 68 -RGGEDVWELRK---RIgLVSPALQLrfprdetvLDvvlsgFFDSIGLYREPTDEQ----RERARELLelLGLAHLADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 150 YGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISH 210
Cdd:COG1119 140 FGTLSQ---GEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-241 |
4.78e-24 |
|
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: 106.46 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNE---RIGKLRQ 71
Cdd:COG2274 477 ENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEfTVLDTVIMGH-----KELWEVKQE---RDRIYALPemseeDGYkvaDLEVkyGEMdgysaearagelllGVG 143
Cdd:COG2274 557 DVFLFSG-TIRENITLGDpdatdEEIIEAARLaglHDFIEALP-----MGY---DTVV--GEG--------------GSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 144 IPVEQhygpmsevapgwKLRVLLAQALFADPDILLLDEPTNNLDIDTirwlEQVLNE------RDSTMIIISHDRHFLNm 217
Cdd:COG2274 612 LSGGQ------------RQRLAIARALLRNPRILILDEATSALDAET----EAIILEnlrrllKGRTVIIIAHRLSTIR- 674
|
250 260
....*....|....*....|....*...
gi 1352184330 218 vcthMAD----LDYGELrVYPGNYDEYM 241
Cdd:COG2274 675 ----LADriivLDKGRI-VEDGTHEELL 697
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
6.71e-24 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.46 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAFEEFTVL---DTVIMG 88
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELRRKVGLVFqnpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 89 HKelwevkqerdriyalpemseedgykVADlEVKYG-EMDGYSAE---ARAGELLLGVGIPVEQHYGP--MSEvapGWKL 162
Cdd:cd03225 91 PT-------------------------VEE-EVAFGlENLGLPEEeieERVEEALELVGLEGLRDRSPftLSG---GQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELlkkLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
1.35e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 11 FGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQ-----DQFAFeefTVLDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPL---TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 IMG---HKELWEVKQERDRIyALPEMSEEDGykVADLEVKygemdgysaearagelllgvgipveqhygPMSEVAPGWKL 162
Cdd:NF040873 79 AMGrwaRRGLWRRLTRDDRA-AVDDALERVG--LADLAGR-----------------------------QLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRH 213
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEehaRGATVVVVTHDLE 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-506 |
2.11e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENA---RIGY 386
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHEyefendltvfewmsqwkqegddeqavrsilgrlLFS---QDDIkkpakvLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:cd03246 81 LPQDDE---------------------------------LFSgsiAENI------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 464 EPTNHLDMESIESLNMA---LELYQGTLIFVSHDREFVSSlATRIL 506
Cdd:cd03246 122 EPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLAS-ADRIL 166
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
2.18e-23 |
|
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: 99.34 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGS-KPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 ---------FEEFTVLDTVIMGHkelwevkQERDRIYALPEMSEEDGYKVADLEvkygemdgysAEARAGELLLGVGIpv 146
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAA-------HARLGRGLLAALLRLPRARREERE----------ARERAEELLERVGL-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 eQHYG--PMSEVAPGWKLRVLLAQALFADPDILLLDEPT---NNLDI-DTIRWLEQVLNERDSTMIIISHDRHFLNMVCT 220
Cdd:COG0411 143 -ADRAdePAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLAD 221
|
250
....*....|
gi 1352184330 221 HMADLDYGEL 230
Cdd:COG0411 222 RIVVLDFGRV 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-514 |
2.53e-23 |
|
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: 98.79 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN--------------ARI 384
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 385 GYYAQDheYEFENDLTVFE---------------WMSQWKQEgdDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLF 449
Cdd:cd03256 81 GMIFQQ--FNLIERLSVLEnvlsgrlgrrstwrsLFGLFPKE--EKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 450 GKLMMQKPNILIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
3.69e-23 |
|
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: 97.59 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR-IGYYAQD 390
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtGVPPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HeyefendlTVFEWMS-----------QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03259 81 Y--------ALFPHLTvaeniafglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE-LSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 460 LIMDEPTNHLDMESIESLNMALELYQG----TLIFVSHDREFVSSLATRIL 506
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-506 |
5.56e-23 |
|
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: 96.10 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS-------------ENARIGY 386
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHeyefendlTVFEWMSqwkqegddeqaVRSILgrllfsqddikkpAKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:cd03229 81 VFQDF--------ALFPHLT-----------VLENI-------------ALGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 467 NHLDMESIESLNMAL----ELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:cd03229 129 SALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-212 |
5.89e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 97.18 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGS----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQDQ 73
Cdd:cd03255 4 KNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFRRRH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 FAF--------EEFTVLDTVimghkelwevkqerdriyALPEMseedgykvadlevkYGEMDGYSAEARAGELLLGVGIP 145
Cdd:cd03255 84 IGFvfqsfnllPDLTALENV------------------ELPLL--------------LAGVPKKERRERAEELLERVGLG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 146 VEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDR 212
Cdd:cd03255 132 DRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-506 |
6.68e-23 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 97.40 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------SENA-----RIGYY 387
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYEFENDlTVFEWMS----QWKQEGDD-EQAVRSILGRLlfsqdDI----KKPAKVLSGGEKGRM-LFGKLMMQkP 457
Cdd:COG1122 81 FQNPDDQLFAP-TVEEDVAfgpeNLGLPREEiRERVEEALELV-----GLehlaDRPPHELSGGQKQRVaIAGVLAME-P 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 458 NILIMDEPTNHLDMESIESL-NMALELYQG--TLIFVSHDREFVSSLATRIL 506
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELlELLKRLNKEgkTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-518 |
7.16e-23 |
|
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: 96.49 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGeKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE----------NARIGYYAQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DheYEFENDLTVFE------WMSQWKQeGDDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:cd03264 80 E--FGVYPNFTVREfldyiaWLKGIPS-KEVKARVDEVLELVnLG--DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 463 DEPTNHLDMES-IESLNMALELYQGTLIFVS-HDREFVSSLATRILEITPERVIdFSG 518
Cdd:cd03264 155 DEPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-231 |
1.54e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.75 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD---------PNERIGKLRQD 72
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksyqknieALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEEFTVLDTVIMGHKELWEVKQERDRIYALPEMSEEDGYKVAdlevkygemdGYSaearagellLGVgipveqhygp 152
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVK----------GFS---------LGM---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 153 msevapgwKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQ-VLNERDS--TMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03268 132 --------KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElILSLRDQgiTVLISSHLLSEIQKVADRIGIINKGK 203
|
..
gi 1352184330 230 LR 231
Cdd:cd03268 204 LI 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-259 |
1.57e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 97.88 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpneRIGklrqdqfafeeftvlDTV 85
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI------KIG---------------ETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 IMGHkelweVKQERDRIyaLPEMS--EE--DGY---KVADLEVKygemdgysaeARAgelllgvgipveqhY-------G 151
Cdd:PRK11819 388 KLAY-----VDQSRDAL--DPNKTvwEEisGGLdiiKVGNREIP----------SRA--------------YvgrfnfkG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 P-----MSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMadLD 226
Cdd:PRK11819 437 GdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LA 514
|
250 260 270
....*....|....*....|....*....|....*.
gi 1352184330 227 Y-GELRV--YPGNYDEYmtaATQARERLLADNAKKK 259
Cdd:PRK11819 515 FeGDSQVewFEGNFQEY---EEDKKRRLGADAARPH 547
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
318-508 |
1.58e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.18 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR-- 383
Cdd:COG1136 3 PLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 -----IGYYAQDHeyefeN---DLTVFE-----WMSQWKQEGDDEQAVRSILGRL-LFSQDDiKKPAKvLSGGEKGRMLF 449
Cdd:COG1136 83 lrrrhIGFVFQFF-----NllpELTALEnvalpLLLAGVSRKERRERARELLERVgLGDRLD-HRPSQ-LSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 450 GKLMMQKPNILIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREfVSSLATRILEI 508
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDsktgeevLELLRELN---RELGTTIVMVTHDPE-LAARADRVIRL 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-506 |
1.72e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 97.96 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN--ERIGKLR----QDQFAfeeftvldtvimghkelwEVKQERDRIYA 104
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdEVLKRFRgtelQNYFK------------------KLYNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 105 LPEMSEE-----DGyKVADLEVKYGEmdgysaEARAGELL--LGVGIPVEQHYGPMSevapGWKL-RVLLAQALFADPDI 176
Cdd:PRK13409 165 KPQYVDLipkvfKG-KVRELLKKVDE------RGKLDEVVerLGLENILDRDISELS----GGELqRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 177 LLLDEPTNNLDI-------DTIRWLEQvlnerDSTMIIISHDRHFLNMvcthMADL---DYGElrvyPGNY--------- 237
Cdd:PRK13409 234 YFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDY----LADNvhiAYGE----PGAYgvvskpkgv 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 238 ----DEYMtaatqaRERLLADNAkkkaqiaelqsfvsRFsanasksrqatsrarqidkikleevkassRQNPfIRFE--- 310
Cdd:PRK13409 301 rvgiNEYL------KGYLPEENM--------------RI-----------------------------RPEP-IEFEerp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 311 -QDKKLFRNALEVEGLTKGFDNgplFKnlnllLEV-------GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEna 382
Cdd:PRK13409 331 pRDESERETLVEYPDLTKKLGD---FS-----LEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 RIGYYAQdheY-EFENDLTVFEWMSQWKQEGDD-----EQAVRSILGRLLfsqddiKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK13409 401 KISYKPQ---YiKPDYDGTVEDLLRSITDDLGSsyyksEIIKPLQLERLL------DKNVKDLSGGELQRVAIAACLSRD 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 457 PNILIMDEPTNHLDMEsiESLNMA------LELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:PRK13409 472 ADLYLLDEPSAHLDVE--QRLAVAkairriAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
2.11e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.58 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQD 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEEFTVLDTVIMGHKELWEVKQERdriyalpemseedgykvadlevkygemdgysaEARAGELLLGVGIPVEQHYGP 152
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEI--------------------------------RARVRELLELVGLEGLLNRYP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 153 mSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDtIRW-----LEQVLNERDSTMIIISHDR 212
Cdd:cd03259 129 -HELSGGQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
274-494 |
3.35e-21 |
|
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: 97.05 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 274 ANASKSRQATSRARqidkikLEEVKASSRQNPFIRFEQDKKLFRNA--LEVEGLTKGFDNGP-LFKNLNLLLEVGEKLAV 350
Cdd:TIGR02868 293 AAQQLTRVRAAAER------IVEVLDAAGPVAEGSAPAAGAVGLGKptLELRDLSAGYPGAPpVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 351 LGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSEN---ARIGYYAQD-HEYefenDLTVFEWMSQWKQEGDDEQAV 418
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVCAQDaHLF----DTTVRENLRLARPDATDEELW 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 419 RSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES----IESLNMALELYq 485
Cdd:TIGR02868 443 AALervgLADWLRALPDgldtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR- 521
|
....*....
gi 1352184330 486 gTLIFVSHD 494
Cdd:TIGR02868 522 -TVVLITHH 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-239 |
3.75e-21 |
|
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: 92.18 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQD------------ 72
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 -QFA--FEEFTVLDTVimghkelwevkqerdriyALP-----EMSEEDgykvadlevkygemdgysAEARAGELLLGVGI 144
Cdd:cd03261 83 fQSGalFDSLTVFENV------------------AFPlrehtRLSEEE------------------IREIVLEKLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 145 PVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQVLNerdSTMIIISHDRHFLNM 217
Cdd:cd03261 127 RGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFA 202
|
250 260
....*....|....*....|..
gi 1352184330 218 VCTHMADLDYGELrVYPGNYDE 239
Cdd:cd03261 203 IADRIAVLYDGKI-VAEGTPEE 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
5.20e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.42 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKLRQDQF 74
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsampPPEwrrQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AFEEfTVLDtvimgHkeLWEVKQERDRIYAlpemseedgykvadlevkygemdgysaEARAGELLLGVGIPVEQHYGPMS 154
Cdd:COG4619 85 LWGG-TVRD-----N--LPFPFQLRERKFD---------------------------RERALELLERLGLPPDILDKPVE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:COG4619 130 RLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
6.48e-21 |
|
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: 92.17 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGS----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----PNERIGKLRQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 -QFAFEE-FTVLD---TVimghkelwevkqerDRIYALPemseedgykvadLEVkYGEMDgysAEARAGELLLGVGIPVE 147
Cdd:COG1124 81 vQMVFQDpYASLHprhTV--------------DRILAEP------------LRI-HGLPD---REERIAELLEQVGLPPS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 148 QHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHflnmVCTHMA 223
Cdd:COG1124 131 FLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLA----VVAHLC 206
|
250
....*....|.
gi 1352184330 224 D----LDYGEL 230
Cdd:COG1124 207 DrvavMQNGRI 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-526 |
7.09e-21 |
|
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: 91.63 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLfKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS---------ENARIGYYAQD 390
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HeYEFENdLTVFEWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:cd03299 80 Y-ALFPH-MTVYKNIAyglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 466 TNHLDMES----IESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVIDFsGNYEDYLRS 526
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEEVFKK 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-508 |
9.97e-21 |
|
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: 91.40 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-----------SENAR 383
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYEFENDLTVFEWMSqwkqE-------GDDEQAVRSIL------GRLLFsqddiKKPAKvLSGGEKGRMLFG 450
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILA----EplrihglPDREERIAELLeqvglpPSFLD-----RYPHQ-LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 451 KLMMQKPNILIMDEPTNHLDMeSI--ESLNMALEL---YQGTLIFVSHDREFVSSLATRILEI 508
Cdd:COG1124 151 RALILEPELLLLDEPTSALDV-SVqaEILNLLKDLreeRGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-515 |
2.21e-20 |
|
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: 89.84 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------KWSENARIGYYAQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHeyefendlTVFEWMS-----------QWKQEGDDEQAVRSILGRL-L--FSQddiKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:cd03293 81 QD--------ALLPWLTvldnvalglelQGVPKAEARERAEELLELVgLsgFEN---AYPHQ-LSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 456 KPNILIMDEPTNHLDMESIESLNMAL-ELYQG---TLIFVSHDREFVSSLATRI--LEITPERVID 515
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELlDIWREtgkTVLLVTHDIDEAVFLADRVvvLSARPGRIVA 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-506 |
2.27e-20 |
|
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: 94.47 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-ERI-----GKLRQDQFAfeefTVLDtvimghKELwEVKQERDRIYA 104
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPSwDEVlkrfrGTELQDYFK----KLAN------GEI-KVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 105 LPEMSeeDGyKVADLEVKYGEmdgysaEARAGEL--LLGVGIPVEQHYGPMSevapGWKL-RVLLAQALFADPDILLLDE 181
Cdd:COG1245 172 IPKVF--KG-TVRELLEKVDE------RGKLDELaeKLGLENILDRDISELS----GGELqRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 182 PTNNLDI-------DTIRwleqVLNERDSTMIIISHDRHFLNMvcthMAD---LDYGElrvyPGNYDeymtAATQARERL 251
Cdd:COG1245 239 PSSYLDIyqrlnvaRLIR----ELAEEGKYVLVVEHDLAILDY----LADyvhILYGE----PGVYG----VVSKPKSVR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 252 LADNAKKKAQIAElqsfvsrfsanasksrqatsrarqidkiklEEVKAssRQNPfIRFE----QDKKLFRNALEVEGLTK 327
Cdd:COG1245 303 VGINQYLDGYLPE------------------------------ENVRI--RDEP-IEFEvhapRREKEEETLVEYPDLTK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 328 GFDNgplFKnlnllLEV-------GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkwSENARIGYYAQdheY-EFENDL 399
Cdd:COG1245 350 SYGG---FS-----LEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ---YiSPDYDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMEsiESLNM 479
Cdd:COG1245 417 TVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAV 494
|
490 500 510
....*....|....*....|....*....|...
gi 1352184330 480 A------LELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG1245 495 AkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-230 |
2.98e-20 |
|
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: 88.26 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAfEEFTVLDT 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA-RKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 VImghkELWEVKQERDRIYAlpEMSeedgykvadlevkygemdgysaearAGELllgvgipveQhygpmsevapgwklRV 164
Cdd:cd03214 81 AL----ELLGLAHLADRPFN--ELS-------------------------GGER---------Q--------------RV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDrhfLNMV---CTHMADLDYGEL 230
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNLAaryADRVILLKDGRI 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
318-527 |
3.29e-20 |
|
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: 89.65 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsENARIGYYAQDHEYEFE- 396
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DGQDITGLSEKELYELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 397 ------------NDLTVFE----WMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKvLSGGekgrmlfgklmMQK-- 456
Cdd:COG1127 83 rigmlfqggalfDSLTVFEnvafPLREHTDLSEAEirELVLEKLELVGLPGAADKMPSE-LSGG-----------MRKrv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 457 ---------PNILIMDEPTNHLD---MESIESLNMAL-ELYQGTLIFVSHDREFVSSLATRILEITPERVIdFSGNYEDY 523
Cdd:COG1127 151 alaralaldPEILLYDEPTAGLDpitSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKII-AEGTPEEL 229
|
....
gi 1352184330 524 LRSK 527
Cdd:COG1127 230 LASD 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-506 |
3.41e-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: 89.42 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFdnGPL--FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR----IG 385
Cdd:cd03219 1 LEVRGLTKRF--GGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEIarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEyEFENdLTVFE--------------WMSQW-KQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLF 449
Cdd:cd03219 79 RTFQIPR-LFPE-LTVLEnvmvaaqartgsglLLARArREEREARERAEELLERVgL--ADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 450 GKLMMQKPNILIMDEPT---NHLD----MESIESLNMalelyQG-TLIFVSHDREFVSSLATRIL 506
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEEteelAELIRELRE-----RGiTVLLVEHDMDVVMSLADRVT 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-527 |
3.48e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 89.76 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSG-TVKW------SEN-----ARIGY 386
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrgGEDvwelrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHEYEFENDLTVFE------------WmsqwkQEGDDEQA--VRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKL 452
Cdd:COG1119 83 VSPALQLRFPRDETVLDvvlsgffdsiglY-----REPTDEQRerARELLELLGLA-HLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 453 MMQKPNILIMDEPTNHLDMESIESLNMALELY--QG--TLIFVSHDREFVSSLATRILEITPERVIDfSGNYEDYLRSK 527
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLKDGRVVA-AGPKEEVLTSE 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-511 |
3.57e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 294 LEEVKASSRQNPFIRFEQDkklfrNALEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGdLQPD 372
Cdd:COG4178 342 LEAADALPEAASRIETSED-----GALALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 373 -SGTVKWSENARI-----------G------YYAQDHEyefendltvfewmsqwkQEGDDE-----QAVRsiLGRLLFSQ 429
Cdd:COG4178 416 gSGRIARPAGARVlflpqrpylplGtlrealLYPATAE-----------------AFSDAElrealEAVG--LGHLAERL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 430 DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLnMAL---ELYQGTLIFVSHdREFVSSLATRIL 506
Cdd:COG4178 477 DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL-YQLlreELPGTTVISVGH-RSTLAAFHDRVL 554
|
....*
gi 1352184330 507 EITPE 511
Cdd:COG4178 555 ELTGD 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-508 |
3.72e-20 |
|
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: 87.82 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsenarigyyaqdheyefeN 397
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 DLTVFEWmsqwkqegdDEQAVRSILGRL-----LFSqDDIKKpaKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDME 472
Cdd:cd03228 63 GVDLRDL---------DLESLRKNIAYVpqdpfLFS-GTIRE--NILSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 1352184330 473 SIESLNMAL-ELYQG-TLIFVSHDREFVsSLATRILEI 508
Cdd:cd03228 131 TEALILEALrALAKGkTVIVIAHRLSTI-RDADRIIVL 167
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
4.84e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.96 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA---- 75
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 -----FEEF------TVLDTV-----IMGHKElwevKQERDRIYALPEMseedgykVaDLEVKygemdgysAEARAGELL 139
Cdd:COG2884 80 rigvvFQDFrllpdrTVYENValplrVTGKSR----KEIRRRVREVLDL-------V-GLSDK--------AKALPHELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 140 LGvgipvEQHygpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQvLNERDSTMIIISHDRHFL 215
Cdd:COG2884 140 GG-----EQQ-------------RVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELV 200
|
.
gi 1352184330 216 N 216
Cdd:COG2884 201 D 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-475 |
5.14e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS-ENARIGYYAQD-----HEY 393
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 394 EFENDLTVFEWMSQWKQ--EGDDEQAVRSI----LGRLLfsqdDIkkPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTN 467
Cdd:PRK13539 83 AMKPALTVAENLEFWAAflGGEELDIAAALeavgLAPLA----HL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
....*...
gi 1352184330 468 HLDMESIE 475
Cdd:PRK13539 157 ALDAAAVA 164
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-235 |
7.91e-20 |
|
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: 88.54 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS---LDPNER-IGKLRQdqfafeeftvlDTVIMG 88
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvagLVPWKRrKKFLRR-----------IGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 89 HK-ELWEVKQERDRIYALPEMseedgYKVADLEVKyGEMDGYSAEARAGELLlgvgipveqhYGPMSEVAPGWKLRVLLA 167
Cdd:cd03267 102 QKtQLWWDLPVIDSFYLLAAI-----YDLPPARFK-KRLDELSELLDLEELL----------DTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 168 QALFADPDILLLDEPTNNLDI---DTIR-WLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPG 235
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVvaqENIRnFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-214 |
1.00e-19 |
|
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: 87.59 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQD------Q 73
Cdd:cd03262 5 NLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltdDKKNINELRQKvgmvfqQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 FA-FEEFTVLDTVIMGHKELWEvkqerdriyalpeMSEEDgykvadlevkygemdgysAEARAGELLLGVGIPVEQHYGP 152
Cdd:cd03262 85 FNlFPHLTVLENITLAPIKVKG-------------MSKAE------------------AEERALELLEKVGLADKADAYP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 153 mSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHF 214
Cdd:cd03262 134 -AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGF 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
337-514 |
1.09e-19 |
|
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: 87.74 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 337 NLNLLLEV-GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----W----------SENARIGYYAQdhEYEFENDLT 400
Cdd:cd03297 14 TLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLfdsrkkinlpPQQRKIGLVFQ--QYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 VFE---WMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES---- 473
Cdd:cd03297 92 VREnlaFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlql 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1352184330 474 IESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-505 |
1.24e-19 |
|
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: 87.27 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-----KWSENA----RIGYYAQD 390
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgkSYQKNIealrRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HeyEFENDLTVFEWMSQW-KQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:cd03268 81 P--GFYPNLTARENLRLLaRLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1352184330 470 DMESIESLN---MALELYQGTLIFVSHDREFVSSLATRI 505
Cdd:cd03268 158 DPDGIKELReliLSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-231 |
1.60e-19 |
|
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: 86.86 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGnRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNE---RIGKLRQDQF 74
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqPQKlrrRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AFEEFTVLDTVimghkelwevkqerDRIYALPEMSEEDgykvadlevkygemdgysAEARAGELLLGVGipVEQHYG-PM 153
Cdd:cd03264 83 VYPNFTVREFL--------------DYIAWLKGIPSKE------------------VKARVDEVLELVN--LGDRAKkKI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI-DTIRWLEqVLNERDSTMIII--SHDRHFLNMVCTHMADLDYGEL 230
Cdd:cd03264 129 GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIRFRN-LLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKL 207
|
.
gi 1352184330 231 R 231
Cdd:cd03264 208 V 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-506 |
1.94e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 87.18 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLF----KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEF 395
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ENDLTVFE--------WMS--------QWKQEGDDEQAVRSILGRLLFSQddIKKPAKV-------LSGGEKGRMLFGKL 452
Cdd:cd03257 82 KEIQMVFQdpmsslnpRMTigeqiaepLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVlnrypheLSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 453 MMQKPNILIMDEPTNHLDMES-IESLNMALEL---YQGTLIFVSHDREFVSSLATRIL 506
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVqAQILDLLKKLqeeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-506 |
1.98e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------SENARIGYYA 388
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDHeyefendlTVFEWMS-----------QWKQEGDDEQAVRSILGR--LLFSQDdiKKPaKVLSGGEK-----GRMLfg 450
Cdd:COG1116 87 QEP--------ALLPWLTvldnvalglelRGVPKAERRERARELLELvgLAGFED--AYP-HQLSGGMRqrvaiARAL-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 451 klmMQKPNILIMDEPTNHLDMESIESLN-MALELYQG---TLIFVSHD-REFVsSLATRIL 506
Cdd:COG1116 154 ---ANDPEVLLMDEPFGALDALTRERLQdELLRLWQEtgkTVLFVTHDvDEAV-FLADRVV 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-505 |
2.54e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 85.17 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsenarigyyaQDHEYEFENDL 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----------DGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 tvfewmsqwkqegddeQAVRsiLGRLLFSQddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLnm 479
Cdd:cd03216 71 ----------------DARR--AGIAMVYQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL-- 121
|
170 180 190
....*....|....*....|....*....|..
gi 1352184330 480 aLELY-----QG-TLIFVSHDREFVSSLATRI 505
Cdd:cd03216 122 -FKVIrrlraQGvAVIFISHRLDEVFEIADRV 152
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-239 |
2.65e-19 |
|
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: 86.96 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQD------------- 72
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrrigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFA--FEEFTVLDTVimghkelwevkqerdriyALP-----EMSEEDgykvadlevkygemdgysAEARAGELLLGVGIP 145
Cdd:COG1127 89 QGGalFDSLTVFENV------------------AFPlrehtDLSEAE------------------IRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 146 -VEQHYgPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-IDTIRWLEQVLNERDS---TMIIISHDRHFLNMVCT 220
Cdd:COG1127 133 gAADKM-P-SELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSAVIDELIRELRDElglTSVVVTHDLDSAFAIAD 210
|
250
....*....|....*....
gi 1352184330 221 HMADLDYGELRVYpGNYDE 239
Cdd:COG1127 211 RVAVLADGKIIAE-GTPEE 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-466 |
2.96e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKlrqdqfafeEFTVLDT 84
Cdd:COG1129 8 RGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GE---------PVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 -------VIMGHKELwevkqerdriyAL-PEMSeedgykVAD------LEVKYGEMDGYSAEARAGELL--LGVGIPVEQ 148
Cdd:COG1129 74 rdaqaagIAIIHQEL-----------NLvPNLS------VAEniflgrEPRRGGLIDWRAMRRRARELLarLGLDIDPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 149 hygPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE-RDS--TMIIIShdrHFLN--------- 216
Cdd:COG1129 137 ---PVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRlKAQgvAIIYIS---HRLDevfeiadrv 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 217 -------MVCTH-MADLDYGELrVypgnydEYMTaatqARErlladnakkkaqiaelqsFVSRFSAnasksrqatsRARQ 288
Cdd:COG1129 211 tvlrdgrLVGTGpVAELTEDEL-V------RLMV----GRE------------------LEDLFPK----------RAAA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 289 IDKIkleevkassrqnpfirfeqdkklfrnALEVEGLTKgfdnGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGD 368
Cdd:COG1129 252 PGEV--------------------------VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 369 LQPDSGTVKWSE------------NARIGYYAQDHEYE--------FEN-DLTVFEWMSQWK--QEGDDEQAVRSILGRL 425
Cdd:COG1129 302 DPADSGEIRLDGkpvrirsprdaiRAGIAYVPEDRKGEglvldlsiRENiTLASLDRLSRGGllDRRRERALAEEYIKRL 381
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1352184330 426 LFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:COG1129 382 RIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
3.04e-19 |
|
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: 84.62 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKLRQDQFAFEEFTVLDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 IMGhkelwevkqerdriyalpemseedgykVADLEVKYGEMDgysaeARAGELLLGVGIPVEQH---YGPMSEVAPGWKL 162
Cdd:pfam00005 81 RLG---------------------------LLLKGLSKREKD-----ARAEEALEKLGLGDLADrpvGERPGTLSGGQRQ 128
|
170 180
....*....|....*....|..
gi 1352184330 163 RVLLAQALFADPDILLLDEPTN 184
Cdd:pfam00005 129 RVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-506 |
3.27e-19 |
|
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: 86.49 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDN--GPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE-----------NARIG 385
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEYEF----ENdLTVFewmsqwKQEGDDEQAVRS--ILGRLLFSQDD-------IKKPAKVLSGGEKGRMLFGKL 452
Cdd:cd03245 82 YVPQDVTLFYgtlrDN-ITLG------APLADDERILRAaeLAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 453 MMQKPNILIMDEPTNHLDMESIESLNMALELYQG--TLIFVSHdREFVSSLATRIL 506
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRII 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
3.71e-19 |
|
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: 86.10 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKLRQDQFAFEEfTVLDTVI 86
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADlrrNIGYVPQDVTLFYG-TLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 87 MGHkelwevkqerdriyalPEMSEEDGYKVADLevkyGEMDGYSAEARAG-ELLLGvgipvEQHYGpmseVAPGWKLRVL 165
Cdd:cd03245 100 LGA----------------PLADDERILRAAEL----AGVTDFVNKHPNGlDLQIG-----ERGRG----LSGGQRQAVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 166 LAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFLNMV 218
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLLDLV 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-211 |
4.73e-19 |
|
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: 85.99 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQDQFA 75
Cdd:cd03293 5 NVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQQDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTVIMGHKELWEVKQERdriyalpemseedgykvadlevkygemdgysaEARAGELLLGVGIP-VEQHYgPmS 154
Cdd:cd03293 85 LPWLTVLDNVALGLELQGVPKAEA--------------------------------RERAEELLELVGLSgFENAY-P-H 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHD 211
Cdd:cd03293 131 QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.77e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.87 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERElar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 -------FAF------EEFTVLDTVimghkelwevkqerdriyALPEMseedgykvadlevkYGEMDGYSAEARAGELLL 140
Cdd:COG1136 83 lrrrhigFVFqffnllPELTALENV------------------ALPLL--------------LAGVSRKERRERARELLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 141 GVGIP-VEQHYgPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFL 215
Cdd:COG1136 131 RVGLGdRLDHR-P-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELA 208
|
..
gi 1352184330 216 NM 217
Cdd:COG1136 209 AR 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-528 |
4.97e-19 |
|
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: 90.20 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN-----------ARIGY 386
Cdd:COG4988 336 SIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQdHEYEFENdlTVFEWMSQWKQEGDDEQAVRSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMQKP 457
Cdd:COG4988 416 VPQ-NPYLFAG--TIRENLRLGRPDASDEELEAALeaagLDEFVAALPDgldtpLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 458 NILIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHDREFVsSLATRILEITPERVIDfSGNYEDYLRSKG 528
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALrRLAKGrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKNG 563
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
1.27e-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: 84.48 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGS--KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNERIGKLRQD---- 72
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngySIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 -QF--AFEEFTVLDTVimghkelwevkqerdRIYA-LPEMSEEDGYKVADLEVKYGEMDGYsAEARAGELllgvgipveq 148
Cdd:cd03263 81 pQFdaLFDELTVREHL---------------RFYArLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTL---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 149 hygpmsevAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03263 135 --------SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIMS 206
|
....*
gi 1352184330 227 YGELR 231
Cdd:cd03263 207 DGKLR 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
320-508 |
1.78e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.33 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW--------SENA------RI 384
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlKRREipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 385 GYYAQDHeyEFENDLTVFEWMS-----QWKQEGDDEQAVRSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:COG2884 82 GVVFQDF--RLLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVgLSDKAK-ALPHE-LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 459 ILIMDEPTNHLD-------MESIESLNMalelyQG-TLIFVSHDREFVSSLATRILEI 508
Cdd:COG2884 158 LLLADEPTGNLDpetsweiMELLEEINR-----RGtTVLIATHDLELVDRMPKRVLEL 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-514 |
1.91e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 88.42 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGdLQPDSGTV------------KWSENAR- 383
Cdd:COG1123 4 LLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 --IGYYAQDHEYEFeNDLTVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKV----LSGGEKGRMLFGKLMMQKP 457
Cdd:COG1123 83 rrIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRyphqLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 458 NILIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:COG1123 162 DLLIADEPTTALDvttqaeiLDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-493 |
1.96e-18 |
|
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: 83.13 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSenariGYYAQDHEYEFENDLTVFewmsqwkqeg 412
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-----GVPVSDLEKALSSLISVL---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 413 ddEQAVRsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES-IESLNMALELYQG-TLIF 490
Cdd:cd03247 81 --NQRPY------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIW 152
|
...
gi 1352184330 491 VSH 493
Cdd:cd03247 153 ITH 155
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
1.98e-18 |
|
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: 82.65 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFafeef 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNEL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 tvldtvimghkelwevkqeRDRIYALPEmseedgykvaDLEVkygeMDGYSAEArageLLLGvgipveqhygpmsevapG 159
Cdd:cd03246 75 -------------------GDHVGYLPQ----------DDEL----FSGSIAEN----ILSG-----------------G 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 160 WKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLASA 162
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-505 |
2.14e-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: 84.09 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLF--KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN----------ARIGYY 387
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQdHEYEFENdLTVFE---WMSQWK-QEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:cd03263 81 PQ-FDALFDE-LTVREhlrFYARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 464 EPTNHLDMESIESLNMALELYQG--TLIFVSHDREFVSSLATRI 505
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-511 |
2.40e-18 |
|
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: 82.20 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLvGDLQP-DSGTVKWSENARIGYYAQdHEYefen 397
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQ-RPY---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 dltvfewMSQwkqegddeqavrsilGRLlfsQDDIKKP-AKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIES 476
Cdd:cd03223 75 -------LPL---------------GTL---REQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 1352184330 477 LNMALELYQGTLIFVSHdREFVSSLATRILEITPE 511
Cdd:cd03223 130 LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-250 |
2.44e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.37 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMK-------ILGGDLepTLGNVS-LDPNERIGKLRQD 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDL--IVDGLKvNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 ------QF-AFEEFTVLDTVIMGHKelwevkQERDriyalpeMSEEDgykvadlevkygemdgysAEARAGELLLGVGIP 145
Cdd:PRK09493 79 agmvfqQFyLFPHLTALENVMFGPL------RVRG-------ASKEE------------------AEKQARELLAKVGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 146 VEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHM 222
Cdd:PRK09493 128 ERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVmqdLAEEGMTMVIVTHEIGFAEKVASRL 206
|
250 260
....*....|....*....|....*...
gi 1352184330 223 ADLDYGELRVyPGNYDEYMTAATQARER 250
Cdd:PRK09493 207 IFIDKGRIAE-DGDPQVLIKNPPSQRLQ 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-211 |
3.00e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 83.77 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DL---EPTLGNVSLD----------PNE---RI 66
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLipgAPDEGEVLLDgkdiydldvdVLElrrRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 67 GKLRQDQFAFeEFTVLDTVIMG---HKELWevKQERDRIyalpemsEEDGYKVADL--EVKygemdgysaeARAGELLLG 141
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGlrlHGIKL--KEELDER-------VEEALRKAALwdEVK----------DRLHALGLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 142 VGipvEQhygpmsevapgwkLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHD 211
Cdd:cd03260 144 GG---QQ-------------QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAElkKEYTIVIVTHN 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-505 |
3.37e-18 |
|
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: 83.46 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENAR-IGYYAQD 390
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 heYEFENDLTVFEWMS---QWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:cd03301 81 --YALYPHMTVYDNIAfglKLRKVPKDEidERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1352184330 466 TNHLD------MES-IESLNMALelyQGTLIFVSHDREFVSSLATRI 505
Cdd:cd03301 158 LSNLDaklrvqMRAeLKRLQQRL---GTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-230 |
4.28e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 83.40 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLE-PTLGNVSLDPNE--------------RI 66
Cdd:cd03258 6 NVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDGTDltllsgkelrkarrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 67 GKLRQdQFA-FEEFTVLDTVimghkelwevkqerdriyALPemseedgykvadLEVkyGEMDGYSAEARAGELLLGVGIP 145
Cdd:cd03258 85 GMIFQ-HFNlLSSRTVFENV------------------ALP------------LEI--AGVPKAEIEERVLELLELVGLE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 146 VEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFLNMVCTH 221
Cdd:cd03258 132 DKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDR 210
|
....*....
gi 1352184330 222 MADLDYGEL 230
Cdd:cd03258 211 VAVMEKGEV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
5.84e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwsPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQD---QFAfeeFTVLDTVIMGHKELWEVKQERDRIyALPEMSEEDgykVADLEVK-YGEMDGysaearaGElllgvgip 145
Cdd:PRK13548 82 PQHsslSFP---FTVEEVVAMGRAPHGLSRAEDDAL-VAAALAQVD---LAHLAGRdYPQLSG-------GE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 146 veqhygpmsevapgwKLRVLLAQAL------FADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDrhfL 215
Cdd:PRK13548 140 ---------------QQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---L 201
|
.
gi 1352184330 216 N 216
Cdd:PRK13548 202 N 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-229 |
6.70e-18 |
|
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: 81.46 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQD-QFAFE 77
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdLEDELPPLRRRiGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 78 EF------TVLDTVIMGhkelwevkqerdriyalpemseedgykvadlevkygemdgysaearagelLLGvgipveqhyg 151
Cdd:cd03229 84 DFalfphlTVLENIALG--------------------------------------------------LSG---------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 pmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQVLNERDS-TMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03229 104 -------GQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
..
gi 1352184330 228 GE 229
Cdd:cd03229 177 GK 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-498 |
8.38e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYEFEN 397
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 DLTVFEWMSQwkQEGDDEQAVRSILGRLLfSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESL 477
Cdd:PRK09544 83 PLTVNRFLRL--RPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|....*.
gi 1352184330 478 -----NMALELYQGTLIfVSHDREFV 498
Cdd:PRK09544 160 ydlidQLRRELDCAVLM-VSHDLHLV 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
307-514 |
1.51e-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: 82.00 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 307 IRFEQDKKLFRNALEVEGL---TKGFDNG-----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK- 377
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLigsLKSLFKRkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 -----WSEN----ARIGY-YAQDHEYEFenDLTVFEWMSQWKQ--EGDDEQAVRSI--LGRLLFSQDDIKKPAKVLSGGE 443
Cdd:cd03267 81 aglvpWKRRkkflRRIGVvFGQKTQLWW--DLPVIDSFYLLAAiyDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 444 KGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMAL----ELYQGTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeynRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.57e-17 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 81.53 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQD 72
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgedvnrlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 -QFAFEEF------TVLDTVimghkelwevkqerdriyALPemseedgykvadLEVKYGEMDGYsaEARAGELLLGVGIP 145
Cdd:TIGR02673 81 iGVVFQDFrllpdrTVYENV------------------ALP------------LEVRGKKEREI--QRRVGAALRQVGLE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 146 VEQHYGPMsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT---IRWLEQVLNERDSTMIIISHDRH 213
Cdd:TIGR02673 129 HKADAFPE-QLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-506 |
1.69e-17 |
|
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: 85.42 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGF-DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENA---RIGY 386
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladADADSwrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQdHEYEFENdlTVFEWMSQWKQEGDDEQAVRSI-----------LGRLLFSQddIKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:TIGR02857 401 VPQ-HPFLFAG--TIAENIRLARPDASDAEIREALeragldefvaaLPQGLDTP--IGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 456 KPNILIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHDREfVSSLATRIL 506
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALrALAQGrTVLLVTHRLA-LAALADRIV 527
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-514 |
1.77e-17 |
|
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: 82.17 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENARIGYYAQ-D 390
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARARRVALvE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HEYEFENDLTVFE--------WMSQWKQE-GDDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILI 461
Cdd:TIGR03873 82 QDSDTAVPLTVRDvvalgripHRSLWAGDsPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 462 MDEPTNHLDMES-IESLNMALELY--QGTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:TIGR03873 161 LDEPTNHLDVRAqLETLALVRELAatGVTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-506 |
2.21e-17 |
|
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: 81.04 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 335 FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSENARIGyyaqdheyeFENDLTVFE----- 403
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvsSLLGLGGG---------FNPELTGREniyln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 404 --WMSQWKQEGDDEqaVRSILGrllFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD-------ME 472
Cdd:cd03220 109 grLLGLSRKEIDEK--IDEIIE---FSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafqekcQR 183
|
170 180 190
....*....|....*....|....*....|....
gi 1352184330 473 SIESLNMAlelyQGTLIFVSHDREFVSSLATRIL 506
Cdd:cd03220 184 RLRELLKQ----GKTVILVSHDPSSIKRLCDRAL 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-489 |
2.55e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.61 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA---RIGYYAQD-----H 391
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGllylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 EYEFENDLTVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIkkPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM 471
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|
gi 1352184330 472 ESIESL--NMALELYQGTLI 489
Cdd:cd03231 159 AGVARFaeAMAGHCARGGMV 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-494 |
2.68e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSENAR-----IGYYA 388
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpiSMLSSRqlarrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDH---EyefenDLTVFE--------WMSQW-KQEGDDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK11231 83 QHHltpE-----GITVRElvaygrspWLSLWgRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1352184330 457 PNILIMDEPTNHLDM-ESIESLNMALELYQG--TLIFVSHD 494
Cdd:PRK11231 157 TPVVLLDEPTTYLDInHQVELMRLMRELNTQgkTVVTVLHD 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
2.84e-17 |
|
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: 81.01 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 17 FENISVKFGGGNRY-----------------GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFeef 79
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 tvldtvimgHKELWEVKQerDRIYAL-PEMSEEDgyKVADLEVKYGEMDGYSAEARAGELLL-GVGIPvEQHYG--PmSE 155
Cdd:cd03257 81 ---------RKEIQMVFQ--DPMSSLnPRMTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLvGVGLP-EEVLNryP-HE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIdTIRWleQVLN-------ERDSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQA--QILDllkklqeELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
..
gi 1352184330 229 EL 230
Cdd:cd03257 223 KI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-466 |
2.92e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 80.94 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW----------SENAR--IGYY 387
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglppHERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYeFENdLTVFE--WMSQWKQEGDDEQAvrsILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMQKPNIL 460
Cdd:cd03224 81 PEGRRI-FPE-LTVEEnlLLGAYARRRAKRKA---RLERVyeLFPrlKERRKQLAGTLSGGEQ-QMLaIARALMSRPKLL 154
|
....*.
gi 1352184330 461 IMDEPT 466
Cdd:cd03224 155 LLDEPS 160
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-514 |
3.15e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 80.40 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-------RIGYYAQDHE 392
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 393 -YEFENDLTVFEWMSQWKQEGDDEQA--VRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:cd03269 81 lYPKMKVIDQLVYLAQLKGLKKEEARrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1352184330 470 DMESIESLNMALELYQG---TLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03269 160 DPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-510 |
5.56e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-SENARigyyAQDHEYEFE-- 396
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR----RQRDEYHQDll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 397 ---------NDLTVFE---WMSQWKQEGDDEqAVRSILGRL-LFSQDDIkkPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:PRK13538 78 ylghqpgikTELTALEnlrFYQRLHGPGDDE-ALWEALAQVgLAGFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 464 EPTNHLDMESIESLNMALE--LYQ-GTLIFVSHDREFVSSLATRILEITP 510
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAqhAEQgGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
8.45e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQD-QFAFEeFTVLDTVIMGHKelwevkqerdriyalPEMSEEDGYKVADLEVKYGEMDGYSAEARAGElllgvgipveq 148
Cdd:PRK09536 83 PQDtSLSFE-FDVRQVVEMGRT---------------PHRSRFDTWTETDRAAVERAMERTGVAQFADR----------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 149 hygPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID-TIRWLEQV--LNERDSTMIIISHDrhfLNM 217
Cdd:PRK09536 136 ---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLELVrrLVDDGKTAVAAIHD---LDL 201
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-213 |
8.49e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.79 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGS--KPL--FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG4181 8 IIELRGLTKTVGTgaGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDArar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 -------FAFEEF------TVLDTVimghkelwevkqerdriyALPemseedgykvadLEVKyGEMDgysAEARAGELLL 140
Cdd:COG4181 87 lrarhvgFVFQSFqllptlTALENV------------------MLP------------LELA-GRRD---ARARARALLE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 141 GVGI-PVEQHY-GPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRH 213
Cdd:COG4181 133 RVGLgHRLDHYpAQLSG---GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPA 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-512 |
1.36e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.02 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFD----NG---PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGtvkwsenaRIGYYAQDHE 392
Cdd:COG4778 5 LEVENLSKTFTlhlqGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--------SILVRHDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 393 YefenDL------TVFE-------WMSQW------------------KQEGDDEQA---VRSILGRLlfsqdDIKK---- 434
Cdd:COG4778 77 V----DLaqasprEILAlrrrtigYVSQFlrviprvsaldvvaepllERGVDREEArarARELLARL-----NLPErlwd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 435 --PAkVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES----IESLNMALElyQGT-LIFVSHDREFVSSLATRILE 507
Cdd:COG4778 148 lpPA-TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGTaIIGIFHDEEVREAVADRVVD 224
|
....*
gi 1352184330 508 ITPER 512
Cdd:COG4778 225 VTPFS 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-527 |
1.92e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 335 FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWseNARI--------GyyaqdheyeFENDLTVfewms 406
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVsallelgaG---------FHPELTG----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 407 qwkqegddEQAVRSIlGRLL-FSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNH 468
Cdd:COG1134 106 --------RENIYLN-GRLLgLSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 469 LDME----SIESLNmalELYQ--GTLIFVSHDREFVSSLATRILEI---------TPERVIDFsgnYEDYLRSK 527
Cdd:COG1134 177 GDAAfqkkCLARIR---ELREsgRTVIFVSHSMGAVRRLCDRAIWLekgrlvmdgDPEEVIAA---YEALLAGR 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-511 |
2.63e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.60 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNvsldpnerigklRQDQF------AFEEFTVLdtvimghkelweVKQE-- 98
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGE------------RQSQFshitrlSFEQLQKL------------VSDEwq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 99 RDRIYALPEMSEEDGYKVADLEvkygeMDGYSAEARAGEL--LLGVGIPVEQHYGPMSEvapGWKLRVLLAQALFADPDI 176
Cdd:PRK10938 85 RNNTDMLSPGEDDTGRTTAEII-----QDEVKDPARCEQLaqQFGITALLDRRFKYLST---GETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 177 LLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHMADLDYGELrvypgnydeymtAATQARERLLA 253
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELlasLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTL------------AETGEREEILQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 254 DnakkkAQIAELqsfvsrfsanasksrqatSRARQIDKIKLEEvKASSRQNPFIRFEQDKKLFRNAleveglTKGFDNGP 333
Cdd:PRK10938 225 Q-----ALVAQL------------------AHSEQLEGVQLPE-PDEPSARHALPANEPRIVLNNG------VVSYNDRP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 334 LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGD-------------LQPDSGTVKWSENARIGYYAQDHEYEFENDLT 400
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 V--------FEWMSQWKQEGDDEQA-VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDm 471
Cdd:PRK10938 355 VrnvilsgfFDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD- 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1352184330 472 esieSLNMALELY---------QGTLIFVSHDREFVSSLATRILEITPE 511
Cdd:PRK10938 434 ----PLNRQLVRRfvdvlisegETQLLFVSHHAEDAPACITHRLEFVPD 478
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
2.79e-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: 77.71 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdqfafeeftvldtv 85
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 imGHKELWEVkqeRDRIYALPemsEEDG----YKVADLEVKYGEMDGYS---AEARAGELLLGVGIpVEQHYGPMSEVAP 158
Cdd:cd03269 61 --GKPLDIAA---RNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWLERLEL-SEYANKRVEELSK 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElarAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-505 |
3.48e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 313 KKLFRNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS--ENARIGYYAQD 390
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HEYEFENdLTVFEWMS-------QWKQE----GDDEQAVRSILGrLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNI 459
Cdd:PRK11607 93 INMMFQS-YALFPHMTveqniafGLKQDklpkAEIASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 460 LIMDEPTNHLDMESIESLNMA----LELYQGTLIFVSHDREFVSSLATRI 505
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-506 |
3.58e-16 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 77.57 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------------KWSE-NARIGY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQdHEYEFENdLTVFEWMS---QWKQEGDDEQAV---RSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03262 81 VFQ-QFNLFPH-LTVLENITlapIKVKGMSKAEAEeraLELLEKVgLADKAD-AYPAQ-LSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 460 LIMDEPTNHLDMESI-ESLNMALELYQG--TLIFVSHDREFVSSLATRIL 506
Cdd:cd03262 157 MLFDEPTSALDPELVgEVLDVMKDLAEEgmTMVVVTHEMGFAREVADRVI 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-249 |
5.08e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 80.97 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEP-----TLGNVSL---DPNE---RIGK 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqsgsiTLGGVDLrdlDEDDlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 69 LRQDQFAFEEfTVLDTVIMG-----HKELWEVKQE---RDRIYALPemseeDGYkvaDLEVkyGEmdgysaearAGELLL 140
Cdd:COG4987 414 VPQRPHLFDT-TLRENLRLArpdatDEELWAALERvglGDWLAALP-----DGL---DTWL--GE---------GGRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 141 GvGipvEQHygpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFLNMV 218
Cdd:COG4987 474 G-G---ERR-------------RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGRTVLLITHRLAGLERM 536
|
250 260 270
....*....|....*....|....*....|.
gi 1352184330 219 cTHMADLDYGELRVyPGNYDEYMTAATQARE 249
Cdd:COG4987 537 -DRILVLEDGRIVE-QGTHEELLAQNGRYRQ 565
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-514 |
5.61e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 302 RQNPFIRFEQDKKLFRNAL----EVEGLTKGF------DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDL-- 369
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLdlseRVAIVLEAFgvelrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 370 QPDSGTVKWSENarigyyaqdheyEFENDLTVFEwmsQWKQEGDDEQAVRsILGRL-LFSQDDIKKPAKVLSGGEKGRML 448
Cdd:COG2401 83 TPVAGCVDVPDN------------QFGREASLID---AIGRKGDFKDAVE-LLNAVgLSDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 449 FGKLMMQKPNILIMDEPTNHLDMES--IESLNMALELYQG--TLIFVSHDREFVSSLAtrileitPERVI 514
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTakRVARNLQKLARRAgiTLVVATHHYDVIDDLQ-------PDLLI 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
415-527 |
5.68e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.06 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 415 EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQGTLIFVSHD 494
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHA 400
|
90 100 110
....*....|....*....|....*....|...
gi 1352184330 495 REFVSSLATRILEITPERVIDFSGNYEDYLRSK 527
Cdd:PLN03073 401 REFLNTVVTDILHLHGQKLVTYKGDYDTFERTR 433
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-505 |
6.44e-16 |
|
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: 77.28 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE--------NAR-IGYYAQD 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlppHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 heYEFENDLTVFEWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:cd03300 81 --YALFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 466 TNHLDMESIESLNMALELYQG----TLIFVSHDREFVSSLATRI 505
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
6.92e-16 |
|
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: 77.22 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE--------------RIGKLRQDQFAFE 77
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 78 EFTVLDTVIMG---HKELWEvkqerdriyALPEMseedgYKVADLEvkygemdgysaeaRAGELLLGVGIpVEQHYGPMS 154
Cdd:cd03256 92 RLSVLENVLSGrlgRRSTWR---------SLFGL-----FPKEEKQ-------------RALAALERVGL-LDKAYQRAD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHD 211
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-211 |
8.13e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 76.99 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNER-IGKLRQDQFA 75
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERnVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTVIMGhkelwevkqerdriyalpemseedgykvadLEVKYGEMDGYSAE--ARAGELLLGVGIP-VEQHYgP 152
Cdd:cd03296 86 FRHMTVFDNVAFG------------------------------LRVKPRSERPPEAEirAKVHELLKLVQLDwLADRY-P 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 153 mSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHD 211
Cdd:cd03296 135 -AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-506 |
8.28e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 76.99 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENAR----------IGYYA 388
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDatdvpvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QdhEYEFENDLTVFEWMS-----QWKQEGDDEQAVRSILGRLL-FSQDDI---KKPAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03296 81 Q--HYALFRHMTVFDNVAfglrvKPRSERPPEAEIRAKVHELLkLVQLDWladRYPAQ-LSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 460 LIMDEPTNHLDMESIESLNMAL-ELYQG---TLIFVSHDREFVSSLATRIL 506
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLrRLHDElhvTTVFVTHDQEEALEVADRVV 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-233 |
1.17e-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: 76.03 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLRQDQFAFE-EFTVLDTV-----IMGHK 90
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLGGGFNpELTGRENIylngrLLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 91 ELwEVKQERDRIYALPEMSEedgykVADLEVKYgemdgYSAearagelllgvgipveqhygpmsevapGWKLRVLLAQAL 170
Cdd:cd03220 116 RK-EIDEKIDEIIEFSELGD-----FIDLPVKT-----YSS---------------------------GMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 171 FADPDILLLDEPTNNLDIDTIRWLEQVLNER---DSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-506 |
1.39e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.26 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA----------RIGYYAQ 389
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 D-----HeyefendLTVFEwms-qwKQEGDDEQAVRSILGRLL--FSQDDIKK--PAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:COG1118 83 HyalfpH-------MTVAEniafglRVRPPSKAEIRARVEELLelVQLEGLADryPSQ-LSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 460 LIMDEPTNHLD------MESieSLNMALELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG1118 155 LLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-515 |
1.39e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK----------WSENARIGYYA 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 Q----DHEYEFENDLTVFEwmsqwKQEGDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILI 461
Cdd:PRK13536 121 QfdnlDLEFTVRENLLVFG-----RYFGMSTREIEAVIPSLLeFARLESKADARVsdLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 462 MDEPTN-------HLDMESIESLnmaleLYQG-TLIFVSH---------DREFVSSLATRILEITPERVID 515
Cdd:PRK13536 196 LDEPTTgldpharHLIWERLRSL-----LARGkTILLTTHfmeeaerlcDRLCVLEAGRKIAEGRPHALID 261
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
1.61e-15 |
|
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: 79.25 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKL 69
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEfTVLDTVIMGhkelwevkqerdRIYALPEMSEEDGYKVAdlevkygeMDGYSAEARAG-ELLLGVGipveq 148
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA------------RPDASDAEIREALERAG--------LDEFVAALPQGlDTPIGEG----- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 149 hyGpmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTirwlEQVLNE------RDSTMIIISHDRHflnmvctHM 222
Cdd:TIGR02857 456 --G--AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEalralaQGRTVLLVTHRLA-------LA 520
|
....*
gi 1352184330 223 ADLDY 227
Cdd:TIGR02857 521 ALADR 525
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-514 |
1.82e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.48 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGT--------VKWSENAR--IGYYAQ 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DheYEFENDLTVFE---WMSQ---WKQEGDDEQAVRSILGRLLFSQDDikKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:cd03265 81 D--LSVDDELTGWEnlyIHARlygVPGAERRERIDELLDFVGLLEAAD--RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 464 EPTNHLDMES-------IESLNMAlelyQGTLIFV-SHDREFVSSLATRILEITPERVI 514
Cdd:cd03265 157 EPTIGLDPQTrahvweyIEKLKEE----FGMTILLtTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-494 |
1.98e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WS--ENARI-GYY 387
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSpaELARRrAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYEFenDLTVFE--WM--SQWKQ-EGDDEQAVRSIL---------GRLLfsqddikkPAkvLSGGEKGRMLFGKLM 453
Cdd:PRK13548 82 PQHSSLSF--PFTVEEvvAMgrAPHGLsRAEDDALVAAALaqvdlahlaGRDY--------PQ--LSGGEQQRVQLARVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 454 MQ------KPNILIMDEPTNHLDM-ESIESLNMALEL---YQGTLIFVSHD 494
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALDLaHQHHVLRLARQLaheRGLAVIVVLHD 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
2.16e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLrqdqfaFE-------EFTVLDTV-----I 86
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVSAL------LElgagfhpELTGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 87 MGHKElWEVKQERDRIYALPEMSEedgykVADLEVKYgemdgYSAearagelllgvgipveqhygpmsevapGWKLRVLL 166
Cdd:COG1134 116 LGLSR-KEIDEKFDEIVEFAELGD-----FIDQPVKT-----YSS---------------------------GMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 167 AQALFADPDILLLDEptnNL---DID----TIRWLEQVLnERDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:COG1134 158 AVATAVDPDILLVDE---VLavgDAAfqkkCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
320-466 |
2.84e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 75.40 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW----------SENAR--IGYY 387
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditglppHRIARlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYeFENdLTVFE--WMSQWKqeGDDEQAVRSILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMQKPNIL 460
Cdd:COG0410 84 PEGRRI-FPS-LTVEEnlLLGAYA--RRDRAEVRADLERVyeLFPrlKERRRQRAGTLSGGEQ-QMLaIGRALMSRPKLL 158
|
....*.
gi 1352184330 461 IMDEPT 466
Cdd:COG0410 159 LLDEPS 164
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-514 |
2.90e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN----------ARIGYYA 388
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QdheyeFEN---DLTVFEWMSQWKQE-GDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILI 461
Cdd:PRK13537 87 Q-----FDNldpDFTVRENLLVFGRYfGLSAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 462 MDEPTN-------HLDMESIESLnmaleLYQG-TLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK13537 162 LDEPTTgldpqarHLMWERLRSL-----LARGkTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-506 |
2.90e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNER----IGKLRQD 72
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarLTPAKAhqlgIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEEFTVLDTVIMGhkelwevkqerdriyaLPEmSEEDGYKVADLEVKYGEMdgYSAEARAGELllgvgipveqhygp 152
Cdd:PRK15439 95 PLLFPNLSVKENILFG----------------LPK-RQASMQKMKQLLAALGCQ--LDLDSSAGSL-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 153 msEVAPGWKLRVLlaQALFADPDILLLDEPTNNLD-IDTIRWLEQV--LNERDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:PRK15439 142 --EVADRQIVEIL--RGLMRDSRILILDEPTASLTpAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 230 LrVYPGNYDEYMTAATqarerlladnakkkaqiaelqsfvsrFSANASKSRQATSRARQidKIKLEeVKASSRQNPfirf 309
Cdd:PRK15439 218 I-ALSGKTADLSTDDI--------------------------IQAITPAAREKSLSASQ--KLWLE-LPGNRRQQA---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 310 eQDKKLfrnaLEVEGLTkgfdnGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENARIGYYA- 388
Cdd:PRK15439 264 -AGAPV----LTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKEINALSt 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 ---------------QDHEYEFENDLT------VFEWMSQWKQEGDdEQAV----RSILGrLLFSQDDikKPAKVLSGGE 443
Cdd:PRK15439 333 aqrlarglvylpedrQSSGLYLDAPLAwnvcalTHNRRGFWIKPAR-ENAVleryRRALN-IKFNHAE--QAARTLSGGN 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 444 KGRMLFGKLMMQKPNILIMDEPTNHLD----------MESIESLNMAlelyqgtLIFVSHDREFVSSLATRIL 506
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlIRSIAAQNVA-------VLFISSDLEEIEQMADRVL 474
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
3.16e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.06 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DqfafeeftvldtvimghkelwevkqerdriYAL-PEMSeedgykVADlEVKYG-EMDGYSAE---ARAGELLLGVGIpv 146
Cdd:COG3842 85 D------------------------------YALfPHLT------VAE-NVAFGlRMRGVPKAeirARVAELLELVGL-- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 147 eQHYG---PmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHDR 212
Cdd:COG3842 126 -EGLAdryP-HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
3.27e-15 |
|
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: 73.57 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQDQFAFEeft 80
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkNIAYVPQDPFLFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 vlDTVimghkelwevkqeRDRIyalpeMSeedgykvadlevkygemdgysaearAGElllgvgipveqhygpmsevapgw 160
Cdd:cd03228 90 --GTI-------------RENI-----LS-------------------------GGQ----------------------- 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRH 213
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-514 |
3.47e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENA------------RIGYY 387
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEhiqhyaskevarRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYefENDLTVFEWMS-----------QWKQEgdDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK10253 87 AQNATT--PGDITVQELVArgryphqplftRWRKE--DEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 457 PNILIMDEPTNHLDM-ESIESLNMALEL--YQG-TLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK10253 162 TAIMLLDEPTTWLDIsHQIDLLELLSELnrEKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-516 |
5.03e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 74.52 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG--DLQ---PDSGTV--------KWSEN----- 381
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIpgaPDEGEVlldgkdiyDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 382 ARIGYYAQdHEYEFenDLTVFEWMS--------QWKQEGDDEqaVRSILGR-LLFSQDDIKKPAKVLSGGEKGRMLFGKL 452
Cdd:cd03260 81 RRVGMVFQ-KPNPF--PGSIYDNVAyglrlhgiKLKEELDER--VEEALRKaALWDEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 453 MMQKPNILIMDEPTNHLDMES---IESLNMALElYQGTLIFVSHDREFVSSLATRILEITPERVIDF 516
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIStakIEELIAELK-KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
320-470 |
5.55e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENARIGY 386
Cdd:COG1101 2 LELKNLSKTFNPGtvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQdheyEFEN-------DLTVFEWMS-----------QWKQEGDDEQAVRSILGRL-LFSQDDIKKPAKVLSGGEkgRM 447
Cdd:COG1101 82 IGR----VFQDpmmgtapSMTIEENLAlayrrgkrrglRRGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQ--RQ 155
|
170 180
....*....|....*....|....*
gi 1352184330 448 LFGKLM--MQKPNILIMDEPTNHLD 470
Cdd:COG1101 156 ALSLLMatLTKPKLLLLDEHTAALD 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
6.02e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------------SLDPNER------IGKLRQDQFAFEEF 79
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtKPGPDGRgrakryIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 TVLD--TVIMGhKELWEVKQERDRIYALpemseedgyKVADLEVKYGE--MDGYSAEARAGElllgvgipveQHygpmse 155
Cdd:TIGR03269 381 TVLDnlTEAIG-LELPDELARMKAVITL---------KMVGFDEEKAEeiLDKYPDELSEGE----------RH------ 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 156 vapgwklRVLLAQALFADPDILLLDEPTNNLD-IDTIRWLEQVLNER---DSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:TIGR03269 435 -------RVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
6.80e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 73.94 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLG-------NVSLDPNE---RIGKLRQ 71
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREvrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVLDTVIMghkelwevkqeRDRIYALPemseedgykvadlevkygemdGYSAEARAGELLLGVGIpVEQHYG 151
Cdd:cd03265 81 DLSVDDELTGWENLYI-----------HARLYGVP---------------------GAERRERIDELLDFVGL-LEAADR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 PMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03265 128 LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH 207
|
....
gi 1352184330 228 GELR 231
Cdd:cd03265 208 GRII 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-212 |
7.15e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.95 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD---------PNER-IGKLRQDqfa 75
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlpPRERrVGFVFQH--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 feeftvldtvimghkelwevkqerdriYAL-PEMSeedgykVAD-----LEVKygEMDGYSAEARAGELLLGVGIP-VEQ 148
Cdd:COG1118 84 ---------------------------YALfPHMT------VAEniafgLRVR--PPSKAEIRARVEELLELVQLEgLAD 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 149 HYgPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI---DTIR-WLEQVLNERDSTMIIISHDR 212
Cdd:COG1118 129 RY-P-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-230 |
7.17e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.84 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNERIGKLRQDQFAFEeftvld 83
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRRDVQLVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 tvimghkelwevkqerDRIYAL-PEMSEEdgYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVE--QHYGPmsEVAPGW 160
Cdd:TIGR02769 96 ----------------DSPSAVnPRMTVR--QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdaDKLPR--QLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-242 |
7.22e-15 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 74.26 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNE---RIGKLRQD 72
Cdd:cd03295 4 ENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPVElrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEEFTVLDTVIMGHKELwevKQERDRIyalpemseedgykvadlevkygemdgysaEARAGELLLGVGIPvEQHYG- 151
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLL---KWPKEKI-----------------------------RERADELLALVGLD-PAEFAd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 --PmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVL----NERDSTMIIISHDRHFLNMVCTHMADL 225
Cdd:cd03295 131 ryP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
250
....*....|....*..
gi 1352184330 226 DYGELRVYpGNYDEYMT 242
Cdd:cd03295 210 KNGEIVQV-GTPDEILR 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
7.28e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV-----SLDP----------NERIGKLRQDQFAFEEFTVLD 83
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKlssaakaelrNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 TVimghkelwevkqerdriyALPEMseedgykvadlevkYGEMDGYSAEARAGELLLGVGIPVEQHYGPmSEVAPGWKLR 163
Cdd:PRK11629 107 NV------------------AMPLL--------------IGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDI---DTIRWLEQVLNERDST-MIIISHD 211
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
320-506 |
7.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLF-----KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGT------------VKWSE-N 381
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkVKLSDiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 382 ARIGYYAQDHEYE-FENdlTVFEWMSQWKQ-----EGDDEQAVRSILGRLLFSQDDIK-KPAKVLSGGEKGRMLFGKLMM 454
Cdd:PRK13637 83 KKVGLVFQYPEYQlFEE--TIEKDIAFGPInlglsEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 455 QKPNILIMDEPTNHLD-------MESIESLNmalELYQGTLIFVSHDREFVSSLATRIL 506
Cdd:PRK13637 161 MEPKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
319-505 |
9.61e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.52 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE--------NAR-IGYYAQ 389
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppEKRnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 D-----HeyefendLTVFE----WMSQWKQEGDD-EQAVRSILGRL-LFSQDDiKKPAKvLSGGEKgrmlfgklmmQ--- 455
Cdd:COG3842 85 DyalfpH-------LTVAEnvafGLRMRGVPKAEiRARVAELLELVgLEGLAD-RYPHQ-LSGGQQ----------Qrva 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 456 -------KPNILIMDEPTNHLDMESIESlnMALELYQ------GTLIFVSHDREFVSSLATRI 505
Cdd:COG3842 146 laralapEPRVLLLDEPLSALDAKLREE--MREELRRlqrelgITFIYVTHDQEEALALADRI 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
1.16e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 73.24 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF-----GSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdq 73
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 fafEEFTVLDTVIMGHKELWEVKqeRDRI-Y------ALPEMSEEDgyKVADLEVKYGEMDGySAEARAGELLLGVGIPV 146
Cdd:COG4778 72 ---HDGGWVDLAQASPREILALR--RRTIgYvsqflrVIPRVSALD--VVAEPLLERGVDRE-EARARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EQHygpmsEVAP-----GWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQvlneRDSTMIIISHDRHF 214
Cdd:COG4778 144 RLW-----DLPPatfsgGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKA----RGTAIIGIFHDEEV 214
|
250
....*....|..
gi 1352184330 215 LNMVCTHMADLD 226
Cdd:COG4778 215 REAVADRVVDVT 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
1.19e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpismlsSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVLDTVIMG---HKELWEvkqerdriyalpEMSEEDGYKVAdlevkygemdgySAEARAGELLLgvgipV 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLWG------------RLSAEDNARVN------------QAMEQTRINHL-----A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EQhygPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID---TIRWLEQVLNERDSTMIIISHDrhfLNMV---CT 220
Cdd:PRK11231 133 DR---RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD---LNQAsryCD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1352184330 221 HMADLDYGELrVYPGNYDEYMTaatqarERLLADNAKKKAQI 262
Cdd:PRK11231 207 HLVVLANGHV-MAQGTPEEVMT------PGLLRTVFDVEAEI 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-530 |
1.34e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-----------RIGYYA 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDHEYEFENDL-TVFEwMSQWKQEG-------DDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK09536 84 QDTSLSFEFDVrQVVE-MGRTPHRSrfdtwteTDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 461 IMDEPTNHLDM-ESIESLNMALELYQG--TLIFVSHDREFVSSLATRILEITPERVIDfSGNYEDYLRSKGIE 530
Cdd:PRK09536 162 LLDEPTASLDInHQVRTLELVRRLVDDgkTAVAAIHDLDLAARYCDELVLLADGRVRA-AGPPADVLTADTLR 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-513 |
1.42e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----------WSENAR 383
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYEF-------------ENDLTVFEWMSQWKQEGDDEQAVRSILGRllfsqddikKPAKvLSGGEKGRMLFG 450
Cdd:PRK13635 83 VGMVFQNPDNQFvgatvqddvafglENIGVPREEMVERVDQALRQVGMEDFLNR---------EPHR-LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 451 KLMMQKPNILIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSlATRIL---------EITPERV 513
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHDLDEAAQ-ADRVIvmnkgeileEGTPEEI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
1.59e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPT-----LGNVSLDPNERIGK------- 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirVGDITIDTARSLSQqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 69 LRQD-QFAFEEF------TVLDTVIMGhkelwevkqerdriyalpemseedgykvaDLEVKyGEMDGySAEARAGELLLG 141
Cdd:PRK11264 83 LRQHvGFVFQNFnlfphrTVLENIIEG-----------------------------PVIVK-GEPKE-EATARARELLAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 142 VGIPVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqVLNERDSTMIIISHDRHF 214
Cdd:PRK11264 132 VGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIR----QLAQEKRTMVIVTHEMSF 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1352184330 215 LNMVCTHMADLDYGELrVYPGNYDEYMTAATQARERLLAD 254
Cdd:PRK11264 207 ARDVADRAIFMDQGRI-VEQGPAKALFADPQQPRTRQFLE 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
1.80e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.35 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnERIGKLRQDQFAFEEF 79
Cdd:PRK13651 6 KNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI-----EWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 -TVLDTVIMG---HKELWEVKQERDRI--------YALPEMS-EEDgykVADLEVKYGeMDGYSAEARAGELLLGVGIPV 146
Cdd:PRK13651 81 eKVLEKLVIQktrFKKIKKIKEIRRRVgvvfqfaeYQLFEQTiEKD---IIFGPVSMG-VSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EqhYGPMS--EVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-IDTIRWLE--QVLNERDSTMIIISHD 211
Cdd:PRK13651 157 S--YLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
1.91e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.32 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP----NERIGKLR------ 70
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRqfinyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 -QDQFAFEEfTVLDTVIMGHKElwevKQERDRIYALPEMSEEDgykvADLEvkygemdgysaearagELLLGVGIPVEQH 149
Cdd:TIGR01193 554 pQEPYIFSG-SILENLLLGAKE----NVSQDEIWAACEIAEIK----DDIE----------------NMPLGYQTELSEE 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 150 YGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDT-IRWLEQVLNERDSTMIIISH 210
Cdd:TIGR01193 609 GSSISG---GQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH 667
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
317-506 |
2.35e-14 |
|
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: 75.55 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGF--DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENAR--- 383
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqWDREELgrh 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYeFENdlTVFEWMSQWkQEGDDEQAVRS---------ILgRLlfsqddikkP----------AKVLSGGEK 444
Cdd:COG4618 408 IGYLPQDVEL-FDG--TIAENIARF-GDADPEKVVAAaklagvhemIL-RL---------PdgydtrigegGARLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 445 -----GRMLFGKlmmqkPNILIMDEPTNHLDMESIESLNMALEL--YQG-TLIFVSHDREFVSSlATRIL 506
Cdd:COG4618 474 qriglARALYGD-----PRLVVLDEPNSNLDDEGEAALAAAIRAlkARGaTVVVITHRPSLLAA-VDKLL 537
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-231 |
2.39e-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: 72.40 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnerigklrqdqfafeeftvLDTvimgHKELWEVKQ 97
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-------------------FDV----VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 98 ------ERDRIYALPEMSEEDGYkVADLevkYGeMDGYSAEARAGEL--LLGVGIPVEQHYGPMSEvapGWKLRVLLAQA 169
Cdd:cd03266 79 rlgfvsDSTGLYDRLTARENLEY-FAGL---YG-LKGDELTARLEELadRLGMEELLDRRVGGFST---GMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 170 LFADPDILLLDEPTNNLDIDTIRWLEQVLNE-RD--STMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQlRAlgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-230 |
2.68e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 10 QFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQ--------DQFAFEEFTV 81
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-GQTINLVRDkdgqlkvaDKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTVIMGHKELWEVKQERDRIYALPemseedgykvadleVKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWK 161
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAP--------------IQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-515 |
2.95e-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: 72.02 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPL----FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV----------KWSENARIG 385
Cdd:cd03266 2 ITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkePAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YyaqdheyeFENDLTVFEWMSQWKQ----------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:cd03266 82 F--------VSDSTGLYDRLTARENleyfaglyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 456 KPNILIMDEPTNHLDMESIESLNMALELY---QGTLIFVSHDREFVSSLATRILEITPERVID 515
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
3.35e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 71.67 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQD-QFAF 76
Cdd:cd03292 5 NVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKiGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 EEFTVLdtvimghkelwevkqerdriyalPEMSEEDGYKVAdLEVKYgeMDGYSAEARAGELLLGVGIPVEQHYGPMsEV 156
Cdd:cd03292 85 QDFRLL-----------------------PDRNVYENVAFA-LEVTG--VPPREIRKRVPAALELVGLSHKHRALPA-EL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVL---NERDSTMIIISHDRHFLN 216
Cdd:cd03292 138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkiNKAGTTVVVATHAKELVD 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-239 |
3.45e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS---LDPNErigklRQDQFAFEEftvldTVIMGHK-ELW 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPFK-----RRKEFARRI-----GVVFGQRsQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 94 ---------EVKQErdrIYALPEmseedgykvADLEVKYGEMDGysaearagelLLGVG----IPVEQhygpMSEvapGW 160
Cdd:COG4586 109 wdlpaidsfRLLKA---IYRIPD---------AEYKKRLDELVE----------LLDLGelldTPVRQ----LSL---GQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDI---DTIR-WLEQVLNERDSTMIIISHDrhflnmvcthMAD----------LD 226
Cdd:COG4586 160 RMRCELAAALLHRPKILFLDEPTIGLDVvskEAIReFLKEYNRERGTTILLTSHD----------MDDiealcdrvivID 229
|
250
....*....|...
gi 1352184330 227 YGELrVYPGNYDE 239
Cdd:COG4586 230 HGRI-IYDGSLEE 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
320-508 |
3.75e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 71.67 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-------RIGYYAQD- 390
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 ----HEYEFENDLTVFEWMS---QWKQEGDDEQAVR-SILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:cd03292 81 gvvfQDFRLLPDRNVYENVAfalEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 463 DEPTNHLD-------MESIESLNMAlelyqGTLIFVS-HDREFVSSLATRILEI 508
Cdd:cd03292 161 DEPTGNLDpdttweiMNLLKKINKA-----GTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-515 |
4.61e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE----------------- 380
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 --NARIGYYAQD-----HEYEFENdltVFEWMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGK 451
Cdd:PRK11264 82 qlRQHVGFVFQNfnlfpHRTVLEN---IIEGPVIVKGEPKEEatARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 452 LMMQKPNILIMDEPTNHLDMESI-ESLNMALELYQG--TLIFVSHDREFVSSLATRILEITPERVID 515
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVgEVLNTIRQLAQEkrTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
318-513 |
5.58e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGP-LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV---------------KWSEN 381
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 382 ARIGYYAQDHE------YEfenDLTvFEWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:PRK13636 84 VGMVFQDPDNQlfsasvYQ---DVS-FGAVNLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 456 KPNILIMDEPTNHLDMESI-ESLNMALELYQG---TLIFVSH---------DREFVSSLATRILEITPERV 513
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHdidivplycDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-528 |
5.59e-14 |
|
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: 71.49 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-----------KWSENARIGYYA 388
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDhEYEFENdlTVFEWMSQWKQEGDDEQAVrsILGRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMQKP 457
Cdd:cd03254 84 QD-TFLFSG--TIMENIRLGRPNATDEEVI--EAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 458 NILIMDEPTNHLDMESIESLNMALE-LYQG-TLIFVSHdREFVSSLATRILEITPERVIDfSGNYEDYLRSKG 528
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEkLMKGrTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAKKG 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
6.36e-14 |
|
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: 74.32 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKLRQDQFAFEEfT 80
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDTVIMGHK-----ELWEVkQERDRIYALPEmSEEDGykvadLEVKYGEMdgysaearaGELLLGvgipveqhygpmse 155
Cdd:TIGR02868 425 VRENLRLARPdatdeELWAA-LERVGLADWLR-ALPDG-----LDTVLGEG---------GARLSG-------------- 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 156 vapGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERdsTMIIISHD 211
Cdd:TIGR02868 475 ---GERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR--TVVLITHH 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
8.63e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.99 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLG-------NVSLDPNERIGKLRQDQFAFeeftvldtvimghk 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLRREHFGF-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 91 elweVKQerdRIYALPEMSEEDGYKVADLevkYGEMDGYSAEARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQAL 170
Cdd:PRK10535 91 ----IFQ---RYHLLSHLTAAQNVEVPAV---YAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1352184330 171 FADPDILLLDEPTNNLD----IDTIRWLEQvLNERDSTMIIISHD 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-226 |
9.17e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFafeeftvLDTV 85
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-------LDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 ImghkelwEVKQERdriyalpEMSEEDGYKVADLevkygemdgYSAEAR--AGELLlgvgipvEQhygPMSEVAPGWKLR 163
Cdd:PRK09544 82 L-------PLTVNR-------FLRLRPGTKKEDI---------LPALKRvqAGHLI-------DA---PMQKLSGGETQR 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDI-------DTIrwlEQVLNERDSTMIIISHDRHFLnmvcthMADLD 226
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVngqvalyDLI---DQLRRELDCAVLMVSHDLHLV------MAKTD 189
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-245 |
1.03e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAfeeftvldtv 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 imghkelwevkqeRDRIYALPEMSEEDGYKVADLeVKYGEMDGYSAEARAG--------ELLLGVGI-PVEQHYgpMSEV 156
Cdd:PRK10575 85 -------------RKVAYLPQQLPAAEGMTVREL-VAIGRYPWHGALGRFGaadrekveEAISLVGLkPLAHRL--VDSL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 157 APGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDrhfLNMV---CTHMADLDYGE 229
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD---INMAaryCDYLVALRGGE 225
|
250
....*....|....*.
gi 1352184330 230 LrVYPGNYDEYMTAAT 245
Cdd:PRK10575 226 M-IAQGTPAELMRGET 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-210 |
1.37e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 68.61 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpnerigklrqdqfafeeftvldt 84
Cdd:cd03216 4 RGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV------------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 vimghkelwevkqerdriyalpemseeDGYKVADLEVKygemdgysaEARAgellLGVGIpVEQhygpMSevaPGWKLRV 164
Cdd:cd03216 60 ---------------------------DGKEVSFASPR---------DARR----AGIAM-VYQ----LS---VGERQMV 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISH 210
Cdd:cd03216 92 EIARALARNARLLILDEPTAALTPAEVERLFKVIRrlrAQGVAVIFISH 140
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-210 |
1.45e-13 |
|
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: 70.34 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKLRQD 72
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 qfafeefTVL--DTVimghkelwevkqeRDRI-YALPEMSEEDGY---KVADLEVKYGEM-DGYsaEARAGELLLgvgip 145
Cdd:cd03253 84 -------TVLfnDTI-------------GYNIrYGRPDATDEEVIeaaKAAQIHDKIMRFpDGY--DTIVGERGL----- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 146 veqhygpmsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03253 137 ---------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
1.45e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 70.44 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFAFEEFTVLDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 89 HKELWEVKQERDRiyALPEMSEedgykvadlevkygemdgysaearagelLLGVGIPVEQHYGPMSEvapGWKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAE----------------------------MLGIDHLLNRKPETLSG---GEQQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1352184330 169 ALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-514 |
2.07e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 69.44 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 338 LNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGtvkwsenaRIGYYAQDHEYE----------F-END----LTVF 402
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG--------RVLINGVDVTAAppadrpvsmlFqENNlfahLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 403 EWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD-MESIES 476
Cdd:cd03298 89 QNVGlglspGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALDpALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1352184330 477 LNMALELY---QGTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03298 168 LDLVLDLHaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-211 |
3.48e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 69.59 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 10 QFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKlrqdqfafeeftvldtviMGH 89
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID-GQDIAA------------------MSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 90 KELWEVKqeRDRI------YAL-PEMSeedgykVADlEVKYG-EMDGYSA---EARAGELLLGVGI-PVEQHYgpMSEVA 157
Cdd:cd03294 94 KELRELR--RKKIsmvfqsFALlPHRT------VLE-NVAFGlEVQGVPRaerEERAAEALELVGLeGWEHKY--PDELS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDiDTIR-----WLEQVLNERDSTMIIISHD 211
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRremqdELLRLQAELQKTIVFITHD 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-514 |
3.98e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------------SENARIGY 386
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsprdAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQdheyEFE--NDLTVFE--WMSQWKQEGD--DEQAVRSILGRLL--FSQD-DIKKPAKVLSGGEKGRMLFGKLMMQKP 457
Cdd:COG1129 84 IHQ----ELNlvPNLSVAEniFLGREPRRGGliDWRAMRRRARELLarLGLDiDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 458 NILIMDEPTNHLDMESIESL-NMALEL-YQG-TLIFVSH---------DR-------EFVSSLATRilEITPERVI 514
Cdd:COG1129 160 RVLILDEPTASLTEREVERLfRIIRRLkAQGvAIIYISHrldevfeiaDRvtvlrdgRLVGTGPVA--ELTEDELV 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-514 |
4.18e-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: 67.96 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGP------LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQP--DSGTV--------KWSENAR 383
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQD---HEYefendLTVFEwmsqwkqegddeqavrsilgRLLFSqddikkpAKV--LSGGEKGRMLFGKLMMQKPN 458
Cdd:cd03213 84 IGYVPQDdilHPT-----LTVRE--------------------TLMFA-------AKLrgLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 459 ILIMDEPTNHLD---MESIESLNMALELYQGTLIFVSHD-REFVSSLATRILEITPERVI 514
Cdd:cd03213 132 LLFLDEPTSGLDsssALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-526 |
4.90e-13 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 68.87 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENA---RIGYY 387
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgedireQDPVElrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQD-----HEYEFENDLTVFEwMSQWKQEGDDEQAVRSI----LGRLLFSQddiKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:cd03295 81 IQQiglfpHMTVEENIALVPK-LLKWPKEKIRERADELLalvgLDPAEFAD---RYPHE-LSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 459 ILIMDEPTNHLDMESIESL-----NMALELYQgTLIFVSHDREFVSSLATRILEITPERVIDFsGNYEDYLRS 526
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLqeefkRLQQELGK-TIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILRS 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
317-504 |
5.43e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 68.61 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDN--GPL--FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW--------SENAR- 383
Cdd:COG4181 6 APIIELRGLTKTVGTgaGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfalDEDARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 ------IGYYAQdheyEF---------ENDLTVFEwmsqWKQEGDDEQAVRSILGRLLFSQDDIKKPAkVLSGGEKGRML 448
Cdd:COG4181 86 rlrarhVGFVFQ----SFqllptltalENVMLPLE----LAGRRDARARARALLERVGLGHRLDHYPA-QLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 449 FGKLMMQKPNILIMDEPTNHLDM---ESIESLNMALELYQG-TLIFVSHDREfvssLATR 504
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHDPA----LAAR 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
5.77e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVLDTVIMG---HkelwevKQERdriyalpeMSEEDGYKVA------DLEvkygemdgysaearagelll 140
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpY------SKGR--------LTAEDREIIDeaiaylDLE-------------------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 141 gvgiPVEQHYgpMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHD 211
Cdd:COG4604 127 ----DLADRY--LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
319-516 |
7.04e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkwsenaRIGyyaqDHEYEFEND 398
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------NIA----GHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 LT-------------VFEWMSQW--------------------KQEGDDEQAvrSILGRLLFSQDDIKKPAKvLSGGEKG 445
Cdd:COG4161 72 PSekairllrqkvgmVFQQYNLWphltvmenlieapckvlglsKEQAREKAM--KLLARLRLTDKADRFPLH-LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 446 RMLFGKLMMQKPNILIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLATRILEITPERVIDF 516
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-244 |
7.08e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLR 70
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 QDQFAFEEFTVLDTVIMG---HKELWEVKQERDriyalpemseEDGYKVADLEVKYGEMDGYSAEARAGelllgvgipve 147
Cdd:PRK10253 88 QNATTPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKAMQATGITHLADQSVDTLSG----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 148 qhygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHDrhfLNMVC---T 220
Cdd:PRK10253 147 -----------GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQACryaS 212
|
250 260
....*....|....*....|....
gi 1352184330 221 HMADLDYGELrVYPGNYDEYMTAA 244
Cdd:PRK10253 213 HLIALREGKI-VAQGAPKEIVTAE 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
7.31e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKLRQDQFAFEEfT 80
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirdltLESlrrQIGVVPQDTFLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDTVIMGHK-----ELWEVKQE---RDRIYALPemseeDGYkvaDLEVkyGEmdgysaearAGELLLGvgipveqhygp 152
Cdd:COG1132 430 IRENIRYGRPdatdeEVEEAAKAaqaHEFIEALP-----DGY---DTVV--GE---------RGVNLSG----------- 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 153 msevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:COG1132 480 ------GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
7.47e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQdqfafeeftvldtvimghKELWEVKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD------------------KYIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 99 RDRIYALPEMSE-EDGykvADLEVKYG----EMDGYSAEARAGELLLGVGIP---VEQHYGPMSevapGWKLR-VLLAQA 169
Cdd:PRK13646 87 IGMVFQFPESQLfEDT---VEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMS----GGQMRkIAIVSI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 170 LFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-243 |
7.78e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnERIGKLRQDQFAFEEFTVldt 84
Cdd:PRK14246 14 SRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD--GKVLYFGKDIFQIDAIKL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 vimgHKELWEVKQERDriyALPEMSEEDgyKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQH---YGPMSEVAPGWK 161
Cdd:PRK14246 89 ----RKEVGMVFQQPN---PFPHLSIYD--NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVARVADYVAFLYNGEL-VEWGSSNE 238
|
....
gi 1352184330 240 YMTA 243
Cdd:PRK14246 239 IFTS 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-508 |
8.18e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENARIGYYAQDHEYEFEnDL 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQ-DA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVFEWMS-----------QWKQEGddEQAVRSIlGRLLFSQDdikKPAkVLSGGEKGRMLFGKLMMQKPNILIMDEPTNH 468
Cdd:PRK11247 91 RLLPWKKvidnvglglkgQWRDAA--LQALAAV-GLADRANE---WPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 469 LD-MESIESLNMALELYQG---TLIFVSHDREFVSSLATRILEI 508
Cdd:PRK11247 164 LDaLTRIEMQDLIESLWQQhgfTVLLVTHDVSEAVAMADRVLLI 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-187 |
9.62e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL----DPNE------RIGKLRQDQF 74
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpVPARarlaraRIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AFEEFTVLDTVI-------MGHKELWEVkqerdriyaLPEMSEedgykVADLEVKygemdgysAEARagelllgvgipve 147
Cdd:PRK13536 125 LDLEFTVRENLLvfgryfgMSTREIEAV---------IPSLLE-----FARLESK--------ADAR------------- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1352184330 148 qhygpMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:PRK13536 170 -----VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-512 |
1.02e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE----RIGKLRQDq 73
Cdd:COG3845 10 GITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaialGIGMVHQH- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 FA-FEEFTVLDTVIMGHKELWEVKQERDRIYAlpemseedgyKVADLEVKYG-EMDgysAEARAGEllLGVGipvEQHyg 151
Cdd:COG3845 89 FMlVPNLTVAENIVLGLEPTKGGRLDRKAARA----------RIRELSERYGlDVD---PDAKVED--LSVG---EQQ-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 152 pmsevapgwklRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLeqvlneRDS--TMIIISHDrhfLNMVcTHM 222
Cdd:COG3845 149 -----------RVEILKALYRGARILILDEPTAVLTpqeadelFEILRRL------AAEgkSIIFITHK---LREV-MAI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 223 ADldygelRV-------YPGNYDeymTAATQARErlladnakkkaqIAELqsFVSRfsanasksrqatsrarqidKIKLE 295
Cdd:COG3845 208 AD------RVtvlrrgkVVGTVD---TAETSEEE------------LAEL--MVGR-------------------EVLLR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 296 EVKASSRQNPfirfeqdkklfrNALEVEGLT-KGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSG 374
Cdd:COG3845 246 VEKAPAEPGE------------VVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 375 TVK--------WSENAR----IGYYAQD-HEYEFENDLTVFE----------------WMsqwkqegdDEQAVRSILGRL 425
Cdd:COG3845 314 SIRldgeditgLSPRERrrlgVAYIPEDrLGRGLVPDMSVAEnlilgryrrppfsrggFL--------DRKAIRAFAEEL 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 426 L--FsqdDIKK-----PAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESL-NMALEL-YQGT-LIFVSHDR 495
Cdd:COG3845 386 IeeF---DVRTpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIhQRLLELrDAGAaVLLISEDL 462
|
570 580
....*....|....*....|..
gi 1352184330 496 EFVSSLATRIL-----EITPER 512
Cdd:COG3845 463 DEILALSDRIAvmyegRIVGEV 484
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
1.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 11 FGSKPLFEnISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpneRIGKlrqdqfafeeftVLDTVIMGHK 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGD------------IVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 91 ELWEVKQERDRIYALPE--MSEEDGYKvadlEVKYGEMD-GYS---AEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRV 164
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPEsqLFEETVLK----DVAFGPQNfGIPkekAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 165 LLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVlNERDSTMIIISH 210
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESI-HQSGQTVVLVTH 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
320-506 |
1.09e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.47 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLfkNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsENARIGYYA----------Q 389
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTALPpaerpvsmlfQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHEYeFeNDLTVFEWM-----SQWKQEGDDEQAVRSILGRL-LFSQDDiKKPAKvLSGGEKGR-MLFGKLMMQKPnILIM 462
Cdd:COG3840 79 ENNL-F-PHLTVAQNIglglrPGLKLTAEQRAQVEQALERVgLAGLLD-RLPGQ-LSGGQRQRvALARCLVRKRP-ILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 463 DEPTNHLD------MesiesLNMALEL---YQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG3840 154 DEPFSALDpalrqeM-----LDLVDELcreRGLTVLMVTHDPEDAARIADRVL 201
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-513 |
1.10e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW---------SENARIGYYAQ 389
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 D-----HEYEFEN---DLTVFEwmsqwKQEGDDEQAVRSILGRLL----FSQDDIKKPAKvLSGGEKGRMLFGKLMMQKP 457
Cdd:PRK10851 82 HyalfrHMTVFDNiafGLTVLP-----RRERPNAAAIKAKVTQLLemvqLAHLADRYPAQ-LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 458 NILIMDEPTNHLDMESIESLNMAL----ELYQGTLIFVSHDREFVSSLATRILEI---------TPERV 513
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMsqgnieqagTPDQV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-505 |
1.18e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFD----NgplfKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsenarigyyaQDHEYE 394
Cdd:COG3845 5 ALELRGITKRFGgvvaN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI----------DGKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 FEN--------------------DLTVFE-----------WMSQWKQEgddEQAVRSILGRLLFSQDdikkP-AKV--LS 440
Cdd:COG3845 71 IRSprdaialgigmvhqhfmlvpNLTVAEnivlgleptkgGRLDRKAA---RARIRELSERYGLDVD----PdAKVedLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 441 GGEKGR--MLfgKLMMQKPNILIMDEPTNHLDMESIESL-----NMALElyQGTLIFVSHD-REfVSSLATRI 505
Cdd:COG3845 144 VGEQQRveIL--KALYRGARILILDEPTAVLTPQEADELfeilrRLAAE--GKSIIFITHKlRE-VMAIADRV 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-513 |
1.23e-12 |
|
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: 66.78 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDlqPDSGTVKwsenARIGYYAQDheyefENDL 399
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTE----GEILFKGED-----ITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVFEwmsqwkqegddeqavRSILGRLLFSQDDIKKPA-KV----------LSGGEKGRMLFGKLMMQKPNILIMDEPTNH 468
Cdd:cd03217 70 PPEE---------------RARLGIFLAFQYPPEIPGvKNadflryvnegFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1352184330 469 LDMESIESLNMALELYQG---TLIFVSHDRefvsslatRILE-ITPERV 513
Cdd:cd03217 135 LDIDALRLVAEVINKLREegkSVLIITHYQ--------RLLDyIKPDRV 175
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-519 |
1.37e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGP-LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------------KWSENaRI 384
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRS-KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 385 GYYAQDheyefeNDLTVFEwMSQWkqegDD---------------EQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLF 449
Cdd:PRK13647 82 GLVFQD------PDDQVFS-STVW----DDvafgpvnmgldkdevERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 450 GKLMMQKPNILIMDEPTNHLDMESIESLNMALELY--QG-TLIFVSHDREFVSSLATRILEITPERVIDFSGN 519
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-212 |
1.41e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErigklrqdqfafeeftV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED----------------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTVImghkelwevkQERD-----RIYAL-PEMSEEDgykvadlEVKYG-EMDGYSAE---ARAGELLLGVGIP-VEQHY 150
Cdd:PRK11432 71 THRSI----------QQRDicmvfQSYALfPHMSLGE-------NVGYGlKMLGVPKEerkQRVKEALELVDLAgFEDRY 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 151 gpMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI-------DTIRWLEQVLNerdSTMIIISHDR 212
Cdd:PRK11432 134 --VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFN---ITSLYVTHDQ 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-506 |
1.70e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-------SENARIGY----- 386
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYlpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 --YAqdheyefenDLTVFE---WMSQWK--QEGDDEQAVRSILGRLlfsqdDI----KKPAKVLSGGekgrmlfgklMMQ 455
Cdd:COG4152 81 glYP---------KMKVGEqlvYLARLKglSKAEAKRRADEWLERL-----GLgdraNKKVEELSKG----------NQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 456 K----------PNILIMDEPTNHLDMESIESL-NMALEL-YQG-TLIFVSHDREFVSSLATRIL 506
Cdd:COG4152 137 KvqliaallhdPELLILDEPFSGLDPVNVELLkDVIRELaAKGtTVIFSSHQMELVEELCDRIV 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-514 |
1.71e-12 |
|
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: 67.22 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENA----- 382
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 -RIGYYAQdhEYEFENDLTVFE----WMSQWKQEGDD-EQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQK 456
Cdd:cd03258 82 rRIGMIFQ--HFNLLSSRTVFEnvalPLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQ-LSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 457 PNILIMDEPTNHLDMESIES-------LNMALELyqgTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSilallrdINRELGL---TIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-505 |
1.96e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK------WSENAR-----IGYYAQDHEYEF-----ENDL 399
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENIRevrkfVGLVFQNPDDQIfsptvEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TvFEWMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESL-- 477
Cdd:PRK13652 101 A-FGPINLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELid 178
|
170 180 190
....*....|....*....|....*....|
gi 1352184330 478 --NMALELYQGTLIFVSHDREFVSSLATRI 505
Cdd:PRK13652 179 flNDLPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-231 |
2.17e-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: 66.55 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------------PNER-IGKLRQDQFAFEEFTVLDTVIMGHKE 91
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlpPQQRkIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 92 LwEVKQERDRIyalPEMSEedgykvadlevkygemdgysaearagelLLGVGIPVEQHYGPMSEvapGWKLRVLLAQALF 171
Cdd:cd03297 103 K-RNREDRISV---DELLD----------------------------LLGLDHLLNRYPAQLSG---GEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 172 ADPDILLLDEPTNNLDIDTIRWLEQVLNERDS----TMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKnlniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-239 |
2.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGklrqdqfafEEFT 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-----G---------EPLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLDtvimghkelwevkqeRDRI-YaLPemsEEDGY----KVADLEVKYGEMDGYS---AEARAGELL--LGVGipvEQHY 150
Cdd:COG4152 67 PED---------------RRRIgY-LP---EERGLypkmKVGEQLVYLARLKGLSkaeAKRRADEWLerLGLG---DRAN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 151 GPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDrhfLNMV---CTHMAD 224
Cdd:COG4152 125 KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVireLAAKGTTVIFSSHQ---MELVeelCDRIVI 201
|
250
....*....|....*
gi 1352184330 225 LDYGELRVYpGNYDE 239
Cdd:COG4152 202 INKGRKVLS-GSVDE 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-187 |
2.75e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL--DP--------NERIGKLRQDQFA 75
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTV-IMGHKELWEVKQERDRIYALPEMseedgykvADLEVKygemdgysAEARAGELllgvgipveqhygpms 154
Cdd:PRK13537 92 DPDFTVRENLlVFGRYFGLSAAAARALVPPLLEF--------AKLENK--------ADAKVGEL---------------- 139
|
170 180 190
....*....|....*....|....*....|...
gi 1352184330 155 evAPGWKLRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:PRK13537 140 --SGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
316-529 |
2.99e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.04 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 316 FRNALEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-----------SENAR 383
Cdd:COG1132 336 VRGEIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleSLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHeYEFenDLTVFEwmsqwkqegddeqAVRsiLGRLLFSQDDIKKPAKV------------------------L 439
Cdd:COG1132 416 IGVVPQDT-FLF--SGTIRE-------------NIR--YGRPDATDEEVEEAAKAaqahefiealpdgydtvvgergvnL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 440 SGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMAL-ELYQG-TLIFVSHdRefVSSL--ATRILEITPERVID 515
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALeRLMKGrTTIVIAH-R--LSTIrnADRILVLDDGRIVE 554
|
250
....*....|....
gi 1352184330 516 fSGNYEDYLRSKGI 529
Cdd:COG1132 555 -QGTHEELLARGGL 567
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
320-514 |
3.16e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.02 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPL-FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-------KWSENA------RIG 385
Cdd:PRK13639 2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepiKYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEYEF-----ENDLTvFEWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK13639 82 IVFQNPDDQLfaptvEEDVA-FGPLNLGLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 461 IMDEPTNHLD-MESIESLNMALEL-YQG-TLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK13639 160 VLDEPTSGLDpMGASQIMKLLYDLnKEGiTIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
3.34e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNERIGKLRQDQFAFEEF-- 79
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtDVSRLHARDRKVGFVFQHYal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 ----TVLDTVIMGHKELweVKQERDRIYALPemseedgYKVADLEvkygEMDGYSAEAragelllgvgipveQHYgPmSE 155
Cdd:PRK10851 86 frhmTVFDNIAFGLTVL--PRRERPNAAAIK-------AKVTQLL----EMVQLAHLA--------------DRY-P-AQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDR 212
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
3.55e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKL-RQDQFAFEEftvldTVIMGHK 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLnRAQRKAFRR-----DIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 91 ELWEVKQERDRIYA--------LPEMSEEDgykvadlevkygemdgysAEARAGELLLGVGIPVEQHYGPMSEVAPGWKL 162
Cdd:PRK10419 97 DSISAVNPRKTVREiireplrhLLSLDKAE------------------RLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-210 |
3.85e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 66.10 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQD 72
Cdd:cd03251 5 NVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEeftvlDTVimghkelwevkqeRDRI-YALPEMSEEDGYKVADLevkygemdgysaeARAGELL----LGVGIPVE 147
Cdd:cd03251 85 VFLFN-----DTV-------------AENIaYGRPGATREEVEEAARA-------------ANAHEFImelpEGYDTVIG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 148 QHYGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03251 134 ERGVKLSG---GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
4.35e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQ 71
Cdd:PRK13632 11 ENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeirkKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 D---QFAfeEFTVLDTVIMGhkeLWEVKQERDriyalpEMSEedgyKVADLEVKYGeMDGYsaearagelllgvgIPVEQ 148
Cdd:PRK13632 91 NpdnQFI--GATVEDDIAFG---LENKKVPPK------KMKD----IIDDLAKKVG-MEDY--------------LDKEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 149 HYgpmseVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13632 141 QN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
319-505 |
4.40e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW--------SENAR-IGYYAQ 389
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdlPPKDRnIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 D-----HeyefendLTVFEWMS---QWKQEGDDE--QAVRSILGRLlfsqdDI-----KKPAKvLSGGEK-----GRMLf 449
Cdd:COG3839 83 SyalypH-------MTVYENIAfplKLRKVPKAEidRRVREAAELL-----GLedlldRKPKQ-LSGGQRqrvalGRAL- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 450 gklmMQKPNILIMDEPTNHLDMESIESlnMALELYQ------GTLIFVSHDREFVSSLATRI 505
Cdd:COG3839 149 ----VREPKVFLLDEPLSNLDAKLRVE--MRAEIKRlhrrlgTTTIYVTHDQVEAMTLADRI 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-509 |
4.53e-12 |
|
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: 65.95 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsENARIGYYAQDHEYEFENdLTVFEWMSQWKQ----- 410
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQN-YSLLPWLTVRENialav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 --------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMAL- 481
Cdd:TIGR01184 80 drvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELm 158
|
170 180 190
....*....|....*....|....*....|.
gi 1352184330 482 ---ELYQGTLIFVSHDREFVSSLATRILEIT 509
Cdd:TIGR01184 159 qiwEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-465 |
4.61e-12 |
|
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: 65.64 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KW--SENAR--IGYY 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLpmHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYeF------ENDLTVFEWMsqwkqeGDDEQAVRSILGRLL--FSQDDI-KKPAKVLSGGEKGRMLFGKLMMQKPN 458
Cdd:cd03218 81 PQEASI-FrkltveENILAVLEIR------GLSKKEREEKLEELLeeFHITHLrKSKASSLSGGERRRVEIARALATNPK 153
|
....*..
gi 1352184330 459 ILIMDEP 465
Cdd:cd03218 154 FLLLDEP 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-514 |
4.76e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG--DLQPDSG----------------------- 374
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 375 ---------------------TVKWSENARIGYYAQDHEYEFENDL---TVFEWMSQWKQEGDDEQAVRSILGRLLFSQD 430
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRTFALYGDDTvldNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 431 DIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALEL----YQGTLIFVSHDREFVSSLATR-- 504
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSHWPEVIEDLSDKai 240
|
250
....*....|....*..
gi 1352184330 505 -------ILEITPERVI 514
Cdd:TIGR03269 241 wlengeiKEEGTPDEVV 257
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
5.02e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.26 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AFEEFTVLDTVIMGHKELWEVKQERdriyalpemseedgykvadlevkygemdgysaEARAGELLLGVGIP-VEQHYgpM 153
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQR--------------------------------LEIAHQMLKKVGLEgAEKRY--I 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVL----NERDSTMIIISHD 211
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-496 |
8.13e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGY----YAQDHEYEFEN---------DL 399
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiYRQQVSYCAQTptlfgdtvyDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVFEWmsQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNM 479
Cdd:PRK10247 101 LIFPW--QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180
....*....|....*....|.
gi 1352184330 480 ALELY----QGTLIFVSHDRE 496
Cdd:PRK10247 179 IIHRYvreqNIAVLWVTHDKD 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-518 |
9.13e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.12 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsENARIGYYAQDHEYEFEndLTVFEWMSQwkqegddeqaVRSILGR 424
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYE--GTVRDLLSS----------ITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 425 LLFSQDDIKKPAKV----------LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDME----SIESLNMALELYQGTLIF 490
Cdd:cd03237 92 HPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFV 171
|
170 180
....*....|....*....|....*...
gi 1352184330 491 VSHDREFVSSLAtrileitpERVIDFSG 518
Cdd:cd03237 172 VEHDIIMIDYLA--------DRLIVFEG 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-211 |
9.48e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 65.53 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------SLDPnERIGKLRQ------ 71
Cdd:TIGR04520 5 NVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldTLDE-ENLWEIRKkvgmvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 ----DQFafeeftVLDTVimghkelwevkqerdriyalpemsEEDgykVA----DLEVKYGEMdgysaEARAGELLLGVG 143
Cdd:TIGR04520 84 qnpdNQF------VGATV------------------------EDD---VAfgleNLGVPREEM-----RKRVDEALKLVG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 144 ipveqhygpMSE---VAP-----GWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQvlnERDSTMIII 208
Cdd:TIGR04520 126 ---------MEDfrdREPhllsgGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNK---EEGITVISI 193
|
...
gi 1352184330 209 SHD 211
Cdd:TIGR04520 194 THD 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 11 FGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdqfafeeftvlDTVIMGHK 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD---------------------DTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 91 ELWEVKQERDRI---YALPE--MSEEDGYKvadlEVKYGEMD-GYS---AEARAGELLLGVGIPVEQHYGPMSEVAPGWK 161
Cdd:PRK13649 76 KNKDIKQIRKKVglvFQFPEsqLFEETVLK----DVAFGPQNfGVSqeeAEALAREKLALVGISESLFEKNPFELSGGQM 151
|
170 180
....*....|....*....|....*.
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-493 |
1.19e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 303 QNPFIRF--EQDKKLFRNALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK- 377
Cdd:PRK11160 320 QKPEVTFptTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 -------WSENA----------RIGYY--------------AQDHEY-------EFENDLTVFEWMSQWKQEGddeqavr 419
Cdd:PRK11160 400 ngqpiadYSEAAlrqaisvvsqRVHLFsatlrdnlllaapnASDEALievlqqvGLEKLLEDDKGLNAWLGEG------- 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 420 silGRLlfsqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESiESLNMAL--ELYQG-TLIFVSH 493
Cdd:PRK11160 473 ---GRQ-------------LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET-ERQILELlaEHAQNkTVLMITH 532
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
320-508 |
1.20e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-------KWSENAR-IGYYAqdH 391
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRfMAYLG--H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 EYEFENDLTVFEWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKpakvLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:PRK13543 90 LPGLKADLSTLENLHflcglHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1352184330 467 NHLDMESIESLNMALELY---QGTLIFVSHDREFVSSLATRILEI 508
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-473 |
1.31e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTL----VGDLQPDS------GTVKWS---------E 380
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsgliTGDKSAGShiellgRTVQREgrlardirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 NARIGYYAQdhEYEFENDLTVFE------------WMS--QWKQEGDDEQAVRSI--LGRLLFSQDDIkkpaKVLSGGEK 444
Cdd:PRK09984 85 RANTGYIFQ--QFNLVNRLSVLEnvligalgstpfWRTcfSWFTREQKQRALQALtrVGMVHFAHQRV----STLSGGQQ 158
|
170 180
....*....|....*....|....*....
gi 1352184330 445 GRMLFGKLMMQKPNILIMDEPTNHLDMES 473
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
1.40e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.39 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltalpPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVLDTVIMG-HKELwevkqerdriyalpEMSEEDGYKVADLEVKYGeMDGYsaEARAGELLLGvgipveqhy 150
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlRPGL--------------KLTAEQRAQVEQALERVG-LAGL--LDRLPGQLSG--------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 151 gpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHD 211
Cdd:COG3840 133 --------GQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-527 |
1.41e-11 |
|
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: 65.90 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 338 LNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----WSENA----------RIGYYAQD-----Heyefen 397
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRkgiflppekrRIGYVFQEarlfpH------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 dLTVFEWM--SQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES-- 473
Cdd:TIGR02142 90 -LSVRGNLryGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRky 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 474 -----IESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVIDFsGNYEDYLRSK 527
Cdd:TIGR02142 169 eilpyLERLHAEFGI---PILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWASP 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-520 |
1.44e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAqDHEYEFEND 398
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 -----LTVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDI----KKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:PRK11248 80 gllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLegaeKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 470 DMESIESLN-MALELYQGT---LIFVSHDREFVSSLATRILEITP------ERV-IDFSGNY 520
Cdd:PRK11248 160 DAFTREQMQtLLLKLWQETgkqVLLITHDIEEAVFMATELVLLSPgpgrvvERLpLNFARRF 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-471 |
1.87e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNER------------IGKLRQDQ 73
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaaqlgIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 FAFEEFTVLDTVIMGH---KELWevkqerdriyalpemseedGYKVADlevkYGEMdgysaEARAGELLLGVGIPVEQHY 150
Cdd:PRK09700 90 SVIDELTVLENLYIGRhltKKVC-------------------GVNIID----WREM-----RVRAAMMLLRVGLKVDLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 151 gPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMII-ISHDRHFLNMVC---THMAD 224
Cdd:PRK09700 142 -KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQlrKEGTAIVyISHKLAEIRRICdryTVMKD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 225 LDYgelrVYPGNYDEymtAATQARERLLADNakkkaqiaELQsfvSRFSANasksRQATSRARQidkikleevkassrqn 304
Cdd:PRK09700 221 GSS----VCSGMVSD---VSNDDIVRLMVGR--------ELQ---NRFNAM----KENVSNLAH---------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 305 pfirfeqdKKLFrnalEVEGLTkGFDNGPLfKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG--------------DLQ 370
Cdd:PRK09700 263 --------ETVF----EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDIS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 371 PDS-------GTVKWSENAR-IGYYaqdHEYEFENDLTVFEWM--SQWK------QEGDDEQAVRSILGRLLFSQDDIKK 434
Cdd:PRK09700 329 PRSpldavkkGMAYITESRRdNGFF---PNFSIAQNMAISRSLkdGGYKgamglfHEVDEQRTAENQRELLALKCHSVNQ 405
|
490 500 510
....*....|....*....|....*....|....*..
gi 1352184330 435 PAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM 471
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-471 |
1.92e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.88 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSenARIGYYAQdheyefendltvFEW-MSQWKQE 411
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--GRISFSSQ------------FSWiMPGTIKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 412 G------DDEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM 471
Cdd:cd03291 117 NiifgvsYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-209 |
2.27e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIgklrqDQFAFEEFT 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-----DPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 VLdtvimGHKElwevkqerdriyAL-PEMSeedgykVAD-LEV---KYGEMDGYSAEAragelLLGVGIPVEQH--YGPM 153
Cdd:PRK13539 77 YL-----GHRN------------AMkPALT------VAEnLEFwaaFLGGEELDIAAA-----LEAVGLAPLAHlpFGYL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 154 SEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDST--MIIIS 209
Cdd:PRK13539 129 SA---GQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQggIVIAA 183
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-210 |
2.40e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL--------DPNERIGKLRQD-----QFA----FEEfTV 81
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagKKNKKLKPLRKKvgivfQFPehqlFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTVIMGHKELwevkqerdriyalpEMSEEDgykvadlevkygemdgysAEARAGELLLGVGIPVE-QHYGPMsEVAPGW 160
Cdd:PRK13634 104 EKDICFGPMNF--------------GVSEED------------------AKQKAREMIELVGLPEElLARSPF-ELSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISH 210
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-218 |
2.87e-11 |
|
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: 65.92 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER---IGKLRQDQFAFEeft 80
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwdREELgrhIGYLPQDVELFD--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 vlDTVimghkelwevkqeRDRIYALPEMSEEDGYKVADLevkygemdgysaeARAGELLL----GVGIPVEQHYGPMSev 156
Cdd:COG4618 420 --GTI-------------AENIARFGDADPEKVVAAAKL-------------AGVHEMILrlpdGYDTRIGEGGARLS-- 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 157 aPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLNMV 218
Cdd:COG4618 470 -GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalkARGATVVVITHRPSLLAAV 533
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-506 |
2.88e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGtvkwsenaRIGYYAQDH-------- 391
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG--------RIMLDGQDIthvpaenr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 -------EYEFENDLTVFEWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:PRK09452 87 hvntvfqSYALFPHMTVFENVAfglrmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ-LSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 460 LIMDEPTNHLDMESieSLNMALELYQ-----G-TLIFVSHDREFVSSLATRIL 506
Cdd:PRK09452 166 LLLDESLSALDYKL--RKQMQNELKAlqrklGiTFVFVTHDQEEALTMSDRIV 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-471 |
3.37e-11 |
|
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: 66.09 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSenARIGYYAQdheyefendltvFEWMSQWKQEG 412
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--GRISFSPQ------------TSWIMPGTIKD 505
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 413 D-------DEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM 471
Cdd:TIGR01271 506 NiifglsyDEYRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-210 |
3.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 17 FENISVKFGG-------------GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERigklrqdQFAFEEFTVLD 83
Cdd:PRK11288 7 FDGIGKTFPGvkalddisfdcraGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-------RFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 TVIMGHKELWEVkqerdriyalPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQHyGPMSEVAPGWKLR 163
Cdd:PRK11288 80 GVAIIYQELHLV----------PEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPD-TPLKYLSIGQRQM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE-RDSTMIII--SH 210
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILyvSH 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
3.85e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 65.45 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQDQfafeeft 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfGKHIGYLPQDV------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 vldtvimghkELWE--VKQERDRIYALPEmSEE--DGYKVADL-EVKYGEMDGY-SAEARAGELLLGvgipveqhygpms 154
Cdd:TIGR01842 402 ----------ELFPgtVAENIARFGENAD-PEKiiEAAKLAGVhELILRLPDGYdTVIGPGGATLSG------------- 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 155 evapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRHFLNMV 218
Cdd:TIGR01842 458 ----GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlkaRGITVVVITHRPSLLGCV 520
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-508 |
4.09e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.91 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPL----FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS---------------E 380
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 NARIGYYAQDHeyEFENDLTVFEWMSQ-----WKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:PRK11629 86 NQKLGFIYQFH--HLLPDFTALENVAMplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 456 KPNILIMDEPTNHLDM---ESIESLNMALELYQGT-LIFVSHDREFVSSLaTRILEI 508
Cdd:PRK11629 163 NPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRM-SRQLEM 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
352-511 |
4.56e-11 |
|
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: 62.24 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 352 GTNGVGKSTLLK----TLVGDLQPDSGTVKWS-----ENARIGYYaqdhEYEFENDltvfewmsqwkqEGDDEQAVRS-- 420
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPNSKGGAHDpklirEGEVRAQV----KLAFENA------------NGKKYTITRSla 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 421 ILGRLLF-SQDDIKKPA----KVLSGGEKgrMLFG--------KLMMQKPNILIMDEPTNHLDMESIE-SLNMALELYQG 486
Cdd:cd03240 93 ILENVIFcHQGESNWPLldmrGRCSGGEK--VLASliirlalaETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKS 170
|
170 180
....*....|....*....|....*....
gi 1352184330 487 TLIF----VSHDREFVsSLATRILEITPE 511
Cdd:cd03240 171 QKNFqlivITHDEELV-DAADHIYRVEKD 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
318-504 |
4.71e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENARIG 385
Cdd:PRK10584 5 NIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEYEFE--------NDLTVFEWMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:PRK10584 85 LRAKHVGFVFQsfmliptlNALENVELPALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 456 KPNILIMDEPTNHLDMESIE-------SLNMAlelYQGTLIFVSHDrefvSSLATR 504
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDkiadllfSLNRE---HGTTLILVTHD----LQLAAR 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-506 |
4.93e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLF---------KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS-------ENAR 383
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYEFENDLTVFewmsqwkqegDDEQAVRSILG---RLLFSQDDIKKPAKV--------------------LS 440
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAV----------NPRKTVREIIReplRHLLSLDKAERLARAsemlravdlddsvldkrppqLS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 441 GGEKGRMLFGKLMMQKPNILIMDEPTNHLDM---ESIESLNMALELYQGT-LIFVSHDREFVSSLATRIL 506
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVM 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
324-505 |
5.55e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 324 GLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG-------DLQPDSGTVKWSENAR--IGYYAQdhEYE 394
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDLFIGEKRMNDVPPAErgVGMVFQ--SYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 FENDLTVFEWMS-------QWKQEGDD--EQAVRSI-LGRLLfsqddIKKPaKVLSGGEKGRMLFGKLMMQKPNILIMDE 464
Cdd:PRK11000 86 LYPHLSVAENMSfglklagAKKEEINQrvNQVAEVLqLAHLL-----DRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1352184330 465 PTNHLD------MES-IESLNMALelyQGTLIFVSHDREFVSSLATRI 505
Cdd:PRK11000 160 PLSNLDaalrvqMRIeISRLHKRL---GRTMIYVTHDQVEAMTLADKI 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-514 |
5.68e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.25 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENARIGYYAQDHEYE--- 394
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 -----FEN-----DLTVFEWMSQWKQEGDD--EQAVRS-ILGRL----LFSQDDIkKPAKvLSGGEKGRMLFGKLMMQKP 457
Cdd:PRK11831 85 rmsmlFQSgalftDMNVFDNVAYPLREHTQlpAPLLHStVMMKLeavgLRGAAKL-MPSE-LSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 458 NILIMDEP-------TNHLDMESIESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK11831 163 DLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
6.22e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.94 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 17 FENISVKFGGGNR-----------------YGLIGANGSGKSTFMKILGGdLE-PTLGNV--------SLDPNERIgKLR 70
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINL-LErPTSGSVlvdgvdltALSERELR-AAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 QD------QFA-FEEFTVLDTVimghkelwevkqerdriyALPemseedgykvadLEVkygemDGYSA---EARAGELLL 140
Cdd:COG1135 82 RKigmifqHFNlLSSRTVAENV------------------ALP------------LEI-----AGVPKaeiRKRVAELLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 141 GVGIPVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRwleQVL------NER-DSTMIIISHDRH 213
Cdd:COG1135 127 LVGLSDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR---SILdllkdiNRElGLTIVLITHEMD 202
|
250
....*....|....*..
gi 1352184330 214 FLNMVCTHMADLDYGEL 230
Cdd:COG1135 203 VVRRICDRVAVLENGRI 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-529 |
6.36e-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: 62.63 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 330 DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-----------SENARIGYYAQDhEYEFeND 398
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaSLRRQIGLVSQD-VFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 lTVFEWMSQWKQEGDDEQAVRSilGRLLFSQDDIKK-PAKV----------LSGGEKGRMLFGKLMMQKPNILIMDEPTN 467
Cdd:cd03251 91 -TVAENIAYGRPGATREEVEEA--ARAANAHEFIMElPEGYdtvigergvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 468 HLDMESIESLNMALE-LYQG-TLIFVSHDREFVSSlATRILEITPERVIDfSGNYEDYLRSKGI 529
Cdd:cd03251 168 ALDTESERLVQAALErLMKNrTTFVIAHRLSTIEN-ADRIVVLEDGKIVE-RGTHEELLAQGGV 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-515 |
8.02e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA---------------- 382
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 -RIGYYAQdhEYEFENDLTVFEWMSQ--WKQEG-DDEQAV---RSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:PRK11124 82 rNVGMVFQ--QYNLWPHLTVQQNLIEapCRVLGlSKDQALaraEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 456 KPNILIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLATRILEITPERVID 515
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEiTAQIVSIIRELAETgiTQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-211 |
8.57e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdQFAFEEFTVldtvimghkel 92
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----------GMVLSEETV----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 93 WEVKQERDRIYALPEmSEEDGYKVADlEVKYG-EMDGYSAE---ARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQ 168
Cdd:PRK13635 77 WDVRRQVGMVFQNPD-NQFVGATVQD-DVAFGlENIGVPREemvERVDQALRQVGMEDFLNREP-HRLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 169 ALFADPDILLLDEPTNNLD-------IDTIRWLEQvlnERDSTMIIISHD 211
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHD 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-529 |
1.21e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 61.48 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW-----------SENARIGYY 387
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDheyefendlTV-FewmsqwkqegDDeqavrSIL-----GRLLFSQDDIKKPAKV----------------------- 438
Cdd:cd03253 81 PQD---------TVlF----------ND-----TIGyniryGRPDATDEEVIEAAKAaqihdkimrfpdgydtivgergl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 439 -LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD----MESIESLNmalELYQG-TLIFVSHDREFVSSlATRILEITPER 512
Cdd:cd03253 137 kLSGGEKQRVAIARAILKNPPILLLDEATSALDthteREIQAALR---DVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
250
....*....|....*..
gi 1352184330 513 VIDfSGNYEDYLRSKGI 529
Cdd:cd03253 213 IVE-RGTHEELLAKGGL 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-211 |
1.23e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 61.48 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFA 75
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTVIMGhkelwevkqerdriyalpemseedgykvadLEVKygEMDGYSAEARAGELLLGVGIPVEQHYGPmSE 155
Cdd:cd03300 84 FPHLTVFENIAFG------------------------------LRLK--KLPKAEIKERVAEALDLVQLEGYANRKP-SQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 156 VAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHD 211
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-216 |
1.28e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSkplF---ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL-----DPNE-----RIGKLRQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDiatrrRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 qfAF---EEFTvldtvimghkelweVKQERD---RIYALPEmsEEDGYKVADLEVKYGEMDgySAEARAGELLLGVgipv 146
Cdd:NF033858 347 --AFslyGELT--------------VRQNLElhaRLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSLPLGI---- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 eqhygpmsevapgwKLRVLLAQALFADPDILLLDEPTNNLD-----------IDtirwleqvLNERDSTMIIIShdRHFL 215
Cdd:NF033858 403 --------------RQRLSLAVAVIHKPELLILDEPTSGVDpvardmfwrllIE--------LSREDGVTIFIS--THFM 458
|
.
gi 1352184330 216 N 216
Cdd:NF033858 459 N 459
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.39e-10 |
|
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: 60.62 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNVSLDpNERIGKLRQDqfafeef 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK-GEDITDLPPE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 tvldtvimghkelwevkqERDR--IYALPEMSEE-DGYKVADL--EVKYGemdgYSAearaGElllgvgipveqhygpms 154
Cdd:cd03217 73 ------------------ERARlgIFLAFQYPPEiPGVKNADFlrYVNEG----FSG----GE----------------- 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 155 evapgwKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLNMV 218
Cdd:cd03217 110 ------KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINklrEEGKSVLIITHYQRLLDYI 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-506 |
1.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNG---PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-----------KWSENAR 383
Cdd:PRK13650 3 NIIEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYEF-----ENDLTvFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:PRK13650 83 IGMVFQNPDNQFvgatvEDDVA-FGLENKGIPHEEMKERVNEALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 459 ILIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVsSLATRIL 506
Cdd:PRK13650 161 IIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
1.80e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.95 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 32 LIGANGSGKSTFMKILGGDLEPTLGNVSL--------DPNERiGKLRQDQ--FAFEEFTVLDTVimghKELWEVKqerdr 101
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEAR-AKLRAKHvgFVFQSFMLIPTL----NALENVE----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 102 iyaLPEMSEedgykvadlevkyGEMDGYSAEaRAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDE 181
Cdd:PRK10584 111 ---LPALLR-------------GESSRQSRN-GAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 1352184330 182 PTNNLDIDT---IRWLEQVLN-ERDSTMIIISHD 211
Cdd:PRK10584 173 PTGNLDRQTgdkIADLLFSLNrEHGTTLILVTHD 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
320-523 |
1.95e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENAR----------IGYYAQ 389
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpakahqLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHEYEFENDLTVFE-WMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNH 468
Cdd:PRK15439 92 PQEPLLFPNLSVKEnILFGLPKRQASMQKMKQLL-AALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 469 LDMESIESL----NMALELYQGtLIFVSHDREFVSSLATRIlEITPERVIDFSGNYEDY 523
Cdd:PRK15439 171 LTPAETERLfsriRELLAQGVG-IVFISHKLPEIRQLADRI-SVMRDGTIALSGKTADL 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-480 |
2.27e-10 |
|
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: 60.35 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 327 KGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPD---SGTVKWS-----ENARigYYAQDHEYEFEND 398
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgipykEFAE--KYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 -----LTVFEWMS-QWKQEGDdeQAVRSIlgrllfsqddikkpakvlSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDme 472
Cdd:cd03233 93 vhfptLTVRETLDfALRCKGN--EFVRGI------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD-- 150
|
....*...
gi 1352184330 473 SIESLNMA 480
Cdd:cd03233 151 SSTALEIL 158
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-235 |
2.93e-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: 60.36 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 3 VSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEP---TLGNVSLDPNER--------IGKLRQ 71
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRkpdqfqkcVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVLDTVI------MGHKELWEVKQERDRIYALPEmseedgykVADLEVkygemdgysaearAGELLLGVGIp 145
Cdd:cd03234 89 DDILLPGLTVRETLTytailrLPRKSSDAIRKKRVEDVLLRD--------LALTRI-------------GGNLVKGISG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 146 veqhygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQvLNERDSTMIIISHD------RHFl 215
Cdd:cd03234 147 -------------GERRRVSIAVQLLWDPKVLILDEPTSGLDsftaLNLVSTLSQ-LARRNRIVILTIHQprsdlfRLF- 211
|
250 260
....*....|....*....|
gi 1352184330 216 nmvcTHMADLDYGELrVYPG 235
Cdd:cd03234 212 ----DRILLLSSGEI-VYSG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-521 |
3.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 337 NLNLLLEVGEKLAVLGTNGVGKSTLLK------------TLVGDLQPDSGTVKWSENAR----IGYYAQDHEYEFENDLT 400
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVKRlrkeIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 VFEWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIES 476
Cdd:PRK13645 109 EKDIAFGPVNLGENKQEAYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1352184330 477 -LNMALEL---YQGTLIFVSHDREFVSSLATRILEITPERVIDFSGNYE 521
Cdd:PRK13645 189 fINLFERLnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-210 |
3.18e-10 |
|
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: 60.32 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKLRQDQ 73
Cdd:cd03254 7 NVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 74 FAFEEfTVLDTVIMGHKElwevKQERDRIYALPEMSeedgykvADLEVKYGEmDGYSAEAR-AGELLlgvgipveqhygp 152
Cdd:cd03254 87 FLFSG-TIMENIRLGRPN----ATDEEVIEAAKEAG-------AHDFIMKLP-NGYDTVLGeNGGNL------------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 153 mSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTirwlEQVLNE------RDSTMIIISH 210
Cdd:cd03254 141 -SQ---GERQLLAIARAMLRDPKILILDEATSNIDTET----EKLIQEaleklmKGRTSIIIAH 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
320-513 |
3.23e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLfkNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENarigyyaQDHEYE----- 394
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG-------QDHTTTppsrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 -----F-ENDLtvFEWMSQW-----------KQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGK-LMMQK 456
Cdd:PRK10771 72 pvsmlFqENNL--FSHLTVAqniglglnpglKLNAAQREKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARcLVREQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 457 PnILIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVSSLATRILEITPERV 513
Cdd:PRK10771 149 P-ILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-515 |
3.29e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGF-----DNGP------LF----------KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVk 377
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLkgalkgLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 wsenaRI-GYYAQDHEYEFENDLT-VFEWMSQ--WkqegD----------------DEQAVRSILGRL--LFSQDDI-KK 434
Cdd:COG4586 80 -----RVlGYVPFKRRKEFARRIGvVFGQRSQlwW----DlpaidsfrllkaiyriPDAEYKKRLDELveLLDLGELlDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 435 PAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES-------IESLNmalELYQGTLIFVSHDREFVSSLATRILe 507
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeairefLKEYN---RERGTTILLTSHDMDDIEALCDRVI- 226
|
....*...
gi 1352184330 508 itperVID 515
Cdd:COG4586 227 -----VID 229
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
320-465 |
3.75e-10 |
|
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: 60.37 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS----------ENAR--IGYY 387
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmhERARlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEYeF------ENDLTVFEwmsqwKQEGDDEQAVRSILGRLL--FSQDDIKK-PAKVLSGGEKGRMLFGKLMMQKPN 458
Cdd:TIGR04406 82 PQEASI-FrkltveENIMAVLE-----IRKDLDRAEREERLEALLeeFQISHLRDnKAMSLSGGERRRVEIARALATNPK 155
|
....*..
gi 1352184330 459 ILIMDEP 465
Cdd:TIGR04406 156 FILLDEP 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-508 |
3.98e-10 |
|
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: 62.15 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG-------------DLEPTLGNVSLDPNER-I 66
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 67 GKLRQDQFAFEEFTVLDTVIMGHkelwevkqerdriyalpemseedgykvaDLEVKYGEMDGYSAEARAGELLLGVGIPV 146
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGN----------------------------EITLPGGRMAYNAMYLRAKNLLRELQLDA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EQHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQvlneRDSTMIIISHDRHFLNMVC 219
Cdd:TIGR02633 133 DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTeketeilLDIIRDLKA----HGVACVYISHKLNEVKAVC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 220 THMADLDYGElrvypgnydeymTAATQARERLLADNAKKKAQIAELQSFVSrfsanasksrqatsraRQIDKIKlEEVka 299
Cdd:TIGR02633 209 DTICVIRDGQ------------HVATKDMSTMSEDDIITMMVGREITSLYP----------------HEPHEIG-DVI-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 300 ssrqnpfirfeqdkklfrnaLEVEGLTKGFDNGPLFK---NLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDL------- 369
Cdd:TIGR02633 258 --------------------LEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgkfegn 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 370 ------QPDSGTVKWSENARIGYYAQDHEYE-FENDLTV-----------FEWMSQWKQEGdDEQAVRSILGRLLFSQDD 431
Cdd:TIGR02633 318 vfingkPVDIRNPAQAIRAGIAMVPEDRKRHgIVPILGVgknitlsvlksFCFKMRIDAAA-ELQIIGSAIQRLKVKTAS 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 432 IKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES---IESLNMALELYQGTLIFVSHDREFVSSLATRILEI 508
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-505 |
4.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE---------------NARIGYYAQDHEYEFENDLT 400
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 401 VFEWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES--- 473
Cdd:PRK13646 104 EREIIFGPKNFKMNLDEVKNYAHRLLmdlgFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrq 183
|
170 180 190
....*....|....*....|....*....|...
gi 1352184330 474 IESLNMALELYQG-TLIFVSHDREFVSSLATRI 505
Cdd:PRK13646 184 VMRLLKSLQTDENkTIILVSHDMNEVARYADEV 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-506 |
4.43e-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: 58.98 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTkgfdNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------------SENARI 384
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 385 GYYAQDHeyefendltvfewmsqwKQEG-DDEQAVRS--ILGRLLfsqddikkpakvlSGGEKGRMLFGKLMMQKPNILI 461
Cdd:cd03215 78 AYVPEDR-----------------KREGlVLDLSVAEniALSSLL-------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 462 MDEPTNHLDMESIEslnmalELYQ---------GTLIFVSHDREFVSSLATRIL 506
Cdd:cd03215 128 LDEPTRGVDVGAKA------EIYRlireladagKAVLLISSELDELLGLCDRIL 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-389 |
4.90e-10 |
|
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: 59.41 E-value: 4.90e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWseNARIGYYAQ 389
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQ 73
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-506 |
4.95e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.01 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLF--ENISVKFGGGNRY-----------------GLIGANGSGKS-TFMKILG----GDLEPTlGNVSLD------- 61
Cdd:COG4172 3 SMPLLsvEDLSVAFGQGGGTveavkgvsfdiaagetlALVGESGSGKSvTALSILRllpdPAAHPS-GSILFDgqdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 62 PNERIGKLRQDQFA--FEE--------FTVldtvimgHKELWEVkqerdriyalpemseedgykvadLEVKYGeMDGYSA 131
Cdd:COG4172 82 SERELRRIRGNRIAmiFQEpmtslnplHTI-------GKQIAEV-----------------------LRLHRG-LSGAAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 132 EARAGELLLGVGIP-VEQHYG--PmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIdTIRwlEQVLN-------ER 201
Cdd:COG4172 131 RARALELLERVGIPdPERRLDayP-HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQ--AQILDllkdlqrEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 202 DSTMIIISHDrhfLNMVcTHMADldygelRVYpgnydeYMtaatqarerlladnakKKAQIAElQSFVSRFSANAsksRQ 281
Cdd:COG4172 207 GMALLLITHD---LGVV-RRFAD------RVA------VM----------------RQGEIVE-QGPTAELFAAP---QH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 282 ATSRarqidkiKLeeVKASSRQNPFIRFEQDKKLfrnaLEVEGLTKGFD-NGPLF----------KNLNLLLEVGEKLAV 350
Cdd:COG4172 251 PYTR-------KL--LAAEPRGDPRPVPPDAPPL----LEARDLKVWFPiKRGLFrrtvghvkavDGVSLTLRRGETLGL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 351 LGTNGVGKSTLLKTLVGdLQPDSGTV--------KWSENARIGYYA------QDHEYEFENDLTVFEWMSqwkqEG---- 412
Cdd:COG4172 318 VGESGSGKSTLGLALLR-LIPSEGEIrfdgqdldGLSRRALRPLRRrmqvvfQDPFGSLSPRMTVGQIIA----EGlrvh 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 413 -------DDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALEL 483
Cdd:COG4172 393 gpglsaaERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVQAqiLDLLRDL 471
|
570 580
....*....|....*....|....*.
gi 1352184330 484 ---YQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG4172 472 qreHGLAYLFISHDLAVVRALAHRVM 497
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-242 |
5.34e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.05 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFafeeftvldtvimgHKEL 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVQYDHHYL--------------HRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 93 WEVKQE--------RDRI-YALPEMSEEDGYKVADLEvkygemdgySAEARAGELLLGVGIPVEQHYGPMSevaPGWKLR 163
Cdd:TIGR00958 558 ALVGQEpvlfsgsvRENIaYGLTDTPDEEIMAAAKAA---------NAHDFIMEFPNGYDTEVGEKGSQLS---GGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHDRHFLNMvCTHMADLDYGELrVYPGNYDEYMT 242
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGTHKQLME 702
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-210 |
5.73e-10 |
|
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: 59.43 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL--------DPNER-IGKLRQDQFA 75
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaaPPADRpVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 76 FEEFTVLDTVIMGHK---ELWEVKQERdriyalpemseedgykvadLEVKYGEMDGYSAEARAGELLLGvgipveqhygp 152
Cdd:cd03298 82 FAHLTVEQNVGLGLSpglKLTAEDRQA-------------------IEVALARVGLAGLEKRLPGELSG----------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 153 msevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN----ERDSTMIIISH 210
Cdd:cd03298 132 ------GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlhaETKMTVLMVTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-212 |
6.96e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.00 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFAF 76
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvpPYQRpINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 EEFTVLDTVIMGhkelweVKQERdriyaLPEmseedgykvadlevkyGEMdgysaEARAGELLLGVGIPVEQHYGPmSEV 156
Cdd:PRK11607 104 PHMTVEQNIAFG------LKQDK-----LPK----------------AEI-----ASRVNEMLGLVHMQEFAKRKP-HQL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD--------IDTIRWLEQVlnerDSTMIIISHDR 212
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQ 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-521 |
7.39e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG-PL----FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA------------ 382
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 -----------------------RIGYYAQDHEYEF-----ENDLtVFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKK 434
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrRVGVVFQFAEYQLfeqtiEKDI-IFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 435 PAKVLSGGEKGRM-LFGKLMMQkPNILIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLATRILEITP 510
Cdd:PRK13651 162 SPFELSGGQKRRVaLAGILAME-PDFLVFDEPTAGLDPQgVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|.
gi 1352184330 511 ERVIDFSGNYE 521
Cdd:PRK13651 241 GKIIKDGDTYD 251
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
319-506 |
9.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.62 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG--PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------SENAR-----IG 385
Cdd:PRK13632 7 MIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitisKENLKeirkkIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEYEF-------------ENDLTVFEWMSQWKQEGDDEQAVRSILgrllfsqddiKKPAKVLSGGEKGRMLFGKL 452
Cdd:PRK13632 87 IIFQNPDNQFigatveddiafglENKKVPPKKMKDIIDDLAKKVGMEDYL----------DKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 453 MMQKPNILIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVsSLATRIL 506
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-506 |
9.76e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNER------------IGKLRQDQFAFEEFTVLDTVIMGHkelwEVKQE 98
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeagIGIIHQELNLIPQLTIAENIFLGR----EFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 99 RDRIyALPEMSEEDGYKVADLEVKYgemdgySAEARAGELLLGvgipvEQHygpMSEVApgwklrvllaQALFADPDILL 178
Cdd:PRK10762 110 FGRI-DWKKMYAEADKLLARLNLRF------SSDKLVGELSIG-----EQQ---MVEIA----------KVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 179 LDEPTNNL-DIDTiRWLEQVLNE-RDSTMII--ISHDRHFLNMVCTHMADLDYGELrvypgnYDEYMTAATQaRERLLad 254
Cdd:PRK10762 165 MDEPTDALtDTET-ESLFRVIRElKSQGRGIvyISHRLKEIFEICDDVTVFRDGQF------IAEREVADLT-EDSLI-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 255 nakkkaqiaelQSFVSRfsanasksrqatsrarqidkiKLEEvkassrQNPfiRFEQDKKLFRnaLEVEGLTkgfdnGPL 334
Cdd:PRK10762 235 -----------EMMVGR---------------------KLED------QYP--RLDKAPGEVR--LKVDNLS-----GPG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 335 FKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE------------NARIGYYAQDHEYE-------- 394
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGIVYISEDRKRDglvlgmsv 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 FEN-DLTVFEWMSQWK---QEGDDEQAVRSILGrlLFsqdDIKKPAK-----VLSGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:PRK10762 348 KENmSLTALRYFSRAGgslKHADEQQAVSDFIR--LF---NIKTPSMeqaigLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1352184330 466 TNHLDMESIEslnmalELYQ--------G-TLIFVSHDREFVSSLATRIL 506
Cdd:PRK10762 423 TRGVDVGAKK------EIYQlinqfkaeGlSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
320-495 |
9.89e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS----ENARIGYYAQ----DH 391
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsiKKDLCTYQKQlcfvGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 392 EYEFENDLTV-----FEWMSQWKQEGDDEqavrsiLGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:PRK13540 82 RSGINPYLTLrenclYDIHFSPGAVGITE------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 1352184330 467 NHLDMESIESLNMALELYQ---GTLIFVSHDR 495
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
1.01e-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: 57.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--PNERIGKLRQDQFAFe 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDgvPVSDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 78 eftvldtvimghkelweVKQerdRIYALpemseedgykvadlevkygemdgysaearAGELLLGVGIPveqhygpmseVA 157
Cdd:cd03247 80 -----------------LNQ---RPYLF-----------------------------DTTLRNNLGRR----------FS 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITH 155
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
330-514 |
1.13e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 330 DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-----------KWSENARI-GYYAQDHEYEF-- 395
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLvGIVFQNPETQFvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ---ENDLTvFEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDME 472
Cdd:PRK13644 93 rtvEEDLA-FGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 473 SIES-LNMALELYQ--GTLIFVSH--------DREFVSSLATRILEITPERVI 514
Cdd:PRK13644 171 SGIAvLERIKKLHEkgKTIVYITHnleelhdaDRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-210 |
1.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.29 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 9 MQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdqfafeEFTVLDTVImg 88
Cdd:PRK13637 16 TPFEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID----------------GVDITDKKV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 89 hkELWEVKQERDRIYALPE--MSEEDGYKvadlEVKYGEMD-GYSAEA---RAGELLLGVGIPVEQhYGPMS--EVAPGW 160
Cdd:PRK13637 77 --KLSDIRKKVGLVFQYPEyqLFEETIEK----DIAFGPINlGLSEEEienRVKRAMNIVGLDYED-YKDKSpfELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDI---DTIrwLEQVLN---ERDSTMIIISH 210
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEI--LNKIKElhkEYNMTIILVSH 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
1.23e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV-----SLDPNER-IGKLRQdqf 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRgLLALRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 afeeftvldtvimghkELWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMdgysaEARAGELLLGVGipvEQHY--GP 152
Cdd:PRK13638 78 ----------------QVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEI-----TRRVDEALTLVD---AQHFrhQP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 153 MSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQVLNErdstMIIISHDRHFLNMVCTHMADL 225
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVL 209
|
250
....*....|..
gi 1352184330 226 DYGELRVY--PG 235
Cdd:PRK13638 210 RQGQILTHgaPG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-493 |
1.28e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------------KWSENARIGYY 387
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQdhEYEFENDLTVFEWM---------------SQWKQEgddEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKL 452
Cdd:PRK09700 86 YQ--ELSVIDELTVLENLyigrhltkkvcgvniIDWREM---RVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 453 MMQKPNILIMDEPTNHLDMESIESLNMALELYQG---TLIFVSH 493
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-514 |
1.35e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkwsenariGYYAQDHEYEfenDL 399
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLR---DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVF-----------EW-------------------------MSQ-WKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGG 442
Cdd:PRK11701 76 YALseaerrrllrtEWgfvhqhprdglrmqvsaggnigerlMAVgARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 443 EKGRMLFGKLMMQKPNILIMDEPTNHLD-------MESIESLNMALELyqgTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGLVRELGL---AVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-501 |
1.36e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLDI-------DTIRWLEQVLNerdSTMIIISHDrhfLNMVcthmadldygelr 231
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilQLLRELQQELN---MGLLFITHN---LSIV------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 232 vypgnydeymtaatqareRLLADNAK--KKAQIAELQSFVSRFSANASKSRQATSRARQIDkiklEEVKASSRQNPFIRF 309
Cdd:PRK15134 221 ------------------RKLADRVAvmQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSG----DPVPLPEPASPLLDV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 310 EQDKKLF--RNALevegLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKST----LLKTLVG------DLQPdsgTVK 377
Cdd:PRK15134 279 EQLQVAFpiRKGI----LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeiwfDGQP---LHN 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 WSENA------RIGYYAQDHEYEFENDLTVFEWMSQWKQ-------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEK 444
Cdd:PRK15134 352 LNRRQllpvrhRIQVVFQDPNSSLNPRLNVLQIIEEGLRvhqptlsAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQR 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 445 GRMLFGKLMMQKPNILIMDEPTNHLD---MESIESLNMAL-ELYQGTLIFVSHDREFVSSL 501
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqQKHQLAYLFISHDLHVVRAL 492
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-505 |
1.39e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQD--------- 390
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 -HEYEFENDLTVFE--WMSQWKQEG---DDEQAVRSILGRLLFSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:PRK11288 85 yQELHLVPEMTVAEnlYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1352184330 463 DEPTNHLDMESIESLnMAL--ELY-QGT-LIFVSHDREFVSSLATRI 505
Cdd:PRK11288 165 DEPTSSLSAREIEQL-FRVirELRaEGRvILYVSHRMEEIFALCDAI 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-211 |
1.50e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 7 VTMQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAF----EE---- 78
Cdd:PRK15056 14 VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqsEEvdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 79 FTVL--DTVIM---GHKELWEVKQERDRiyalpemseedgykvadlevkygemdgysaeARAGELLLGVGIpVEQHYGPM 153
Cdd:PRK15056 93 FPVLveDVVMMgryGHMGWLRRAKKRDR-------------------------------QIVTAALARVDM-VEFRHRQI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 154 SEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE-RDS--TMIIISHD 211
Cdd:PRK15056 141 GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEgkTMLVSTHN 201
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-513 |
1.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.95 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkwsenarigyYAQDHEYEFENDLtvfeWMSQWKQ----E 411
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----------YVDGLDTSDEENL----WDIRNKAgmvfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 412 GDDEQAVRSILGR--------LLFSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:PRK13633 93 NPDNQIVATIVEEdvafgpenLGIPPEEIRErvdeslkkvgmyeyrrhAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 467 NHLD-------MESIESLNmalELYQGTLIFVSH--------DREFVSSLATRILEITPERV 513
Cdd:PRK13633 173 AMLDpsgrrevVNTIKELN---KKYGITIILITHymeeaveaDRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-513 |
2.18e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 307 IRFEQDKKLF---RNALEvegltkgfdngplfkNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------- 376
Cdd:PRK10908 2 IRFEHVSKAYlggRQALQ---------------GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 377 ---KWSE----NARIGYYAQDHEYEFenDLTVFEWMS-----QWKQEGDDEQAVRSILGR--LLfsqDDIKKPAKVLSGG 442
Cdd:PRK10908 67 trlKNREvpflRRQIGMIFQDHHLLM--DRTVYDNVAipliiAGASGDDIRRRVSAALDKvgLL---DKAKNFPIQLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 443 EKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLATRILEITPERV 513
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
2.18e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnERIGKLRqDQFAFEEft 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR--MRDGQLR-DLYALSE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 vldtvimghkelwevkQERDRIyalpeMSEEDGYkvadleVKYGEMDGY----SAEARAGELLLGVGipvEQHYGPMSEV 156
Cdd:PRK11701 81 ----------------AERRRL-----LRTEWGF------VHQHPRDGLrmqvSAGGNIGERLMAVG---ARHYGDIRAT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 157 APGWKLRVLLAQA----------------------LFADPDILLLDEPTNNLDI-------DTIRWLeqvLNERDSTMII 207
Cdd:PRK11701 131 AGDWLERVEIDAAriddlpttfsggmqqrlqiarnLVTHPRLVFMDEPTGGLDVsvqarllDLLRGL---VRELGLAVVI 207
|
....
gi 1352184330 208 ISHD 211
Cdd:PRK11701 208 VTHD 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-210 |
2.44e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPTlGNVSldpneriGKLRQDQFAFEEFTVLDT- 84
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYE-------GEIIFEGEELQASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 85 ----VIMgHKELWEVkqerdriyalPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELL--LGVGIPVEQhygPMSEVAP 158
Cdd:PRK13549 81 ragiAII-HQELALV----------KELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqLKLDINPAT---PVGNLGL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNL---DIDTIRWLEQVLNERDSTMIIISH 210
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
320-519 |
2.98e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGP----LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLvGDL-QPDSGTVKWS-------ENARIGYY 387
Cdd:PRK10535 5 LELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLdKPTSGTYRVAgqdvatlDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDH------EYEFENDLTV---FEWMSQWKQEGDDEQAVRSI--LGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQK 456
Cdd:PRK10535 84 RREHfgfifqRYHLLSHLTAaqnVEVPAVYAGLERKQRLLRAQelLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 457 PNILIMDEPTNHLDMESIESLnMALeLYQ-----GTLIFVSHDREfVSSLATRILEITPERVIDFSGN 519
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEV-MAI-LHQlrdrgHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-231 |
3.45e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE---RIGKLRQDQFAFEEFTVLDTVIMGH 89
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 90 KELWevkqerdrIYA-LPEMSEEDGYKVADLEVKYgemdgysaearagellLGVGIPVEQHYGPMSEvapGWKLRVLLAQ 168
Cdd:TIGR01257 2031 EHLY--------LYArLRGVPAEEIEKVANWSIQS----------------LGLSLYADRLAGTYSG---GNKRKLSTAI 2083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 169 ALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVsiiREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
326-514 |
3.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.92 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 326 TKGFDNgplfknLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE---------------NARIGYYAQD 390
Cdd:PRK13641 20 KKGLDN------ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 391 HEYE-FENdlTVFE-WMSQWKQEGDDEQAVRSI----LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDE 464
Cdd:PRK13641 94 PEAQlFEN--TVLKdVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 465 PTNHLDMESIESLNMALELYQG---TLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
4.00e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPtlgnvSLDPNERIgklrqdqfafeeftVLDTVIMGHKELW 93
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-----DDNPNSKI--------------TVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 94 EVKQERDRIYALPEmSEEDGYKVADlEVKYGemdgysAEARA----------GELLLGVGIPVEQHYGPmSEVAPGWKLR 163
Cdd:PRK13640 81 DIREKVGIVFQNPD-NQFVGATVGD-DVAFG------LENRAvprpemikivRDVLADVGMLDYIDSEP-ANLSGGQKQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLD-------IDTIRwleQVLNERDSTMIIISHD 211
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDpagkeqiLKLIR---KLKKKNNLTVISITHD 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
310-470 |
4.75e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.91 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 310 EQDKKLFRNALEVEGLTKGfdngpLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPD---SGTVK-------WS 379
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKH-----LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLlngmpidAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 380 ENARIGYYAQDHEYeFENDLTVFE---WMSQWK---QEGDDE--QAVRSILGRL-LFSQDD--IKKPA--KVLSGGEKGR 446
Cdd:TIGR00955 96 EMRAISAYVQQDDL-FIPTLTVREhlmFQAHLRmprRVTKKEkrERVDEVLQALgLRKCANtrIGVPGrvKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 1352184330 447 MLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-508 |
4.83e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTL-------VGDLQPDSGTVKwsenariGYYAQDHE 392
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-------DPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 393 YEFENDLtVFEWMSQWKQ------------------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMM 454
Cdd:PRK09493 75 IRQEAGM-VFQQFYLFPHltalenvmfgplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 455 QKPNILIMDEPTNHLDME-SIESLNMALELYQG--TLIFVSHDREFVSSLATRILEI 508
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKVASRLIFI 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
4.91e-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: 56.49 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNER-IGKLRQDQFAF 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 EEFTVLDTVIMGHKELwevKQERDRIyalpemsEEDGYKVADLevkygemdgysaeARAGELLlgvgipveQHYgPmSEV 156
Cdd:cd03301 85 PHMTVYDNIAFGLKLR---KVPKDEI-------DERVREVAEL-------------LQIEHLL--------DRK-P-KQL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 157 APGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-528 |
6.09e-09 |
|
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: 56.73 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 330 DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-----------KWSENARIGYYAQdheyefEND 398
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGVVLQ------ENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 L---TVFEWMSQwkqeGDDEQAVRSIL--GRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:cd03252 87 LfnrSIRDNIAL----ADPGMSMERVIeaAKLAGAHDFISElpegydtivgeQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 463 DEPTNHLDMESIESL--NMALELYQGTLIFVSHDREFVSSlATRILEITPERVIDfSGNYEDYLRSKG 528
Cdd:cd03252 163 DEATSALDYESEHAImrNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAENG 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-505 |
7.40e-09 |
|
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: 54.69 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkwsenarigyyaqdheyeFENDLTVFEWMSqwkqegddeqavrsilgR 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------IYIDGEDILEEV-----------------L 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 425 LLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMALELYQG---------TLIFVSHDR 495
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTTNDE 126
|
170
....*....|
gi 1352184330 496 EFVSSLATRI 505
Cdd:smart00382 127 KDLGPALLRR 136
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-210 |
7.88e-09 |
|
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: 55.88 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQDQfafeeftvld 83
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTIIPQDP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 TVIMGhkelwEVKQERDRiyaLPEMSEEDGYKVadLEVKYGemdgysaearagelllgvGIPVEQhygpmsevapGWKLR 163
Cdd:cd03369 92 TLFSG-----TIRSNLDP---FDEYSDEEIYGA--LRVSEG------------------GLNLSQ----------GQRQL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAH 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-183 |
8.32e-09 |
|
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: 55.90 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnERIGKLRQDQFA-------------FEEFTVLDTVIMG--HKELWEV 95
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-RDITGLPPHERAragigyvpegrriFPELTVEENLLLGayARRRAKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 96 KQERDRIYAL-PEMSEEdgykvadlevkygemdgysAEARAGELLLGvgipvEQHygpMsevapgwklrVLLAQALFADP 174
Cdd:cd03224 109 KARLERVYELfPRLKER-------------------RKQLAGTLSGG-----EQQ---M----------LAIARALMSRP 151
|
....*....
gi 1352184330 175 DILLLDEPT 183
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-210 |
9.96e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 55.58 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--PNERIG--KLR-------QD 72
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvDISKIGlhDLRsrisiipQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEEfTV---LDtvIMGH---KELWEVKQE---RDRIYALPEMseedgykvADLEVKYGEmDGYSAearagelllgvg 143
Cdd:cd03244 87 PVLFSG-TIrsnLD--PFGEysdEELWQALERvglKEFVESLPGG--------LDTVVEEGG-ENLSV------------ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 144 ipveqhygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03244 143 ---------------GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-210 |
1.02e-08 |
|
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: 56.01 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKP---LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKL----RQDQFAF- 76
Cdd:cd03249 4 KNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLnlrwLRSQIGLv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 -EEFTVLDTVImghkelwevkqeRDRI-YALPEMSEEDGYKVADL----EVKYGEMDGYSAEaragelllgVGipveQHY 150
Cdd:cd03249 83 sQEPVLFDGTI------------AENIrYGKPDATDEEVEEAAKKanihDFIMSLPDGYDTL---------VG----ERG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 151 GPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03249 138 SQLSG---GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRamKGRTTIVIAH 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-470 |
1.13e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 338 LNLLLEVGEKLAVLGTNGVGKSTLLKTLVGdLQPDSGTV--------KWS--ENARI-GYYAQDHEYEFENDltVFEWMS 406
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleAWSaaELARHrAYLSQQQTPPFAMP--VFQYLT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 407 QWKQEGDDEQAVRSILGRL---LFSQDDIKKPAKVLSGGEKGRM-LFGKLMMQKPNI------LIMDEPTNHLD 470
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVaeaLGLDDKLGRSVNQLSGGEWQRVrLAAVVLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-470 |
1.44e-08 |
|
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: 55.35 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 334 LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPD---SGTV----------KWSEnaRIGYYAQD---HEYefen 397
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkpdQFQK--CVAYVRQDdilLPG---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 398 dLTVFEWM--------------SQWKQEGDDEQ----AVRSILGRLLfsqddikkpaKVLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03234 96 -LTVRETLtytailrlprkssdAIRKKRVEDVLlrdlALTRIGGNLV----------KGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|.
gi 1352184330 460 LIMDEPTNHLD 470
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
1.55e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF------GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnerigklrqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 afeeftvLDTVIMGHkeLWEVKQERDRIYALPE------MSEEDgykvadleVKYG-EMDGYSAE---ARAGELLLGVGI 144
Cdd:PRK13633 72 -------LDTSDEEN--LWDIRNKAGMVFQNPDnqivatIVEED--------VAFGpENLGIPPEeirERVDESLKKVGM 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 145 PVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRwleqVLNERDS-TMIIISH 210
Cdd:PRK13633 135 YEYRRHAP-HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIK----ELNKKYGiTIILITH 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-506 |
1.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA---------------RIGYYAQDHEYE-FENdl 399
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQlFEE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TV-----FEWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRM-LFGKLMMQkPNILIMDEPTNHLD--- 470
Cdd:PRK13634 102 TVekdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVaIAGVLAME-PEVLVLDEPTAGLDpkg 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1352184330 471 ----MESIESLNMALELyqgTLIFVSHDREFVSSLATRIL 506
Cdd:PRK13634 181 rkemMEMFYKLHKEKGL---TTVLVTHSMEDAARYADQIV 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
320-516 |
2.17e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 54.34 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGF--DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE-----------NARIGY 386
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHEY---EFENDLTVFEwmsqwkqEGDDEQavrsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:cd03369 87 IPQDPTLfsgTIRSNLDPFD-------EYSDEE---------IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 464 EPTNHLDMESIESLNMAL-ELYQG-TLIFVSHDREFVSSLAtRILEITPERVIDF 516
Cdd:cd03369 151 EATASIDYATDALIQKTIrEEFTNsTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-506 |
2.57e-08 |
|
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: 55.88 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 349 AVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----WSENA----------RIGYYAQD-----HeyefendLTVFE----- 403
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSArgiflpphrrRIGYVFQEarlfpH-------LSVRGnllyg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 404 -WMSQWKQEGDDEQAVRSILG--RLLfsqdDiKKPAKvLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES------- 473
Cdd:COG4148 102 rKRAPRAERRISFDEVVELLGigHLL----D-RRPAT-LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeilpy 175
|
170 180 190
....*....|....*....|....*....|...
gi 1352184330 474 IESLNMALELyqgTLIFVSHDREFVSSLATRIL 506
Cdd:COG4148 176 LERLRDELDI---PILYVSHSLDEVARLADHVV 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-230 |
2.68e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdPNERIgklrqdqfafeeftvldTVIMGHKELWEVKQ 97
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-AGYHI-----------------TPETGNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 98 ERDRIYALPE--MSEEDGYKvadlEVKYGEMD-GYS---AEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRVLLAQALF 171
Cdd:PRK13641 86 KVSLVFQFPEaqLFENTVLK----DVEFGPKNfGFSedeAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 172 ADPDILLLDEPTNNLDIDTIRWLEQVLNERDS---TMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
2.74e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLEPTL---GNVSLD------PNERIGKL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYNghniysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQD-QFAFEE-----FTVLDTVIMGHKelweVKQERDRiyALPEMSEEDGYKVADL--EVKYGEMDgySAEARAGelllg 141
Cdd:PRK14239 85 RKEiGMVFQQpnpfpMSIYENVVYGLR----LKGIKDK--QVLDEAVEKSLKGASIwdEVKDRLHD--SALGLSG----- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 142 vgipveqhygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:PRK14239 152 -----------------GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGlkDDYTMLLVTR 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
329-502 |
2.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 329 FDNGPLFkNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE---------------NARIGYYAQDHEY 393
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 394 EFENDLTVFEWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHL 469
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1352184330 470 DMES-IESLNMALELYQG--TLIFVSHDREFVSSLA 502
Cdd:PRK13643 176 DPKArIEMMQLFESIHQSgqTVVLVTHLMDDVADYA 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
4.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErigkLRQDQfafeeftvldtvimghKELWEVKQE 98
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP----IKYDK----------------KSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 99 --------RDRIYAlPEMSEEDGYKVADLEVKYGEMdgysaEARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQAL 170
Cdd:PRK13639 80 vgivfqnpDDQLFA-PTVEEDVAFGPLNLGLSKEEV-----EKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 171 FADPDILLLDEPTNNLD---IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-211 |
4.17e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.08 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKLrqdqfafeeftVLDTV 85
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-----GRD-----------VTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 ImghkelwevkQERDrI------YAL-PEMSeedgykVAD-----LEVKygemdGYSA---EARAGEL--LLGVGiPVEQ 148
Cdd:COG3839 72 P----------KDRN-IamvfqsYALyPHMT------VYEniafpLKLR-----KVPKaeiDRRVREAaeLLGLE-DLLD 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 149 HYgPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:COG3839 129 RK-P-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
338-470 |
4.67e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 338 LNLLLEVGEKLAVLGTNGVGKSTLLKTLVGdLQPDSGTV--------KWS--ENARI-GYYAQDHEYEFenDLTVFEWMS 406
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngrplsDWSaaELARHrAYLSQQQSPPF--AMPVFQYLA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 407 QWKQEGDDEQAVRSILGRL---LFSQDDIKKPAKVLSGGEKGRMLFGKLMMQ-KPNI------LIMDEPTNHLD 470
Cdd:COG4138 92 LHQPAGASSEAVEQLLAQLaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLD 165
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-183 |
4.74e-08 |
|
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: 53.83 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA-------------FEEFTVLDTVIMG---HKELWE 94
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRIArlgigyvpegrriFPSLTVEENLLLGayaRRDRAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 95 VKQERDRIYAL-PEMseedgykvadlevkyGEMdgysAEARAGELLLGvgipvEQHygpMseVApgwklrvlLAQALFAD 173
Cdd:COG0410 112 VRADLERVYELfPRL---------------KER----RRQRAGTLSGG-----EQQ---M--LA--------IGRALMSR 154
|
170
....*....|
gi 1352184330 174 PDILLLDEPT 183
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-514 |
4.86e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQdqfaf 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 eeftVLDTVIMGHKELWEVK-QERDRIYALPEMSEED----GYKVADLEVKYGEMDGYSAEARAGELLLGVGIPVEQ--- 148
Cdd:PRK10261 87 ----VIELSEQSAAQMRHVRgADMAMIFQEPMTSLNPvftvGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 149 ----HygpmsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDID---TIRWLEQVLN-ERDSTMIIISHDRHFLNMVCT 220
Cdd:PRK10261 163 srypH-----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQkEMSMGVIFITHDMGVVAEIAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 221 HMADLDYGElRVYPGNYDEYMTAATQARER-LLAdnAKKKAQIAELQSFVSRFSANASKSRQATSRARQIDKIKLEEVKA 299
Cdd:PRK10261 238 RVLVMYQGE-AVETGSVEQIFHAPQHPYTRaLLA--AVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGEPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 300 SSRqNPFIRFEQDKKLF-RNALEVEGLTK-GFDNGPlfknlnlllevGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK 377
Cdd:PRK10261 315 QVR-NLVTRFPLRSGLLnRVTREVHAVEKvSFDLWP-----------GETLSLVGESGSGKSTTGRALLRLVESQGGEII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 W--------------SENARIGYYAQDHEYEFENDLTV-FEWMSQWKQEG--DDEQAVRSI---LGRLLFSQDDIKKPAK 437
Cdd:PRK10261 383 FngqridtlspgklqALRRDIQFIFQDPYASLDPRQTVgDSIMEPLRVHGllPGKAAAARVawlLERVGLLPEHAWRYPH 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 438 VLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALELYQG---TLIFVSHDREFVSSLATR-------- 504
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDLQRDfgiAYLFISHDMAVVERISHRvavmylgq 541
|
570
....*....|
gi 1352184330 505 ILEITPERVI 514
Cdd:PRK10261 542 IVEIGPRRAV 551
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
318-506 |
4.92e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS---------ENARIGYYA 388
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDHEYEFENDLT-VFEWMSQW--------------------KQEGDdEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRM 447
Cdd:PRK10619 84 KNQLRLLRTRLTmVFQHFNLWshmtvlenvmeapiqvlglsKQEAR-ERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 448 LFGKLMMQKPNILIMDEPTNHLDMESI-ESLNMALELYQ--GTLIFVSHDREFVSSLATRIL 506
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVI 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-493 |
5.06e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLvgdlqpdSGTVKWSENARI-GYYAQDHEYEF 395
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-------NRLIELYPEARVsGEVYLDGQDIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ENDLT--------VFEW------MSQW-------------KQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKG 445
Cdd:PRK14247 74 KMDVIelrrrvqmVFQIpnpipnLSIFenvalglklnrlvKSKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 446 RMLFGKLMMQKPNILIMDEPTNHLDMES---IESLNMALElYQGTLIFVSH 493
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELK-KDMTIVLVTH 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-493 |
7.16e-08 |
|
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: 53.24 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYyaqDHEYEFE------NDLTVFE--- 403
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYLHSkvslvgQEPVLFArsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 404 ------WMSQWKQEGDDEQAVRS-----ILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDME 472
Cdd:cd03248 105 qdniayGLQSCSFECVKEAAQKAhahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|....*
gi 1352184330 473 SIESLNMAleLYQG----TLIFVSH 493
Cdd:cd03248 185 SEQQVQQA--LYDWperrTVLVIAH 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
8.37e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsLDPNERIGKLRQD-QFAFEEF- 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDtRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 80 -----TVLDTVIMGHKELWEVKQERdriyALPEMSEEDgykvadlevkygemdgysaeaRAGELllgvgipveqhygPmS 154
Cdd:PRK11247 92 llpwkKVIDNVGLGLKGQWRDAALQ----ALAAVGLAD---------------------RANEW-------------P-A 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 155 EVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-504 |
8.65e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTL--VGDLQPD---SGTVKWSEN------------- 381
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 382 ARIGY-YAQDHEYEF---ENDLTVFEWMSQWKQEGDDEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:PRK14239 86 KEIGMvFQQPNPFPMsiyENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEvkDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 456 KPNILIMDEPTNHLDMES---IESLNMALElYQGTLIFVSHDREFVSSLATR 504
Cdd:PRK14239 166 SPKIILLDEPTSALDPISagkIEETLLGLK-DDYTMLLVTRSMQQASRISDR 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-502 |
8.90e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLvGDLQPDSGTVKwsENARIGYYAQDhEYEFEND 398
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVR--VEGRVEFFNQN-IYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 399 L-------------------TVFE----------WMSQWKQEGDDEQAVRSilGRLLfsqDDIK----KPAKVLSGGEKG 445
Cdd:PRK14258 83 LnrlrrqvsmvhpkpnlfpmSVYDnvaygvkivgWRPKLEIDDIVESALKD--ADLW---DEIKhkihKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 446 RMLFGKLMMQKPNILIMDEPTNHLD------MES-IESLNMALELyqgTLIFVSHDREFVSSLA 502
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasmkVESlIQSLRLRSEL---TMVIVSHNLHQVSRLS 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
320-470 |
9.94e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENA-------------RIGY 386
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHEYE-FENDL---TVFEWMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIM 462
Cdd:PRK13638 82 VFQDPEQQiFYTDIdsdIAFSLRNLGVPEAEITRRVDEAL-TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
....*...
gi 1352184330 463 DEPTNHLD 470
Cdd:PRK13638 161 DEPTAGLD 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
281-470 |
1.00e-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: 54.92 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 281 QATSRARQIDKIKLEEVKASSRQNPF-------IRFEQDKKLFRNA--LEVEGLTKGFDNG--PLFKNLNLLLEVGEKLA 349
Cdd:TIGR01271 1170 RSVSRVFKFIDLPQEEPRPSGGGGKYqlstvlvIENPHAQKCWPSGgqMDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVG 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 350 VLGTNGVGKSTLLKTLV------GDLQPDSgtVKWSE------NARIGYYAQD---HEYEFENDLTVFE-WMSQ--WKQE 411
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLrllsteGEIQIDG--VSWNSvtlqtwRKAFGVIPQKvfiFSGTFRKNLDPYEqWSDEeiWKVA 1327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 412 gdDEQAVRSIL----GRLLFSQDDikkPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:TIGR01271 1328 --EEVGLKSVIeqfpDKLDFVLVD---GGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
1.04e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnerigklrqdqfafeefTVLDTVIMGHKE 91
Cdd:PRK13647 17 GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---------------------KVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 92 LWEVKQ-------ERDRIYAlpeMSEEDgykvadlEVKYG----EMDGYSAEARAGELLLGVGIPVEQHYGPMsEVAPGW 160
Cdd:PRK13647 75 KWVRSKvglvfqdPDDQVFS---STVWD-------DVAFGpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPY-HLSYGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
320-505 |
1.08e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLqPDSG-----------TVKWSENARI---- 384
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL-TGGGaprgarvtgdvTLNGEPLAAIdapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 385 -----GYYAQDHEYEFE---NDLTVFEWMSQWKQEGDDEQAVRSILGRLLFSQDD---IKKPAKVLSGGEKGRMLFGKLM 453
Cdd:PRK13547 81 larlrAVLPQAAQPAFAfsaREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 454 MQ---------KPNILIMDEPTNHLDMESIESL-----NMALELYQGTLIFVsHDREFVSSLATRI 505
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRI 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-241 |
1.24e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnerigklrqdqfafeeftvLDTVIMGHKELWEVKQ 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 98 ER-----DRIYALPEMSEEDgykvadlEVKYG-EMDGYSAEAR---AGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQ 168
Cdd:PRK10070 106 KKiamvfQSFALMPHMTVLD-------NTAFGmELAGINAEERrekALDALRQVGLENYAHSYP-DELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 169 ALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYM 241
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV-VQVGTPDEIL 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
1.38e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLEPTL---GNVSL---DPNER---IGKLR-QD 72
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVrveGRVEFfnqNIYERrvnLNRLRrQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 73 QFAFEE-----FTVLDTVIMGHKEL-WEVKQERDRIYalpemseEDGYKVADL--EVKYgemdgysaearagelllgvgi 144
Cdd:PRK14258 91 SMVHPKpnlfpMSVYDNVAYGVKIVgWRPKLEIDDIV-------ESALKDADLwdEIKH--------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 145 pvEQHYGPMsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN----ERDSTMIIISHDRHFLNMVCT 220
Cdd:PRK14258 143 --KIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslrlRSELTMVIVSHNLHQVSRLSD 219
|
250
....*....|..
gi 1352184330 221 HMADLDYGELRV 232
Cdd:PRK14258 220 FTAFFKGNENRI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-211 |
1.40e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErigklrqdqfafeeftvldtviMGHKELW 93
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL----------------------LTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 94 EVKQERDRIYALPEmSEEDGYKVADlEVKYG-EMDGYSAE---ARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQA 169
Cdd:PRK13650 78 DIRHKIGMVFQNPD-NQFVGATVED-DVAFGlENKGIPHEemkERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 170 LFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
1.46e-07 |
|
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: 52.09 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLRQDQFAFEEfTVLDTVIMG---- 88
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQEPWIQNG-TIRENILFGkpfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 89 HKELWEVKQ----ERDrIYALPemseeDGykvaDL-EVkyGEMdgysaearaGELLLGvgipveqhygpmsevapGWKLR 163
Cdd:cd03250 94 EERYEKVIKacalEPD-LEILP-----DG----DLtEI--GEK---------GINLSG-----------------GQKQR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDIDTIRWL-EQVLNE---RDSTMIIISHDRHFL 215
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGlllNNKTRILVTHQLQLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
311-506 |
1.47e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.56 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 311 QDKKLFrnaLEVEGLTKGFD---NGPLF----KNL------NLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK 377
Cdd:PRK15079 3 EGKKVL---LEVADLKVHFDikdGKQWFwqppKTLkavdgvTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 378 WsenarIGyyaqdheyefeNDLTVfewMS--QWKQEGDDEQAV----------RSILGRLL----------FSQDDIKKP 435
Cdd:PRK15079 80 W-----LG-----------KDLLG---MKddEWRAVRSDIQMIfqdplaslnpRMTIGEIIaeplrtyhpkLSRQEVKDR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 436 AKVL------------------SGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALELYQG---TLIFVS 492
Cdd:PRK15079 141 VKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQAqvVNLLQQLQREmglSLIFIA 219
|
250
....*....|....
gi 1352184330 493 HDREFVSSLATRIL 506
Cdd:PRK15079 220 HDLAVVKHISDRVL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
333-493 |
1.51e-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: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGT---------------------------VKWSENAR-- 383
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlldgvplvqydhhylhrqvalvgqepVLFSGSVRen 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 384 IGYYAQDHEYEfendltvfEWMSQWKQEGDDEqavrSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:TIGR00958 575 IAYGLTDTPDE--------EIMAAAKAANAHD----FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|
gi 1352184330 464 EPTNHLDMESIESLNMALELYQGTLIFVSH 493
Cdd:TIGR00958 643 EATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
1.55e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLE-----PTLGNVSLDpNERIGKL------R 70
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLD-GQDIFKMdvielrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 QDQFAFE------EFTVLDTVIMGHKELWEVKQERDRIYALPEMSEEdgykvADL--EVKygemdgysaearagelllgv 142
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVALGLKLNRLVKSKKELQERVRWALEK-----AQLwdEVK-------------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 143 gipvEQHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:PRK14247 138 ----DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLElkKDMTIVLVTH 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-506 |
1.74e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.13 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGF--DNGPLF--KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQP---DSGTVKW--------SENA-- 382
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFdgedllklSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 -----RIGYYAQD--------HeyefendlTVFEWMSQ--WKQEGDDEQAVRSILGRLLfSQDDIKKPAKV-------LS 440
Cdd:COG0444 82 kirgrEIQMIFQDpmtslnpvM--------TVGDQIAEplRIHGGLSKAEARERAIELL-ERVGLPDPERRldrypheLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 441 GGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALEL---YQGTLIFVSHDREFVSSLATRIL 506
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiLNLLKDLqreLGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-473 |
1.75e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.16 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV------------KWSENaRIGYYAQdheyefENDL- 399
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlRWLRS-QIGLVSQ------EPVLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 --TVFEWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:cd03249 90 dgTIAENIRYGKPDATDEEVEEAA--KKANIHDFIMSlPdgydtlvgerGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
....*..
gi 1352184330 467 NHLDMES 473
Cdd:cd03249 168 SALDAES 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-199 |
1.94e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNerigklrqdQFAFEEFTVLDTVI-MGHKELWEVK 96
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---------PLHFGDYSYRSQRIrMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 97 QERDRIyalpemseedgYKVADLEVKYG-EMDGYSAEARAGELLLGVGI-PVEQHYGPMSeVAPGWKLRVLLAQALFADP 174
Cdd:PRK15112 101 NPRQRI-----------SQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHM-LAPGQKQRLGLARALILRP 168
|
170 180
....*....|....*....|....*
gi 1352184330 175 DILLLDEPTNNLDIdTIRwlEQVLN 199
Cdd:PRK15112 169 KVIIADEALASLDM-SMR--SQLIN 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-493 |
2.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTL--VGDLQPDS---GTVK------WSENA--- 382
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRlfgrniYSPDVdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 383 ----RIGYYAQ-----DHEYEFENDLTVFEWMSQWKQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKGRMLFG 450
Cdd:PRK14267 82 evrrEVGMVFQypnpfPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1352184330 451 KLMMQKPNILIMDEPTNHLD---MESIESLNMALElYQGTLIFVSH 493
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELK-KEYTIVLVTH 206
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
339-471 |
2.17e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 339 NLLLEVGEKL------AVLGTNGVGKSTLLKTLVGDLQPDSGTVKWS---------------ENARIGYYAQDHE----Y 393
Cdd:PRK11144 12 DLCLTVNLTLpaqgitAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiclppEKRRIGYVFQDARlfphY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 394 EFENDLT--VFEWMsqwKQEGDDEQAVRSI---LGRLLFSqddikkpakvLSGGEKGRMLFGKLMMQKPNILIMDEPTNH 468
Cdd:PRK11144 92 KVRGNLRygMAKSM---VAQFDKIVALLGIeplLDRYPGS----------LSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
...
gi 1352184330 469 LDM 471
Cdd:PRK11144 159 LDL 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
2.61e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKIL------------GGDLepTLGNVS-------LDP 62
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDV--LLGGRSifnyrdvLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 63 NERIGKLRQDQFAFEeFTVLDTVIMGHkelwevkqerdRIYALPEMSEEDGYkvadlevkygemdgysAEARAGELLLGV 142
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGV-----------RAHKLVPRKEFRGV----------------AQARLTEVGLWD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 143 GIPVEQHYGPMsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDS--TMIIISHD 211
Cdd:PRK14271 152 AVKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
320-513 |
2.77e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.91 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFdnGPLF--KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYyaQDHEYE--- 394
Cdd:PRK11300 6 LSVSGLMMRF--GGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 ----FEN-----DLTVFE--WMSQWKQEGDD-----------EQAVRSILGRLLFSQDDI------KKPAKVLSGGEKGR 446
Cdd:PRK11300 82 vvrtFQHvrlfrEMTVIEnlLVAQHQQLKTGlfsgllktpafRRAESEALDRAATWLERVgllehaNRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 447 MLFGKLMMQKPNILIMDEPTNHLDMESIESLN-MALEL---YQGTLIFVSHDREFVSSLATRILEI---------TPERV 513
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDeLIAELrneHNVTVLLIEHDMKLVMGISDRIYVVnqgtplangTPEEI 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-217 |
2.99e-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: 2.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRW-LEQVLNERDST----MIIISHDRHFLNM 217
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQknfqLIVITHDEELVDA 188
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-218 |
3.28e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNVSLDpneriGklrQDqfafeeftVLD 83
Cdd:COG0396 5 NLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLD-----G---ED--------ILE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 tvimghkelWEVkQERDR---IYALPEMSEEDGYKVADL------EVKYGEMDGYSAEARAGELLLGVGIPVEqhygpM- 153
Cdd:COG0396 69 ---------LSP-DERARagiFLAFQYPVEIPGVSVSNFlrtalnARRGEELSAREFLKLLKEKMKELGLDED-----Fl 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 154 -SEVAPGW----KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE---RDSTMIIISHDRHFLNMV 218
Cdd:COG0396 134 dRYVNEGFsggeKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlrsPDRGILIITHYQRILDYI 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
333-498 |
3.37e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYYAQDHEYE------------------ 394
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysvayaaqkpwllnat 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 395 FENDLTvFE--WMSQWKQEGDDEQAVRSILGRLLF-SQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM 471
Cdd:cd03290 95 VEENIT-FGspFNKQRYKAVTDACSLQPDIDLLPFgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190
....*....|....*....|....*....|..
gi 1352184330 472 ESIESLNMA--LELYQG---TLIFVSHDREFV 498
Cdd:cd03290 174 HLSDHLMQEgiLKFLQDdkrTLVLVTHKLQYL 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
3.66e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnerigklrqdqfaf 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 77 eefTVLDTVI-MGHKELWEVKQERDRI---YALPEMS------EEDgykVADLEVKYGEmDGYSAEARAGELLLGVGIPV 146
Cdd:PRK13645 69 ---IVGDYAIpANLKKIKEVKRLRKEIglvFQFPEYQlfqetiEKD---IAFGPVNLGE-NKQEAYKKVPELLKLVQLPE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 147 EQHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13645 142 DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
3.88e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 51.00 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER----IGKL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpMHKRarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVldtvimghkelwevkqeRDRIYALPEMSEEDGYKvadlevkygemdgysAEARAGELLLGVGI-PVEQ 148
Cdd:cd03218 81 PQEASIFRKLTV-----------------EENILAVLEIRGLSKKE---------------REEKLEELLEEFHItHLRK 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 149 HYGpmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD---IDTIRWLEQVLNERDSTMIIISH 210
Cdd:cd03218 129 SKA--SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
320-493 |
4.66e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------------SENARIGYY 387
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpksSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQdhEYEFENDLTVFE-----------WMS-QWK---QEGDDeqavrsILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKL 452
Cdd:PRK10762 85 HQ--ELNLIPQLTIAEniflgrefvnrFGRiDWKkmyAEADK------LLARLNLRFSS-DKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1352184330 453 MMQKPNILIMDEPTNHL-DMESiESL-NMALEL-YQGT-LIFVSH 493
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTET-ESLfRVIRELkSQGRgIVYISH 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-502 |
4.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 330 DNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKwsENARIGYYAQD--------------HEYEF 395
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKDifqidaiklrkevgMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 EN---DLTVFEWMS-QWKQEG-DDEQAVRSILGRLLFS-------QDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMD 463
Cdd:PRK14246 99 PNpfpHLSIYDNIAyPLKSHGiKEKREIKKIVEECLRKvglwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1352184330 464 EPTNHLDM---ESIESLNMALElYQGTLIFVSHDREFVSSLA 502
Cdd:PRK14246 179 EPTSMIDIvnsQAIEKLITELK-NEIAIVIVSHNPQQVARVA 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-211 |
4.75e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN--------------ERIGKLRQ 71
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvrKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVLDTVIMGHKELWEVKQERDRIYALPEMseedgykvadlevkygemdgysaEAragelllgVGIPVEQHYG 151
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKL-----------------------EA--------VGLRGAAKLM 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 152 PmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDS----TMIIISHD 211
Cdd:PRK11831 141 P-SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-242 |
4.77e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.52 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFL-NMVCTHMadLDYGELRVYpGNYDE 239
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLeQFDRICV--MDNGQIIEQ-GTHQE 559
|
...
gi 1352184330 240 YMT 242
Cdd:PRK11160 560 LLA 562
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
283-528 |
4.83e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.27 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 283 TSRARQIDKIKLEEVKASSRQNPFIRfeqDKKLFRNALEVEGLTKGFDN-GPLFKNLNLLLEVGEKLAVLGTNGVGKSTL 361
Cdd:PRK13657 301 MAAPKLEEFFEVEDAVPDVRDPPGAI---DLGRVKGAVEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 362 LKTLVGDLQPDSGTVKW-------------------------------SENARIGyyaqdheyefENDLTVFEWMSQWKQ 410
Cdd:PRK13657 378 INLLQRVFDPQSGRILIdgtdirtvtraslrrniavvfqdaglfnrsiEDNIRVG----------RPDATDEEMRAAAER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 EgddeQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLNMAL-ELYQGTLI 489
Cdd:PRK13657 448 A----QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdELMKGRTT 523
|
250 260 270
....*....|....*....|....*....|....*....
gi 1352184330 490 FVSHDREFVSSLATRILEITPERVIDfSGNYEDYLRSKG 528
Cdd:PRK13657 524 FIIAHRLSTVRNADRILVFDNGRVVE-SGSFDELVARGG 561
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
334-494 |
4.88e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 334 LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENA---RIGYYAQdhEYEFENDLTVF 402
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleSWSSKAfarKVAYLPQ--QLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 403 E--------WMSQWKQEG-DDEQAVR---SILGRLLFSQddikKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:PRK10575 104 ElvaigrypWHGALGRFGaADREKVEeaiSLVGLKPLAH----RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*...
gi 1352184330 471 M-ESIESLNMALELYQG---TLIFVSHD 494
Cdd:PRK10575 180 IaHQVDVLALVHRLSQErglTVIAVLHD 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
320-514 |
4.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.25 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLN---LLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK-----------WSENARIG 385
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQDHEYEF-----ENDLTvfewMSQWKQEGDDEQAVRSILGRLL-FSQDDIK--KPAKvLSGGEKGRMLFGKLMMQKP 457
Cdd:PRK13642 85 MVFQNPDNQFvgatvEDDVA----FGMENQGIPREEMIKRVDEALLaVNMLDFKtrEPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 458 NILIMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVSSlATRILEITPERVI 514
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
339-491 |
5.33e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 339 NLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSG--TVKWSENARIGYYAQDH--EYEFE---NDLtvfewMSQwkQE 411
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFSHITRLSFEQLQKlvSDEWQrnnTDM-----LSP--GE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 412 GDDEQAVRSILgrllfsQDDIKKPA-------------------KVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDME 472
Cdd:PRK10938 96 DDTGRTTAEII------QDEVKDPArceqlaqqfgitalldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|..
gi 1352184330 473 SIESLNMALE-LYQG--TLIFV 491
Cdd:PRK10938 170 SRQQLAELLAsLHQSgiTLVLV 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-210 |
5.46e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRqDQFAfeeft 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRRQR-DEYH----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 81 vLDTVIMGHkeLWEVKqerdriyalPEMSEEDGYKVadlevkYGEMDGYSAEARAGELLLGVG------IPVEQhygpMS 154
Cdd:PRK13538 74 -QDLLYLGH--QPGIK---------TELTALENLRF------YQRLHGPGDDEALWEALAQVGlagfedVPVRQ----LS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 155 EvapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISH 210
Cdd:PRK13538 132 A---GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAqhaEQGGMVILTTH 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
5.55e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKfgGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKlrqdqfafeeftVLDTVIMGHKELWE---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----GK------------PIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 95 VKQERDRIYALPEMSEEDGYKVADLEVKYGEMdgysaEARAGELLLGVGIPVEQHyGPMSEVAPGWKLRVLLAQALFADP 174
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 175 DILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNPKE 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
119-253 |
6.05e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 119 LEVKYGEMDGYSAEARAGELLLGVGI-PVEQHYGPmSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD------IDTI 191
Cdd:PRK15134 389 LRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqILAL 467
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 192 rwLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYMTAATQARER-LLA 253
Cdd:PRK15134 468 --LKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV-VEQGDCERVFAAPQQEYTRqLLA 527
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
345-470 |
6.36e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSEN---------ARIGYYAQDHeyEFENDLTVFEWM---------- 405
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANnrkptkqilKRTGFVTQDD--ILYPHLTVRETLvfcsllrlpk 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 406 SQWKQEGDD-EQAVRSILGrLLFSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:PLN03211 172 SLTKQEKILvAESVISELG-LTKCENTIIGNSFIrgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
7.69e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLF--ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIgklrqDQFAFEEFtvld 83
Cdd:PRK13648 12 NVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN-NQAI-----TDDNFEKL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 tvimgHKELWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMdgysaEARAGELLLGVGIPVEQHYGPMSeVAPGWKLR 163
Cdd:PRK13648 82 -----RKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEM-----HRRVSEALKQVDMLERADYEPNA-LSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDpdarQNLLDLVRKVKSEHNITIISITHD 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-367 |
9.38e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 9.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG 367
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-233 |
9.84e-07 |
|
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: 50.06 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN--ERIGKLR----QDQFafeEFTVLDTVIMGHKELWeV----KQERD 100
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRgselQNYF---TKLLEGDVKVIVKPQY-VdlipKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 101 RIYALPEMSEEDGYKvaDLEVKYGEMDGYsaearagelllgvgipVEQHygpMSEVAPGWKLRVLLAQALFADPDILLLD 180
Cdd:cd03236 106 KVGELLKKKDERGKL--DELVDQLELRHV----------------LDRN---IDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 181 EPTNNLDID---TIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLdYGELRVY 233
Cdd:cd03236 165 EPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAY 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-505 |
1.11e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.08 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 321 EVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLkTLVGDLQP-DSGTV--------KWSENA---RIGYYA 388
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SMISRLLPpDSGEVlvdgldvaTTPSRElakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QdheyefEND----LTVFEWM-------SQWKQEGDDEQAVRSILGRLlfSQDDIK-KPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:COG4604 82 Q------ENHinsrLTVRELVafgrfpySKGRLTAEDREIIDEAIAYL--DLEDLAdRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 457 PNILIMDEPTNHLDMEsiESLNM-------ALELyQGTLIFVSHDREFVSSLATRI 505
Cdd:COG4604 154 TDYVLLDEPLNNLDMK--HSVQMmkllrrlADEL-GKTVVIVLHDINFASCYADHI 206
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
1.14e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.99 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE----------RIGKLR 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 71 --QDQFAFEEFTVLDTVImghkelweVKQERD-RIYALPEMSEEDGYKVADLEvkygemdgysAEARAGELLLGVGIpVE 147
Cdd:PRK11300 85 tfQHVRLFREMTVIENLL--------VAQHQQlKTGLFSGLLKTPAFRRAESE----------ALDRAATWLERVGL-LE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 148 QHYGPMSEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVL----NERDSTMIIISHD 211
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHD 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-226 |
1.35e-06 |
|
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: 48.30 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPtLGNvsldpnERIGKLRQDQFAFeeftvldtvimghkel 92
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWP-WGS------GRIGMPEGEDLLF---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 93 wevkqerdriyaLPEMSeedgykvadlevkygemdgYSAEARAGELLLgvgipveqhYGPMSEVAPGWKLRVLLAQALFA 172
Cdd:cd03223 69 ------------LPQRP-------------------YLPLGTLREQLI---------YPWDDVLSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 173 DPDILLLDEPTNNLDIDTIRWLEQVLNERDSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-232 |
1.46e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------SLDPN--ERIGKL-----RQDQFAFEEFTV 81
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidTGDFSklQGIRKLvgivfQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTVIMGHKELW----EVKQERDRiyALPEMSEEdgykvadlevKYgemdgysaearagelllgvgipveQHYGPMSeVA 157
Cdd:PRK13644 96 EEDLAFGPENLClppiEIRKRVDR--ALAEIGLE----------KY------------------------RHRSPKT-LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDT-IRWLEQV--LNERDSTMIIISHdrhflNMVCTHMAD----LDYGEL 230
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIkkLHEKGKTIVYITH-----NLEELHDADriivMDRGKI 213
|
..
gi 1352184330 231 RV 232
Cdd:PRK13644 214 VL 215
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-216 |
1.47e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.57 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGD--LEPTLGNVSLD--------PNERIgklRQDQF- 74
Cdd:TIGR01978 5 DLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKgqdllelePDERA---RAGLFl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 75 AF---EEFTVLDTVIMGHKELWEVKQERDRiyalPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGvgipveqhyg 151
Cdd:TIGR01978 82 AFqypEEIPGVSNLEFLRSALNARRSARGE----EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSG---------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 152 pmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLN 216
Cdd:TIGR01978 148 -------GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINrlrEPDRSFLIITHYQRLLN 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-269 |
1.69e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKS-TFMKILGGDLEPtlgnvsldpneriGKLRQDQFAFEEFTVLDTvimghkelwEVK 96
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------------GRVMAEKLEFNGQDLQRI---------SEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 97 QERDRIYALPEMSEED-----------GYKVAD-LEVKYGemdGYSAE--ARAGELLLGVGIPveqhyGPMS--EVAP-- 158
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDpmtslnpcytvGFQIMEaIKVHQG---GNKKTrrQRAIDLLNQVGIP-----DPASrlDVYPhq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 159 ---GWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNERDSTMIIISHDRHFLNMVCTHMADLDYGELr 231
Cdd:PRK11022 154 lsgGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1352184330 232 VYPGNYDEYMTAA----TQARERLLADNAKKKAQIAELQSFV 269
Cdd:PRK11022 233 VETGKAHDIFRAPrhpyTQALLRALPEFAQDKARLASLPGVV 274
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-245 |
1.75e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAFEEFTVLDTVIMGHKELWEVKQERDRIyALPEMSE 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEI-AKPLQIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 111 edgyKVADLEVKygEMDGysaearaGELllgvgipveQhygpmsevapgwklRVLLAQALFADPDILLLDEPTNNLDID- 189
Cdd:cd03237 107 ----QILDREVP--ELSG-------GEL---------Q--------------RVAIAACLSKDADIYLLDEPSAYLDVEq 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 190 ---TIRWLEQVLNERDSTMIIISHDrhFLnmvcthMADLDYGELRVYPGNYDEYMTAAT 245
Cdd:cd03237 151 rlmASKVIRRFAENNEKTAFVVEHD--II------MIDYLADRLIVFEGEPSVNGVANP 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-474 |
2.00e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.12 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV----------KWSENAR--IGYY 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllPLHARARrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 388 AQDHEY-----EFENDLTVFEWMSQWKQEGDDEQAvRSILGRLLFS--QDDIkkpAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK10895 84 PQEASIfrrlsVYDNLMAVLQIRDDLSAEQREDRA-NELMEEFHIEhlRDSM---GQSLSGGERRRVEIARALAANPKFI 159
|
170
....*....|....
gi 1352184330 461 IMDEPTNHLDMESI 474
Cdd:PRK10895 160 LLDEPFAGVDPISV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-217 |
2.21e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.26 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTL---GNVSL----------DPNE---RIG 67
Cdd:COG1117 16 NLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLdgediydpdvDVVElrrRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 68 KLRQDQFAFEeFTVLDTVIMGHKelweVKQERDRiyalpemseedgykvadlevkyGEMDgysaeARAGELLLGVGIPve 147
Cdd:COG1117 96 MVFQKPNPFP-KSIYDNVAYGLR----LHGIKSK----------------------SELD-----EIVEESLRKAALW-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 148 qhygpmSEV-----APGWKL------RVLLAQALFADPDILLLDEPTNNLD-IDTIRwLEQVLNE--RDSTMIIISHdrh 213
Cdd:COG1117 142 ------DEVkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElkKDYTIVIVTH--- 211
|
....
gi 1352184330 214 flNM 217
Cdd:COG1117 212 --NM 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-230 |
2.31e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.07 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLE-----PTLGNVSL----------DPNE---RIG 67
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLfgrniyspdvDPIEvrrEVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 68 KLRQDQFAFEEFTVLDTVIMGHK--ELWEVKQERDRI--YALPEMSEEDgykvadlEVKyGEMDGYSAEARAGElllgvg 143
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKELDERveWALKKAALWD-------EVK-DRLNDYPSNLSGGQ------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 144 ipveqhygpmsevapgwKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISHDRHFLNMVCTH 221
Cdd:PRK14267 155 -----------------RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFElkKEYTIVLVTHSPAQAARVSDY 217
|
....*....
gi 1352184330 222 MADLDYGEL 230
Cdd:PRK14267 218 VAFLYLGKL 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
329-493 |
2.40e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 329 FDNGP--------LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLvGDLQPD-SGTVKWSENARIGYYAQdHEY----EF 395
Cdd:TIGR00954 454 FENIPlvtpngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQ-RPYmtlgTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ENDLTVFEWMSQWKQEGDDEQAVRSIL-----GRLL---FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTN 467
Cdd:TIGR00954 532 RDQIIYPDSSEDMKRRGLSDKDLEQILdnvqlTHILereGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180
....*....|....*....|....*.
gi 1352184330 468 HLDMESIESLNMALELYQGTLIFVSH 493
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-211 |
2.43e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP--------NER----IGKL 69
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVLDTV--IMGHKELWEVKQERDRIyalPEMSEEdgYKVADLEVKYGEmdgysaearagelllgvgipve 147
Cdd:PRK10895 84 PQEASIFRRLSVYDNLmaVLQIRDDLSAEQREDRA---NELMEE--FHIEHLRDSMGQ---------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 148 qhygpmsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVlneRDSTM--IIISHD 211
Cdd:PRK10895 137 -------SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvIDIKRIIEHL---RDSGLgvLITDHN 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-494 |
2.63e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 342 LEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSENARIGYyaqDHEYE----------FEN---DLtvfewmsqw 408
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA---DPEAQkllrqkiqivFQNpygSL--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 409 kqegDDEQAVRSILGRLLFSQDDIKKP---AKVL--------------------SGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:PRK11308 106 ----NPRKKVGQILEEPLLINTSLSAAerrEKALammakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|....
gi 1352184330 466 TNHLDMeSIES--LNMALELYQ--GT-LIFVSHD 494
Cdd:PRK11308 182 VSALDV-SVQAqvLNLMMDLQQelGLsYVFISHD 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-210 |
2.96e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLR--QDQFAFEEFTVldtVIMGHKEL 92
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTneQDYQGDEEQNV---GMKNVNEF 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 93 WEVKQERD-RIYALPEMSEE---DG-----YKVADLE--------------------VKYGEMDGYSAE-------ARAG 136
Cdd:PTZ00265 1259 SLTKEGGSgEDSTVFKNSGKillDGvdicdYNLKDLRnlfsivsqepmlfnmsiyenIKFGKEDATREDvkrackfAAID 1338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 137 ELLLGVGIPVEQHYGPMSE-VAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVL----NERDSTMIIISH 210
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-261 |
3.23e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnERIGKLR--------QDQFAFEEFTVLDTVIMGH 89
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----DRNGEVSviaisaglSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 90 KelwevkqeRDRIYAL-PEMseedgykvadleVKYGEMdgysaearaGELLlgvgipveqhYGPMSEVAPGWKLRVLLAQ 168
Cdd:PRK13546 116 K--------RKEIKAMtPKI------------IEFSEL---------GEFI----------YQPVKKYSSGMRAKLGFSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 169 ALFADPDILLLDEPTNNLDID-TIRWLEQV--LNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVYpGNYDEYMtaat 245
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDQTfAQKCLDKIyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVL---- 231
|
250
....*....|....*..
gi 1352184330 246 QARERLLADNAKK-KAQ 261
Cdd:PRK13546 232 PKYEAFLNDFKKKsKAE 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
337-466 |
3.45e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 337 NLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWsENARIGYYAQDHEYE---------FENDL 399
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditDW-QTAKIMREAVAIVPEgrrvfsrmtVEENL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 400 TVFEWMSQWKQEGDDEQAVRSILGRLlfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPT 466
Cdd:PRK11614 102 AMGGFFAERDQFQERIKWVYELFPRL---HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
163-226 |
4.50e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.42 E-value: 4.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNER--DSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-503 |
4.62e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 332 GPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVK--------WSENARI-------GYYAQDHEYE-F 395
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitsTSKNKDIkqirkkvGLVFQFPESQlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 396 ENdlTVFEWMSQWKQ-----EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLD 470
Cdd:PRK13649 100 EE--TVLKDVAFGPQnfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1352184330 471 MESIESLnMAL--ELYQG--TLIFVSHDREFVSSLAT 503
Cdd:PRK13649 178 PKGRKEL-MTLfkKLHQSgmTIVLVTHLMDDVANYAD 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-227 |
5.04e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsLDPNERIGKlrqdqfafeeftvldtvimghKE 91
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITK---------------------EN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 92 LWEVKQERDRIYALPEmsEEDGYKVADLEVKYGE----MDGYSAEARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLA 167
Cdd:PRK13652 73 IREVRKFVGLVFQNPD--DQIFSPTVEQDIAFGPinlgLDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 168 QALFADPDILLLDEPTNNLDIDTIRWLEQVLNERDST--MIIIsHDRHFLNMVcTHMADLDY 227
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVI-FSTHQLDLV-PEMADYIY 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
345-494 |
5.43e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSG----TVKWSEnaRIGYYA----QDHEYEF-ENDLTVfewmSQWKQ----- 410
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeEPSWDE--VLKRFRgtelQNYFKKLyNGEIKV----VHKPQyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 ------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMEsiESLN 478
Cdd:PRK13409 173 pkvfkgkvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR--QRLN 250
|
170 180
....*....|....*....|
gi 1352184330 479 MAL---ELYQG-TLIFVSHD 494
Cdd:PRK13409 251 VARlirELAEGkYVLVVEHD 270
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-239 |
5.54e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpnerIGKlrqdqfafeeftvlDTVIMGHKELWEVKQER 99
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW-----LGK--------------DLLGMKDDEWRAVRSDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 100 DRIYALPEMSEEDGYKVAD-----LEVKYGEMDGYSAEARAGELLLGVGI-P-VEQHYgPmSEVAPGWKLRVLLAQALFA 172
Cdd:PRK15079 101 QMIFQDPLASLNPRMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKVGLlPnLINRY-P-HEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 173 DPDILLLDEPTNNLDID----TIRWLEQVLNERDSTMIIISHDrhfLNMVcTHMADldygelRV---YPGN------YDE 239
Cdd:PRK15079 179 EPKLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHD---LAVV-KHISD------RVlvmYLGHavelgtYDE 248
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-243 |
6.28e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 27 GNRYGLIGANGSGKS-TFMKILGgdleptlgnvSLDPNERIGklrqDQFAFEEFTVLDtviMGHKELWEVKQER-DRIYA 104
Cdd:PRK09473 42 GETLGIVGESGSGKSqTAFALMG----------LLAANGRIG----GSATFNGREILN---LPEKELNKLRAEQiSMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 105 LPEMSEEDGYKVAD--LEV--KYGEMDGYSAEARAGELLLGVGIPVEQHYGPM--SEVAPGWKLRVLLAQALFADPDILL 178
Cdd:PRK09473 105 DPMTSLNPYMRVGEqlMEVlmLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 179 LDEPTNNLDIDTIRWLEQVLNE--RD--STMIIISHDRHFLNMVCTHMadldygeLRVYPGNYDEYMTA 243
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNElkREfnTAIIMITHDLGVVAGICDKV-------LVMYAGRTMEYGNA 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-187 |
6.35e-06 |
|
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: 46.78 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPT-------LGNVSLDPNE---RIGKLRQDQFAFEEFTV 81
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvsgevlINGRPLDKRSfrkIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTvimghkeLWevkqerdriyalpemseedgykvadlevkygemdgYSAEARagelllgvGIPVEQhygpmsevapgwK 161
Cdd:cd03213 100 RET-------LM-----------------------------------FAAKLR--------GLSGGE------------R 117
|
170 180
....*....|....*....|....*.
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLD 187
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-254 |
6.68e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 6 NVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdleptlgnVSLDpNERIgklRQDQFAFEEFTV 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKD-NWRV---TADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LDTVIMGHKELweVKQERDRIYALPEM----SEEDGYKVADlevkygEMDGYSAEA-----------RAGELLLGVGIpv 146
Cdd:PRK15093 76 LRLSPRERRKL--VGHNVSMIFQEPQScldpSERVGRQLMQ------NIPGWTYKGrwwqrfgwrkrRAIELLHRVGI-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 147 EQHYGPMS----EVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIDT----IRWLEQVLNERDSTMIIISHDRHFLNMV 218
Cdd:PRK15093 146 KDHKDAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1352184330 219 CTHMADLDYGElRVYPGNYDEYMTAA----TQARERLLAD 254
Cdd:PRK15093 226 ADKINVLYCGQ-TVETAPSKELVTTPhhpyTQALIRAIPD 264
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-210 |
8.81e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.30 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLePTLGNV--------SLDPN---ERIGKLRQDQFAFEEfTVL 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielrELDPEswrKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 83 DTVIMGHkelwevkqerdriyalPEMSEEDGYKVADLevkygemdgysaeARAGE----LLLGVGIPV-EQHYGpmseVA 157
Cdd:PRK11174 441 DNVLLGN----------------PDASDEQLQQALEN-------------AWVSEflplLPQGLDTPIgDQAAG----LS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 158 PGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:PRK11174 488 VGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTH 542
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-228 |
9.74e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 46.72 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNeriGKLRQDQFAFEEFTV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 82 LdtvimGHKelwevkqerDRIYALPEMSEEDGYKVADlevkYGEMDGYSAEARAGelLLGVG-IPVEQhygpmseVAPGW 160
Cdd:cd03231 78 L-----GHA---------PGIKTTLSVLENLRFWHAD----HSDEQVEEALARVG--LNGFEdRPVAQ-------LSAGQ 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 161 KLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHdrHFLNMVCTHMADLDYG 228
Cdd:cd03231 131 QRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAghcARGGMVVLTTH--QDLGLSEAGARELDLG 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
320-505 |
1.08e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKST-------LLKT-----LVGD--------LQPDSGT 375
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSppvvyPSGDirfhgeslLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 376 VKWSENARIGYYAQD--------HEYEFEndltVFEWMSQwkQEGDDEQAVRS-ILGRLlfSQDDIKKPAK-------VL 439
Cdd:PRK15134 86 LRGVRGNKIAMIFQEpmvslnplHTLEKQ----LYEVLSL--HRGMRREAARGeILNCL--DRVGIRQAAKrltdyphQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352184330 440 SGGEKGRMLFGKLMMQKPNILIMDEPTNHLDM-----------ESIESLNMAlelyqgtLIFVSHDREFVSSLATRI 505
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMG-------LLFITHNLSIVRKLADRV 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
318-495 |
1.09e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 318 NALEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSG---------TVKWSENARIGYYA 388
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 389 QDHeyefendlTVFEWMSQwkqeGDDEQAVRSILGRllfSQDDIKKPAK-----------------VLSGGEKGRMLFGK 451
Cdd:PRK11432 85 QSY--------ALFPHMSL----GENVGYGLKMLGV---PKEERKQRVKealelvdlagfedryvdQISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1352184330 452 LMMQKPNILIMDEPTNHLD------M-ESIESLNMALELyqgTLIFVSHDR 495
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDanlrrsMrEKIRELQQQFNI---TSLYVTHDQ 197
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-493 |
1.12e-05 |
|
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: 46.72 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGT-----VKWSE------NARIGYYAQDhEYEFENdlTV 401
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgVDISKiglhdlRSRISIIPQD-PVLFSG--TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 402 FEWMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKVLSGGEK---G-RMLF--GKLMMQKPNILIMDEPTNHLDMES 473
Cdd:cd03244 95 RSNLDPFGEYSDEElwQALERVGLKEFVESLPGGLDTVVEEGGENlsvGqRQLLclARALLRKSKILVLDEATASVDPET 174
|
170 180
....*....|....*....|..
gi 1352184330 474 IESLNMAL--ELYQGTLIFVSH 493
Cdd:cd03244 175 DALIQKTIreAFKDCTVLTIAH 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-196 |
1.18e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN------------ERIGK 68
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 69 LRQDQFAFEEFTVLDTVIMG--HKELWEVKQERDRIYAL-PEMSEEdgykvadlevkygemdgysaeaRAgelllgvgip 145
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELfPRLHER----------------------RI---------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352184330 146 veQHYGPMSEvapGWKLRVLLAQALFADPDILLLDEPTNNLD-------IDTIRWLEQ 196
Cdd:PRK11614 133 --QRAGTMSG---GEQQMLAIGRALMSQPRLLLLDEPSLGLApiiiqqiFDTIEQLRE 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-190 |
1.31e-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: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSldPNERIGKLRQDQFAFEEfTVLDTVIMGhkelwe 94
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPG-TIKDNIIFG------ 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 95 vkqerdriyalpemseedgykvadleVKYGEMDgYSAEARAGELLLGVGIPVEQHYGPMSE----VAPGWKLRVLLAQAL 170
Cdd:TIGR01271 511 --------------------------LSYDEYR-YTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAV 563
|
170 180
....*....|....*....|
gi 1352184330 171 FADPDILLLDEPTNNLDIDT 190
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVT 583
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
319-473 |
1.33e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNG-PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV--------KWSENARIGYYAQ 389
Cdd:PRK15056 6 GIVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 390 DHEYEFENDLTVFE-----------WMSQWKQEgdDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:PRK15056 86 SEEVDWSFPVLVEDvvmmgryghmgWLRRAKKR--DRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQ 162
|
170
....*....|....*
gi 1352184330 459 ILIMDEPTNHLDMES 473
Cdd:PRK15056 163 VILLDEPFTGVDVKT 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-493 |
1.38e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG-------------DLQP-DSGTVKWSENARIG 385
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifEGEElQASNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQdhEYEFENDLTVFEWM---SQWKQEG---DDEQAVRS--ILGRLlfsQDDIKKPAKV--LSGGEKGRMLFGKLMMQ 455
Cdd:PRK13549 86 IIHQ--ELALVKELSVLENIflgNEITPGGimdYDAMYLRAqkLLAQL---KLDINPATPVgnLGLGQQQLVEIAKALNK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1352184330 456 KPNILIMDEPTNHLDMESIESLnmaLELYQG------TLIFVSH 493
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVL---LDIIRDlkahgiACIYISH 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-526 |
1.41e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 334 LFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVkWSENArIGYYAQD--------------HEYEFENDL 399
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERS-IAYVPQQawimnatvrgnilfFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 400 TVFEWMSQWkqEGDdeqaVRSILGRLlfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIEslNM 479
Cdd:PTZ00243 753 ADAVRVSQL--EAD----LAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE--RV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 480 ALELYQGTL-----IFVSHDREFVsSLATRILEITPERViDFSGNYEDYLRS 526
Cdd:PTZ00243 822 VEECFLGALagktrVLATHQVHVV-PRADYVVALGDGRV-EFSGSSADFMRT 871
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
345-505 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWsENARIGYyaqdheyefendltvfewmsqwkqegddeqavrsilgr 424
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY-------------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 425 llfsqddikKPAKV-LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMEsiESLNMA------LELYQGTLIFVSHDREF 497
Cdd:cd03222 66 ---------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE--QRLNAArairrlSEEGKKTALVVEHDLAV 134
|
....*...
gi 1352184330 498 VSSLATRI 505
Cdd:cd03222 135 LDYLSDRI 142
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-494 |
2.38e-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: 45.82 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV----KWSEnaRIGYYAQDHEYEFENDLTVFEWMSQWKQEGDDE--QAV 418
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE--ILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLipKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 419 RSILGRLLFSQDDIKKPAKV----------------LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMEsiESLNMAL- 481
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELvdqlelrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNAARl 181
|
170
....*....|....*..
gi 1352184330 482 --ELYQGT--LIFVSHD 494
Cdd:cd03236 182 irELAEDDnyVLVVEHD 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-72 |
2.46e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.85 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGS-----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNER--- 65
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklPEYKrak 80
|
....*...
gi 1352184330 66 -IGKLRQD 72
Cdd:COG1101 81 yIGRVFQD 88
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-480 |
2.96e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 345 GEKLAVLGTNGVGKSTLLKTLVGDLQPDSG----TVKWSEnaRIGYYA----QDHEYE-FENDLTVfewmSQWKQ----- 410
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGdydeEPSWDE--VLKRFRgtelQDYFKKlANGEIKV----AHKPQyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 ------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMEsiESLN 478
Cdd:COG1245 173 pkvfkgtvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY--QRLN 250
|
..
gi 1352184330 479 MA 480
Cdd:COG1245 251 VA 252
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
352-478 |
3.10e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 352 GTNGVGKSTLLKTLVGDLQPDSGTVkWSENARIGYYAQ------DHEYEFENDLTVFEWMSQWKQEGDDEQAVRSILGRL 425
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNI-YYKNCNINNIAKpyctyiGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYF 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 426 LFsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESIESLN 478
Cdd:PRK13541 112 KL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
160-248 |
3.40e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.31 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 160 WKlRVLLAQA-LFADPDI------LLLDEPTNNLDIDTIRWLEQVLNERDS---TMIIISHDrhfLNMVCTHmAD----L 225
Cdd:PRK03695 132 WQ-RVRLAAVvLQVWPDInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LNHTLRH-ADrvwlL 206
|
90 100
....*....|....*....|...
gi 1352184330 226 DYGELRVYpGNYDEYMTAATQAR 248
Cdd:PRK03695 207 KQGKLLAS-GRRDEVLTPENLAQ 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-210 |
3.71e-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: 45.62 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 2 LVSSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKST----FMKILGGDLEPTLGNVSLDP------NERIGKL 69
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNTEGDIQIDGVSWNSvplqkwRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 70 RQDQFAFEEFTVLDTVIMGH---KELWEVkqerdriyalpemSEEDGYKVAdLEVKYGEMDgysaearageLLLGVGIPV 146
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKwsdEEIWKV-------------AEEVGLKSV-IEQFPGQLD----------FVLVDGGCV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 147 EQHygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--RDSTMIIISH 210
Cdd:cd03289 139 LSH---------GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
333-473 |
4.34e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 333 PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLV---------GDLQPDSGTVKWSENARIGYYAQdhEYEFENDLTVFE 403
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEILINGRPLDKNFQRSTGYVEQ--QDVHSPNLTVRE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 404 wmsqwkqegddeqavrsilgRLLFSqddikkpAKV--LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES 473
Cdd:cd03232 99 --------------------ALRFS-------ALLrgLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
317-506 |
4.43e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 317 RNALEVEGLTKGFDNG----PLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSE------------ 380
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 381 -------------NARIGYYAQDHEYEFENDLTVFEWMSQ---WKQEGDDEQAVRSI-----LGRLLFSQDDIKKPAKVL 439
Cdd:PRK10261 90 lseqsaaqmrhvrGADMAMIFQEPMTSLNPVFTVGEQIAEsirLHQGASREEAMVEAkrmldQVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352184330 440 SGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIESLNMAL------ELYQGtLIFVSHDREFVSSLATRIL 506
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLikvlqkEMSMG-VIFITHDMGVVAEIADRVL 240
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-511 |
5.22e-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: 43.85 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 336 KNLNLLLEVGEKLAVLGTNGVGKSTLLKTlvgdlqpdsgTVKWSENARIGYYAQdheyEFENDLTVFEwmsqwkqegDDE 415
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNE----------GLYASGKARLISFLP----KFSRNKLIFI---------DQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 416 QAVRSI-LGRLLFSQddikkPAKVLSGGEKGRMLFGKLMMQ--KPNILIMDEPTNHLDMESIESLNMALE--LYQG-TLI 489
Cdd:cd03238 69 QFLIDVgLGYLTLGQ-----KLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKglIDLGnTVI 143
|
170 180
....*....|....*....|..
gi 1352184330 490 FVSHDREFVSSlATRILEITPE 511
Cdd:cd03238 144 LIEHNLDVLSS-ADWIIDFGPG 164
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
5.52e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKfgGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 72 DQFAFEEFTVLDTVIMG-HKELWEVKQERDRIYALPE-MSEEDgykvaDLEVKYGEMDGysaearagelllgvgipveqh 149
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlNPGLKLNAAQREKLHAIARqMGIED-----LLARLPGQLSG--------------------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 150 ygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISH 210
Cdd:PRK10771 133 ---------GQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
133-224 |
5.61e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 133 ARAGELLLGVGIPVEqHYG--P-MseVAPGWKLRVLLAQALFADPDILLLDEPTNNLDIdTIRwlEQVLN-------ERD 202
Cdd:PRK11308 132 EKALAMMAKVGLRPE-HYDryPhM--FSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQ--AQVLNlmmdlqqELG 205
|
90 100
....*....|....*....|..
gi 1352184330 203 STMIIISHDrhfLNMVcTHMAD 224
Cdd:PRK11308 206 LSYVFISHD---LSVV-EHIAD 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
32-209 |
6.57e-05 |
|
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: 44.18 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 32 LIGANGSGKSTFMKILGGDLEptlGNVSLDpneriGKLRQDQFAFEEFtvldtvimghkelwEVKQERDRIYAlpemSEE 111
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTE---GNVSVE-----GDIHYNGIPYKEF--------------AEKYPGEIIYV----SEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 112 DgYKVADLEVKygEMDGYSAEARAGELLLGvgipveqhygpmseVAPGWKLRVLLAQALFADPDILLLDEPTNNLD---- 187
Cdd:cd03233 92 D-VHFPTLTVR--ETLDFALRCKGNEFVRG--------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDssta 154
|
170 180
....*....|....*....|....*
gi 1352184330 188 ---IDTIRWLEQVLneRDSTMIIIS 209
Cdd:cd03233 155 leiLKCIRTMADVL--KTTTFVSLY 177
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-245 |
7.29e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.45 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPTLGNVSLD--------PNE---RIGKLRQDQ---FAFEEFTVLDTv 85
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwsAAElarHRAYLSQQQsppFAMPVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 86 imgHkelwevkqerdriYALPEMSEEDGYKVADLevkygemdgysaeARAGELLLGVGIPVEQHYGpmsevapG-WKlRV 164
Cdd:COG4138 93 ---H-------------QPAGASSEAVEQLLAQL-------------AEALGLEDKLSRPLTQLSG-------GeWQ-RV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 165 LLAQALF-----ADPD--ILLLDEPTNNLDI------DtiRWLEQvLNERDSTMIIISHDrhfLNMVCTHmAD----LDY 227
Cdd:COG4138 136 RLAAVLLqvwptINPEgqLLLLDEPMNSLDVaqqaalD--RLLRE-LCQQGITVVMSSHD---LNHTLRH-ADrvwlLKQ 208
|
250
....*....|....*...
gi 1352184330 228 GELrVYPGNYDEYMTAAT 245
Cdd:COG4138 209 GKL-VASGETAEVMTPEN 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-251 |
1.18e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 32 LIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQD---QFA--FEEFTVLDTVIMGHKELWEVKQERDRIYALp 106
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrkLFSavFTDFHLFDQLLGPEGKPANPALVEKWLERL- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 107 EMS---EEDGYKVADLEVKYGEmdgysaearagelllgvgipveqhygpmsevapgwKLRVLLAQALFADPDILLLDEPT 183
Cdd:PRK10522 433 KMAhklELEDGRISNLKLSKGQ-----------------------------------KKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 184 NNLDIDTIRWLEQVL----NERDSTMIIISHDRHFLnmvctHMAD----LDYGELRVYPGnyDEYMTAATQARERL 251
Cdd:PRK10522 478 ADQDPHFRREFYQVLlpllQEMGKTIFAISHDDHYF-----IHADrlleMRNGQLSELTG--EERDAASRDAVART 546
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-211 |
1.27e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.93 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKlrqdqfafeeftvldtvimghKELWEVKQER 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID-GELLTA---------------------ENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 100 DRIYALPEmSEEDGYKVADlEVKYG-EMDGYSAE---ARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQALFADPD 175
Cdd:PRK13642 84 GMVFQNPD-NQFVGATVED-DVAFGmENQGIPREemiKRVDEALLAVNMLDFKTREP-ARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1352184330 176 ILLLDEPTNNLD----IDTIRWLEQVLNERDSTMIIISHD 211
Cdd:PRK13642 161 IIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
290-473 |
1.38e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 290 DKIKLEEVKASSRQNpfIRFEQDKklfRNALEVegltkgfdngplFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDL 369
Cdd:PTZ00265 373 DGKKLKDIKKIQFKN--VRFHYDT---RKDVEI------------YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 370 QPDSGTV-------------KWSEnARIGYYAQDhEYEFEND-----------LTVFEWMSQWKQEG-----DDEQAVRS 420
Cdd:PTZ00265 436 DPTEGDIiindshnlkdinlKWWR-SKIGVVSQD-PLLFSNSiknnikyslysLKDLEALSNYYNEDgndsqENKNKRNS 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 421 ILGRLLFSQDDIKKP------------------------------------------------AKVLSGGEKGRMLFGKL 452
Cdd:PTZ00265 514 CRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARA 593
|
250 260
....*....|....*....|.
gi 1352184330 453 MMQKPNILIMDEPTNHLDMES 473
Cdd:PTZ00265 594 IIRNPKILILDEATSSLDNKS 614
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-76 |
1.46e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLR---QDQFAF 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-RQSIKKDLctyQKQLCF 78
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-61 |
2.16e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 2.16e-04
10 20 30
....*....|....*....|....*....|.
gi 1352184330 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLD 61
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWD 59
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-485 |
2.22e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 5 SNVTMQF-GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERigklrqdQFAFEEFTVLD 83
Cdd:PRK10982 2 SNISKSFpGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-------DFKSSKEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 84 TVIMGHKELWEVKQER--DRI----YALPEMSEEDGYKVADLEVKYGEMD-GYSAEARAGELllgvgiPVEQHygPMSEV 156
Cdd:PRK10982 74 GISMVHQELNLVLQRSvmDNMwlgrYPTKGMFVDQDKMYRDTKAIFDELDiDIDPRAKVATL------SVSQM--QMIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 157 apgwklrvllAQALFADPDILLLDEPTNNLDIDTIRWLEQV---LNERDSTMIIISHDRHFLNMVCTHMADLDYGELrvy 233
Cdd:PRK10982 146 ----------AKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHKMEEIFQLCDEITILRDGQW--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 234 pgnydeymtAATQARERLLADnakkkaQIAEL---QSFVSRFSANASKSRQATsrarqidkikleevkassrqnpfirfe 310
Cdd:PRK10982 213 ---------IATQPLAGLTMD------KIIAMmvgRSLTQRFPDKENKPGEVI--------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 311 qdkklfrnaLEVEGLTKgfDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW------------ 378
Cdd:PRK10982 251 ---------LEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhgkkinnhnane 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 379 ----------SENARIGYYAQ-DHEY-----EFENDLTVFEWMSQWKQEGDDEQAVRSIlgrllfsqdDIKKPAK----- 437
Cdd:PRK10982 320 ainhgfalvtEERRSTGIYAYlDIGFnslisNIRNYKNKVGLLDNSRMKSDTQWVIDSM---------RVKTPGHrtqig 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1352184330 438 VLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESieslnmALELYQ 485
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA------KFEIYQ 432
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-266 |
3.11e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNER---IGKLRQDQFAFEEFTVLDTVIMGHKelwev 95
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaISSGLNGQLTGIENIELKGLMMGLT----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 96 KQERDRIyaLPEMSEedgykVADLevkygemdgysaearaGELLlgvgipveqhYGPMSEVAPGWKLRVLLAQALFADPD 175
Cdd:PRK13545 117 KEKIKEI--IPEIIE-----FADI----------------GKFI----------YQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 176 ILLLDEPTNNLDID-TIRWLEQV--LNERDSTMIIISHDRHFLNMVCTHMADLDYGELRVY------PGNYD----EYMT 242
Cdd:PRK13545 164 ILVIDEALSVGDQTfTKKCLDKMneFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYgdikevVDHYDeflkKYNQ 243
|
250 260
....*....|....*....|....
gi 1352184330 243 AATQARERLladnakKKAQIAELQ 266
Cdd:PRK13545 244 MSVEERKDF------REEQISQFQ 261
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-74 |
3.39e-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: 43.25 E-value: 3.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1352184330 32 LIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQF 74
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTADNREAY 404
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-231 |
3.58e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnerigklrqdqfafeeftvldtvimghkelwevkqerdriyalp 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 107 emseedgykvadlevKYGEMDGYSAEARAGELLLGVGIPVEQHYGPMsevapgwKLRVLLAQALFADPDILLLDEPTNNL 186
Cdd:smart00382 34 ---------------IYIDGEDILEEVLDQLLLIIVGGKKASGSGEL-------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1352184330 187 DIDTIRWLEQVLNERDSTMIIISHDRHFLnMVCTHMADLDYGELR 231
Cdd:smart00382 92 DAEQEALLLLLEELRLLLLLKSEKNLTVI-LTTNDEKDLGPALLR 135
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
439-526 |
3.88e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 439 LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMeSIES--LNMALELYQG---TLIFVSHDREFVSSLATRILEITPERV 513
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqiIELLLELQQKenmALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|...
gi 1352184330 514 IDfSGNYEDYLRS 526
Cdd:PRK11022 233 VE-TGKAHDIFRA 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
140-215 |
4.08e-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: 41.15 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 140 LGVG-IPVEQhygPMSEVAPGWKLRVLLAQALFADPD--ILLLDEPTNNLDIDTIRWLEQVLNE-RDS--TMIIISHDRH 213
Cdd:cd03238 74 VGLGyLTLGQ---KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLgnTVILIEHNLD 150
|
..
gi 1352184330 214 FL 215
Cdd:cd03238 151 VL 152
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
159-211 |
5.35e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 5.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLD-IDTIRwLEQVLNE--RDSTMIIISHD 211
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHElkEQYTIIIVTHN 209
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
287-376 |
5.56e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 287 RQIDKIKLEEVKAS-SRQNPFIRFEQdkklfrnaLEVEGLT-----KGFDNGPLfknlNLLLEVGEKLAVLGTNGVGKST 360
Cdd:PRK10522 297 NKLNKLALAPYKAEfPRPQAFPDWQT--------LELRNVTfayqdNGFSVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90
....*....|....*.
gi 1352184330 361 LLKTLVGDLQPDSGTV 376
Cdd:PRK10522 365 LAMLLTGLYQPQSGEI 380
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
331-473 |
7.01e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 331 NGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG--DLQPDSGTVKWSENARIGYYAQDHEYEFENDLTV--FEWMS 406
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMknVNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 407 QWKQEGD-DEQAVRSILGRLLF------------------------------------------SQDDIKKPAKV----- 438
Cdd:PTZ00265 1260 LTKEGGSgEDSTVFKNSGKILLdgvdicdynlkdlrnlfsivsqepmlfnmsiyenikfgkedaTREDVKRACKFaaide 1339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1352184330 439 -------------------LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES 473
Cdd:PTZ00265 1340 fieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-218 |
7.25e-04 |
|
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: 42.34 E-value: 7.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352184330 162 LRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE--------RDSTMIIISHDRHFLNMV 218
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiiksrsqqRNFQLLVITHDEDFVELL 1276
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-200 |
7.57e-04 |
|
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: 40.49 E-value: 7.57e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1352184330 163 RVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLNE 200
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
159-236 |
8.55e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLD--------IDTIRwLEQVLNerdSTMIIISHDRhflnMVCTHMAD----LD 226
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISR-LHKRLG---RTMIYVTHDQ----VEAMTLADkivvLD 208
|
90
....*....|....*....
gi 1352184330 227 YG---------ELRVYPGN 236
Cdd:PRK11000 209 AGrvaqvgkplELYHYPAN 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
411-509 |
8.68e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.31 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 EGD-DEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMES---IESLNMALElY 484
Cdd:PRK14243 121 KGDmDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELK-E 199
|
90 100
....*....|....*....|....*
gi 1352184330 485 QGTLIFVSHDREfvssLATRILEIT 509
Cdd:PRK14243 200 QYTIIIVTHNMQ----QAARVSDMT 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
331-529 |
1.05e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 331 NGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKWSenariGYYAQDheYEFENDLTVFEWMSQWKQ 410
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD-----GHDLRD--YTLASLRNQVALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 411 EGDDEQAVRSILGRL-LFSQDDIKKPAKV------------------------LSGGEKGRMLFGKLMMQKPNILIMDEP 465
Cdd:PRK11176 428 LFNDTIANNIAYARTeQYSREQIEEAARMayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 466 TNHLDMESIESLNMALELYQG--TLIFVSHDREFVSSlATRILEITPERVIDfSGNYEDYLRSKGI 529
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIVE-RGTHAELLAQNGV 571
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
159-210 |
1.06e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 159 GWKLRVLLAQALFADPDILLLDEPTNNLDIDTIR----WLEQVLNERDSTMIIISH 210
Cdd:PRK11144 132 GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSH 187
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
320-376 |
1.10e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG--DLQPDSGTV 376
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTV 60
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
320-526 |
1.21e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.17 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 320 LEVEGLTKGFdngplfKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTV-------------KWSENARIGY 386
Cdd:PRK10070 35 LEKTGLSLGV------KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 387 YAQDHEYEFENDLTVFE------WMSQWKQEGDDEQAVRSIlgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDntafgmELAGINAEERREKALDAL--RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352184330 461 IMDEPTNHLD----MESIESLNMALELYQGTLIFVSHDREFVSSLATRILEI---------TPERVIDFSGNyeDYLRS 526
Cdd:PRK10070 187 LMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqngevvqvgTPDEILNNPAN--DYVRT 263
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
439-521 |
1.33e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 439 LSGGEKGRMLFGKLMMQKPNILIMDEPTNHLDMESiESLNMALEL----YQGTLIFVSHDREFVSSLATRILEITPERVI 514
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG-EHEMMQLILdakaNNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....*..
gi 1352184330 515 DFSGNYE 521
Cdd:PRK13631 256 KTGTPYE 262
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
434-524 |
1.60e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 434 KPAKVLSGGEKGRM-LFGKLM--MQKPNILIMDEPTNHLDMESIESLNMALE--LYQG-TLIFVSHDREFVsSLATRILE 507
Cdd:PRK00635 805 RPLSSLSGGEIQRLkLAYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQslTHQGhTVVIIEHNMHVV-KVADYVLE 883
|
90
....*....|....*..
gi 1352184330 508 ITPErvidfSGNYEDYL 524
Cdd:PRK00635 884 LGPE-----GGNLGGYL 895
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
1.75e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 1 MLVSSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNV--------SLDPNER--IGK 68
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIlfkgesilDLEPEERahLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 69 LRQDQFAFEeftvldtvIMGHKE---LWEVKQERDRIYALPEMSEEDGYKVADLEVKYGEMDGYSAEARAGELLLGvgip 145
Cdd:CHL00131 87 FLAFQYPIE--------IPGVSNadfLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSG---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352184330 146 veqhygpmsevapGWKLRVLLAQALFADPDILLLDEPTNNLDIDTIRWLEQVLN---ERDSTMIIISHDRHFLNMV 218
Cdd:CHL00131 155 -------------GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINklmTSENSIILITHYQRLLDYI 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-188 |
1.83e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 1.83e-03
10 20
....*....|....*....|....*
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDI 188
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
319-466 |
2.83e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 319 ALEVEGLTKGFDNgplF---KNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVGDLQPDSGTVKW---SENA-------RIG 385
Cdd:NF033858 266 AIEARGLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqPVDAgdiatrrRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 386 YYAQdheyEFE--NDLTVfewmsqwKQ------------EGDDEQAVRSILGRllFS-QDDIKKPAKVLSGGEKGRMLFG 450
Cdd:NF033858 343 YMSQ----AFSlyGELTV-------RQnlelharlfhlpAAEIAARVAEMLER--FDlADVADALPDSLPLGIRQRLSLA 409
|
170
....*....|....*.
gi 1352184330 451 KLMMQKPNILIMDEPT 466
Cdd:NF033858 410 VAVIHKPELLILDEPT 425
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
320-367 |
2.96e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1352184330 320 LEVEGLTKGFDNGPLFKNLNLLLEVGEKLAVLGTNGVGKSTLLKTLVG 367
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
130-230 |
3.43e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.30 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 130 SAEARAGELLLGVGIP----VEQHYgPMsEVAPGWKLRVLLAQALFADPDILLLDEPTNNLDI----DTIRWLEQVLNER 201
Cdd:PRK10418 113 ADDATLTAALEAVGLEnaarVLKLY-PF-EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKR 190
|
90 100
....*....|....*....|....*....
gi 1352184330 202 DSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10418 191 ALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
3.43e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.43e-03
10 20
....*....|....*....|....*
gi 1352184330 164 VLLAQALFADPDILLLDEPTNNLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-221 |
4.18e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMK----ILGGDLEPTlgnvsldpNERIGKLRQDQFAFEEFTvldtvimgh 89
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSAT--------RRRSGVKAGCIVAAVSAE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184330 90 kelwevkqerdRIYALPEMSeedgykvadlevkygemdgysaearagelllgvgipveqhyGPMSEVApgwKLRVLLAQA 169
Cdd:cd03227 71 -----------LIFTRLQLS-----------------------------------------GGEKELS---ALALILALA 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352184330 170 LFADPDILLLDEPTNNLDIDTIRWLEQVLNER---DSTMIIISHD-------RHFLNMVCTH 221
Cdd:cd03227 96 SLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLpelaelaDKLIHIKKVI 157
|
|
| |
