|
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: 1233.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGHAELWEVKQERDRIYALAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 241 MTAATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRQNPFIRFEQDKKLFRNAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFENDLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 VFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMA 480
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 695729787 481 LEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLRSKGID 530
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-525 |
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: 764.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 TVIMGHAELWEVKQERDRIYALAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLR 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMTA 243
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 244 ATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRqNPFIRFEQDKKLFRNALEVE 323
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 324 ALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyEFENDLTVFD 403
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-ELDPDKTVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 404 WMSQWKqEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEM 483
Cdd:COG0488 399 ELRDGA-PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD 477
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 695729787 484 YQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLR 525
Cdd:COG0488 478 FPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-523 |
1.35e-96 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 306.33 E-value: 1.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEfT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGHAELWEVKQErdriyaLAEMSEE-DGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 160 WKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYD- 238
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 239 -EYMTAATQARERLLADNAKKKaqIADLQSFVSRFSANASKSRQATSRARQIDKIKLeeVKASSRQNPF-IRFEQDKKLF 316
Cdd:PRK10636 234 fEVQRATRLAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdHEYEF- 395
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ-HQLEFl 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 ENDLTVFDWMSQWKQEgDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIE 475
Cdd:PRK10636 389 RADESPLQHLARLAPQ-ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 695729787 476 SLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDY 523
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-522 |
1.06e-95 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 303.80 E-value: 1.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDT 84
Cdd:PRK11147 7 HGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 VIMGHAELWEVKQERDRIYALAE--MSEEDGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQhygPMSEVAPGWKL 162
Cdd:PRK11147 87 VAEGIEEQAEYLKRYHDISHLVEtdPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMT 242
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 243 AATQAReRLLAD-NA---KKKAQ----IAdlQSFVSRFSAN-----ASKS-RQATSRARQID---KIKLEEVKASSRqnp 305
Cdd:PRK11147 244 EKEEAL-RVEELqNAefdRKLAQeevwIR--QGIKARRTRNegrvrALKAlRRERSERREVMgtaKMQVEEASRSGK--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 306 fIRFeqdkklfrnalEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIG 385
Cdd:PRK11147 318 -IVF-----------EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQdHEYEFENDLTVFDWMSQWKQE----GDDeqavRSILGRL---LFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPN 458
Cdd:PRK11147 386 YFDQ-HRAELDPEKTVMDNLAEGKQEvmvnGRP----RHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 459 ILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVD-FTGNYED 522
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIGrYVGGYHD 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-523 |
6.01e-91 |
|
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: 288.76 E-value: 6.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDTVIMGHAE 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 92 LWEVKQERDRIYALaeMSEED------GYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQhyGPMSEVAPGWKLRVL 165
Cdd:TIGR03719 96 IKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKLSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 166 LAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMtaaT 245
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL---E 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 246 QARERLL----ADNAKKKAQIADLQsfvsrFSANASKSRQATSRARQidkIKLEEV--KASSRQNPF--IRFEQDKKLFR 317
Cdd:TIGR03719 249 QKQKRLEqeekEESARQKTLKRELE-----WVRQSPKGRQAKSKARL---ARYEELlsQEFQKRNETaeIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyEFEN 397
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD-ALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 DLTVFDWMSqwkqEGDDEQAV-------RSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:TIGR03719 400 NKTVWEEIS----GGLDIIKLgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 471 MESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPE-RVVDFTGNYEDY 523
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-523 |
6.25e-87 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 278.54 E-value: 6.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEEFTVLDTVIMGHAE 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 92 LWEVKQERDRIYAlaEMSEEDGY------KVAELETQYGEMDGYSAEARagelllgvgipVEQHY---------GPMSEV 156
Cdd:PRK11819 98 VKAALDRFNEIYA--AYAEPDADfdalaaEQGELQEIIDAADAWDLDSQ-----------LEIAMdalrcppwdAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGN 236
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 237 YDEYMtaaTQARERLL----ADNAKKKAqIADLQSFVsRFSAnasKSRQATSRARqidkIK-LEEV--KASSRQNPF--I 307
Cdd:PRK11819 245 YSSWL---EQKAKRLAqeekQEAARQKA-LKRELEWV-RQSP---KARQAKSKAR----LArYEELlsEEYQKRNETneI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 308 RFEQDKKLFRNALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYY 387
Cdd:PRK11819 313 FIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEyEFENDLTVFDWMSqwkqEGDD-------EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:PRK11819 393 DQSRD-ALDPNKTVWEEIS----GGLDiikvgnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 461 VMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPE-RVVDFTGNYEDY 523
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQVEWFEGNFQEY 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-525 |
7.11e-83 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 272.12 E-value: 7.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGgdLEPTLGnvsLDPNERIGKLRQDQFAfEEFTVLDTV 85
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQEVVG-DDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 IMGHAELWEVKQERDRIYALAEMSEEDGY-------------------KVAELETQYGEMDGYSAEARAGELLLGVGIPV 146
Cdd:PLN03073 256 LNTDIERTQLLEEEAQLVAQQRELEFETEtgkgkgankdgvdkdavsqRLEEIYKRLELIDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 EQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 227 YGELRVYPGNYDEY-MTAATQARERLLADNAKKKAQiADLQSFVSRFSANASKSRQATSRARQIDKIK-LEEVKassrQN 304
Cdd:PLN03073 416 GQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLGhVDAVV----ND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 305 PFIRFE---QDKKLFRNALEVEALTKGFDEGP-LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE 380
Cdd:PLN03073 491 PDYKFEfptPDDRPGPPIISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 381 NAQIGYYAQDHEYEFENDLTVFDWMSQWkQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:PLN03073 571 KVRMAVFSQHHVDGLDLSSNPLLYMMRC-FPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 461 VMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLR 525
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-512 |
1.39e-58 |
|
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: 191.12 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdheyefendl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 tvfdwmsqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNM 479
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 695729787 480 ALEMYQGTLIFVSHDREFVSSLATRVIEITPER 512
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-527 |
2.49e-58 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 202.22 E-value: 2.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 322 VEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyeFENDLTV 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP--LDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 FDW---------------------MSQWKQEGDD----------------EQAVRSILGRLLFSQDDIKKPAKVLSGGEK 444
Cdd:COG0488 79 LDTvldgdaelraleaeleeleakLAEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 445 GRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYL 524
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
...
gi 695729787 525 RSK 527
Cdd:COG0488 239 EQR 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-241 |
1.64e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 172.56 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAF-EEF 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELdPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 TVLDtvimghaELWEVKQERDRIYA---LAEM--SEEDGYK-VAELetqygemdgySaearAGElllgvgipveqhygpm 153
Cdd:COG0488 395 TVLD-------ELRDGAPGGTEQEVrgyLGRFlfSGDDAFKpVGVL----------S----GGE---------------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 154 sevapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:COG0488 438 -------KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
....*...
gi 695729787 234 PGNYDEYM 241
Cdd:COG0488 511 PGGYDDYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-229 |
1.86e-45 |
|
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: 156.45 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQdqfafeeftvldt 84
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 vimghaelwevkqerdriyalaemseedgykvaeletqygemdgysaearagelllgvgipveqhygpMSevaPGWKLRV 164
Cdd:cd03221 71 --------------------------------------------------------------------LS---GGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-506 |
1.78e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 127.47 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA---QIGYY 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYEFenDLTVFD--------WMSQWKQEG-DDEQAVRSILGRLlfsqdDIK----KPAKVLSGGEKGRMLFGKLMM 454
Cdd:COG1120 81 PQEPPAPF--GLTVRElvalgrypHLGLFGRPSaEDREAVEEALERT-----GLEhladRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 455 EKPNILVMDEPTNHLD-------MESIESLNmalEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqlevLELLRRLA---RERGRTVVMVLHDLNLAARYADRLV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-506 |
3.39e-33 |
|
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: 132.33 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTL---GNVSLDPNE----------- 64
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDllelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 65 RIGKLRQDQFafeefTVLDTVIMGHAelwevkqerdriyaLAEMSEEDGYKVAEletqygemdgysAEARAGELLLGVGI 144
Cdd:COG1123 84 RIGMVFQDPM-----TQLNPVTVGDQ--------------IAEALENLGLSRAE------------ARARVLELLEAVGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 145 PVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHDRHFLNM 217
Cdd:COG1123 133 ERRLDRYP-HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqaeiLDLLRELQR---ERGTTVLLITHDLGVVAE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 218 VCTHMADLDYGELrvypgnydeymtAATQARERLLADNAKKKAqiadlqsfVSRFSANASKSRQATSRARQIdkikleev 297
Cdd:COG1123 209 IADRVVVMDDGRI------------VEDGPPEEILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL-------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 298 kassrqnpfirfeqdkklfrnaLEVEALTKGFDEG-----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPD 372
Cdd:COG1123 261 ----------------------LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 373 NGTV--------KWSENA------QIGYYAQDHEYEFENDLTVFDWMSQ------WKQEGDDEQAVRSILGRLLFSQDDI 432
Cdd:COG1123 319 SGSIlfdgkdltKLSRRSlrelrrRVQMVFQDPYSSLNPRMTVGDIIAEplrlhgLLSRAERRERVAELLERVGLPPDLA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 433 KKPAKVLSGGEK-----GRMlfgkLMMEkPNILVMDEPTNHLD-------MESIESLNmalEMYQGTLIFVSHDREFVSS 500
Cdd:COG1123 399 DRYPHELSGGQRqrvaiARA----LALE-PKLLILDEPTSALDvsvqaqiLNLLRDLQ---RELGLTYLFISHDLAVVRY 470
|
....*.
gi 695729787 501 LATRVI 506
Cdd:COG1123 471 IADRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
5.82e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 126.31 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVLDTVIMG---HAELWEVKQERDR--IY-ALAEMSeedgykVAELETQ-YGEMDGysaearaGELllgv 142
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFGRPSAEDReaVEeALERTG------LEHLADRpVDELSG-------GER---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 143 gipveQhygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNM- 217
Cdd:COG1120 144 -----Q--------------RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNLa 201
|
250 260 270
....*....|....*....|....*....|
gi 695729787 218 --VCTHMADLDYGELRVYpGNYDEYMTAAT 245
Cdd:COG1120 202 arYADRLVLLKDGRIVAQ-GPPEEVLTPEL 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-526 |
1.06e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENAQIGYYAQDHE 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 393 yeFEND--LTVFDW--MSQWKQEG-------DDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:COG1121 86 --VDWDfpITVRDVvlMGRYGRRGlfrrpsrADREAVDEALERVgL--EDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 461 VMDEPTNHLDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVvdFTGNYEDYLRS 526
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTP 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-513 |
5.10e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QdheyefENDL---TVFDWMS---QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:COG4619 81 Q------EPALwggTVRDNLPfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 463 DEPTNHLDMES---IESL-NMALEMYQGTLIFVSHDREFVSSLATRVIEITPERV 513
Cdd:COG4619 155 DEPTSALDPENtrrVEELlREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-508 |
4.90e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQIGYYAQDHEYE 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 FENDLTVFDW--MSQWKQEG-------DDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDE 464
Cdd:cd03235 81 RDFPISVRDVvlMGLYGHKGlfrrlskADKAKVDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695729787 465 PTNHLDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-239 |
9.37e-31 |
|
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: 119.96 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----------PNERIGKLR 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 QDQFAFEEFTVLDtVIMGHAELWEVKqerdriyalaemSEEDGYKVAELETQYGeMDGYsAEARAGELllgvgipveqhy 150
Cdd:COG4555 81 DERGLYDRLTVRE-NIRYFAELYGLF------------DEELKKRIEELIELLG-LEEF-LDRRVGEL------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 151 gpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:COG4555 134 ------STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
250
....*....|..
gi 695729787 228 GELrVYPGNYDE 239
Cdd:COG4555 208 GKV-VAQGSLDE 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-512 |
1.07e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 118.35 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW----SENAQIGYYAQ----DH 391
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepIRDAREDYRRRlaylGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLTVFD----WMSQWKQEGDDEQAVRSI----LGRLLfsqddiKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:COG4133 83 ADGLKPELTVREnlrfWAALYGLRADREAIDEALeavgLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 464 EPTNHLDMESIESLNMALEMY---QGTLIFVSHDREFVssLATRVIEITPER 512
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
1.37e-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: 117.11 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNE-------RIGKLRQ 71
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkDIKKepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVImghaelwevkqerdriyalaemseedgykvaeletqygemdgYSAearagelllgvgipveqhyg 151
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------------LSG-------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 pmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:cd03230 99 -------GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
..
gi 695729787 229 EL 230
Cdd:cd03230 172 RI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
4.23e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQdQF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 AFEE---FTVLDTVIMG---HAELWEV--KQERDRIY-ALAEMseedgyKVAELE-TQYGEMDGysaearaGELllgvgi 144
Cdd:COG1121 85 EVDWdfpITVRDVVLMGrygRRGLFRRpsRADREAVDeALERV------GLEDLAdRPIGELSG-------GQQ------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 145 pveQhygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDrhfLNMV--- 218
Cdd:COG1121 146 ---Q--------------RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHD---LGAVrey 205
|
250 260 270
....*....|....*....|....*....|
gi 695729787 219 CTHMADLDYGelRVYPGNYDEYMTAATQAR 248
Cdd:COG1121 206 FDRVLLLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
9.14e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.09 E-value: 9.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP------NERIGKLRQdQFAFE- 77
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 78 EF--TVLDTVIMGhaeLWEvkqerdRIYALAEMSEEDGYKVAE-LETqyGEMDGYsAEARAGELllgvgipveqhygpms 154
Cdd:cd03235 82 DFpiSVRDVVLMG---LYG------HKGLFRRLSKADKAKVDEaLER--VGLSEL-ADRQIGEL---------------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 155 evAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLNDRDSTMIIISHDrhfLNMVCTH 221
Cdd:cd03235 134 --SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHD---LGLVLEY 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
3.29e-29 |
|
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: 114.50 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA----- 75
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRRrlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 ------FEEFTVLDTVIMgHAELWEVKQERDRIY-ALAEMSeedgykVAELETQYGEMdgYSAearagelllgvgipveq 148
Cdd:COG4133 81 ghadglKPELTVRENLRF-WAALYGLRADREAIDeALEAVG------LAGLADLPVRQ--LSA----------------- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 149 hygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFL 215
Cdd:COG4133 135 ----------GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhlaRGGAVLLTTHQPLEL 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-527 |
5.43e-29 |
|
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: 120.43 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdhEYEFENDLTV----------- 401
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ--EPQLDPTKTVrenveegvaei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 ------FDWMS-QWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLSGGEKGRMLFG 450
Cdd:TIGR03719 97 kdaldrFNEISaKYAEPDADFDKLAAEQAEL---QEIIDaadawdldsqleiamdalrcppwdADVTKLSGGERRRVALC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 451 KLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLRSK 527
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 250
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
328-527 |
6.62e-29 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 120.83 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 328 GFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFENdlTVFDWMSQ 407
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEG--TVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 408 WKQE-GDDEQAVRSILGRLLFSQDD--IKKPAKV---------------------------------LSGGEKGRMLFGK 451
Cdd:PRK11147 90 GIEEqAEYLKRYHDISHLVETDPSEknLNELAKLqeqldhhnlwqlenrinevlaqlgldpdaalssLSGGWLRKAALGR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 452 LMMEKPNILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLRSK 527
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEK 245
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
1.44e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 113.62 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----------PNERIGKLRQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMgHAELWEV--KQERDRIYALAEMseedgykvAELETQygemdgysAEARAGELLLgvgipveqh 149
Cdd:COG1131 81 EPALYPDLTVRENLRF-FARLYGLprKEARERIDELLEL--------FGLTDA--------ADRKVGTLSG--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 150 ygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:COG1131 135 ---------GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
....
gi 695729787 227 YGEL 230
Cdd:COG1131 206 KGRI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-508 |
1.60e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 111.34 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ----IGYYAQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEEvkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 dhEYEFENDLTVFDWMSqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHL 469
Cdd:cd03230 81 --EPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695729787 470 DMESIESLNMALEMY---QGTLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03230 127 DPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
6.16e-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: 109.26 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRqdqfafeeftvldt 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 vimghaelweVKQERDRIYALAEMSeedgykvaeletqygemdgysaearagelllgvgipveqhygpmsevaPGWKLRV 164
Cdd:cd00267 68 ----------LEELRRRIGYVPQLS------------------------------------------------GGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-525 |
1.81e-27 |
|
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: 115.67 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNV------------------------- 58
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 59 ---SLDPNE----------------RIGKLRQDQFA-FEEFTVLDTVImghaelwevkqerdriyalaEMSEEDGYKvae 118
Cdd:TIGR03269 85 cggTLEPEEvdfwnlsdklrrrirkRIAIMLQRTFAlYGDDTVLDNVL--------------------EALEEIGYE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 119 letqygemdGYSAEARAGELLLGVGIpveQHYgpMSEVAP----GWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRW- 193
Cdd:TIGR03269 142 ---------GKEAVGRAVDLIEMVQL---SHR--ITHIARdlsgGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLv 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 194 ---LEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEymtaatqarerlladnakkkaqiadlqsFVS 270
Cdd:TIGR03269 208 hnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI-KEEGTPDE----------------------------VVA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 271 RFSANASKSRQATSRARQIDKIKLEEVKASsrqnpFIRFEQdkklfrnaleveALTKGFDegplfknfNLLLEV--GEKI 348
Cdd:TIGR03269 259 VFMEGVSEVEKECEVEVGEPIIKVRNVSKR-----YISVDR------------GVVKAVD--------NVSLEVkeGEIF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 349 AILGANGVGKSTMLKTLVGELQPDNGTV------KWSENAQIG---------YYAQDH-EY------------------E 394
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGpdgrgrakrYIGILHqEYdlyphrtvldnlteaiglE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 FENDLTVFDWMSQWKQEGDDEQAVRSILGRLlfsqddikkPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD---- 470
Cdd:TIGR03269 394 LPDELARMKAVITLKMVGFDEEKAEEILDKY---------PDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitk 463
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 471 ---MESIesLNMALEMYQgTLIFVSHDREFVSSLATRVIEITPERVVDfTGNYEDYLR 525
Cdd:TIGR03269 464 vdvTHSI--LKAREEMEQ-TFIIVSHDMDFVLDVCDRAALMRDGKIVK-IGDPEEIVE 517
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-467 |
4.15e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 106.58 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDHeyEFENDLTVFD 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 404 ------WMSQWKQEGDDEQA--VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:pfam00005 79 nlrlglLLKGLSKREKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-527 |
5.48e-27 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 114.45 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdhEYEFENDLTV----------- 401
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ--EPQLDPEKTVrenveegvaev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 ------FDWMS-QWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLSGGEKGRMLFG 450
Cdd:PRK11819 99 kaaldrFNEIYaAYAEPDADFDALAAEQGEL---QEIIDaadawdldsqleiamdalrcppwdAKVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 451 KLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLRSK 527
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-240 |
3.43e-26 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 112.34 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpneRIGklrqdqfafeeftvlDTV 85
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------EIG---------------ETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 IMGHaelweVKQERDRIyalaemseeDGYKvaeleTQYGEMDGYSAEARAGelllGVGIPVEQHYG-----------PMS 154
Cdd:TIGR03719 386 KLAY-----VDQSRDAL---------DPNK-----TVWEEISGGLDIIKLG----KREIPSRAYVGrfnfkgsdqqkKVG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMadLDY-GELRV- 232
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFeGDSHVe 520
|
....*....
gi 695729787 233 -YPGNYDEY 240
Cdd:TIGR03719 521 wFEGNFSEY 529
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-508 |
5.18e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 103.86 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEnaqigyyaqdheyefendlt 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 vfdwmsQWKQEGDDEQAVRSILgrLLFSqddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESL-NM 479
Cdd:cd00267 61 ------KDIAKLPLEELRRRIG--YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlEL 122
|
170 180 190
....*....|....*....|....*....|.
gi 695729787 480 ALEMYQG--TLIFVSHDREFVSSLATRVIEI 508
Cdd:cd00267 123 LRELAEEgrTVIIVTHDPELAELAADRVIVL 153
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-506 |
6.38e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 106.10 E-value: 6.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE----------NAQIGYYAQ 389
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkepreaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHE-YEFendLTVFDWM----SQWKQEGDD-EQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:COG4555 82 ERGlYDR---LTVRENIryfaELYGLFDEElKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 464 EPTNHLDMESIESL-NMALEMYQ--GTLIFVSHDREFVSSLATRVI 506
Cdd:COG4555 158 EPTNGLDVMARRLLrEILRALKKegKTVLFSSHIMQEVEALCDRVV 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-528 |
6.72e-26 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 111.80 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 334 LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQ----------------DHEY-EFE 396
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQetpalpqpaleyvidgDREYrQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 NDLtvfdwmsQWKQEGDDEQAVRSILGRLL-------------------FSQDDIKKPAKVLSGGEKGRMLFGKLMMEKP 457
Cdd:PRK10636 96 AQL-------HDANERNDGHAIATIHGKLDaidawtirsraasllhglgFSNEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 458 NILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYEDYLRSKG 528
Cdd:PRK10636 169 DLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-241 |
1.06e-25 |
|
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: 111.46 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNE---RIGKLRQ 71
Cdd:COG2274 477 ENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEfTVLDTVIMGHAELwevkqERDRIYALAEMSE--------EDGYkvaelETQYGEMdgysaearagelllGVG 143
Cdd:COG2274 557 DVFLFSG-TIRENITLGDPDA-----TDEEIIEAARLAGlhdfiealPMGY-----DTVVGEG--------------GSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 144 IPVEQhygpmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNmvcth 221
Cdd:COG2274 612 LSGGQ------------RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR----- 674
|
250 260
....*....|....*....|....
gi 695729787 222 MAD----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 ... |
321-508 |
1.17e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 104.47 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYY 387
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYEFENDlTVFD----WMSQWKQEGDD-EQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:cd03225 81 FQNPDDQFFGP-TVEEevafGLENLGLPEEEiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 463 DEPTNHLDMESIESLnmaLEMYQG------TLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03225 159 DEPTAGLDPAGRREL---LELLKKlkaegkTIIIVTHDLDLLLELADRVIVL 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-506 |
4.94e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 103.60 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ----IGYYAQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHeyEFENDLTVFDWMSQWKQ-----EGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:COG1131 81 EP--ALYPDLTVRENLRFFARlyglpRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 464 EPTNHLDMESIESLNMALEMY--QGTLIFVS-HDREFVSSLATRVI 506
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
6.26e-25 |
|
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: 103.29 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 -------FEEFTVLDTVIMGHAElwevkQERDRIYALAEMSEEDgykvaeletqygemdgySAEARAGELLLGVGIpveQ 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVAAQA-----RTGSGLLLARARREER-----------------EARERAEELLERVGL---A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 149 HYG--PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQtLNDRDSTMIIISHDRHFLNMVCTHM 222
Cdd:cd03219 135 DLAdrPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeeteELAELIRE-LRERGITVLLVEHDMDVVMSLADRV 213
|
....*...
gi 695729787 223 ADLDYGEL 230
Cdd:cd03219 214 TVLDQGRV 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
7.35e-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: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----PNERIGKLRQ----- 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 -----DQFaFEEfTVLDtvimghaelwEVkqerdrIYALAEMseedGYKVAEletqygemdgysAEARAGELLLGVGIpv 146
Cdd:COG1122 81 fqnpdDQL-FAP-TVEE----------DV------AFGPENL----GLPREE------------IRERVEEALELVGL-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 eQHYGpmsEVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFLNMV 218
Cdd:COG1122 125 -EHLA---DRPPhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLVAEL 200
|
250
....*....|..
gi 695729787 219 CTHMADLDYGEL 230
Cdd:COG1122 201 ADRVIVLDDGRI 212
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
9.78e-25 |
|
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: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 223 ADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDkiKLEEVKASSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALE--KMERIEKPER 78
|
....*..
gi 695729787 303 QNPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
1.41e-24 |
|
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: 102.81 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGS-KPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 ---------FEEFTVLDTVIMGHaelwevkQERDRIYALAEMSEEDGYKVAELEtqygemdgysAEARAGELLLGVGIpv 146
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAA-------HARLGRGLLAALLRLPRARREERE----------ARERAEELLERVGL-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 eQHYG--PMSEVAPGWKLRVLLAQALFSNPDILLLDEP--------TNNLdIDTIRWLEQtlnDRDSTMIIISHDRHFLN 216
Cdd:COG0411 143 -ADRAdePAGNLSYGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRD---ERGITILLIEHDMDLVM 217
|
250
....*....|....
gi 695729787 217 MVCTHMADLDYGEL 230
Cdd:COG0411 218 GLADRIVVLDFGRV 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-231 |
3.79e-24 |
|
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: 100.37 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD---------PNERIGKLRQD 72
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksyqknieALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEEFTVLDTVIMGHAELWEVKQERDRIYALAEMSEEDGYKVAeletqygemdGYSaearagellLGvgipveqhygp 152
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVK----------GFS---------LG----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 153 MsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03268 131 M-------KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
..
gi 695729787 230 LR 231
Cdd:cd03268 204 LI 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
7.36e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 100.27 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQIGYYAQDHE-- 392
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSEAELYRLRRRmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 393 YEFE-----NDLTVFD----WMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILV 461
Cdd:cd03261 81 MLFQsgalfDSLTVFEnvafPLREHTRLSEEEirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 462 MDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVVdFTGNYEDYLRS 526
Cdd:cd03261 160 YDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-506 |
7.72e-24 |
|
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: 99.25 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEGP-LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--------AQIGYYAQDH 391
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDlTVFDWMS-QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:cd03226 81 DYQLFTD-SVREELLlGLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 695729787 471 MESIESLNMALE--MYQGTLIFV-SHDREFVSSLATRVI 506
Cdd:cd03226 159 YKNMERVGELIRelAAQGKAVIViTHDYEFLAKVCDRVL 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
316-529 |
1.40e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 104.92 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 316 FRNALEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN-----------A 382
Cdd:COG2274 470 LKGDIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 383 QIGYYAQDheyefeNDL---TVFDWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGRML 448
Cdd:COG2274 550 QIGVVLQD------VFLfsgTIRENITLGDPDATDEEIIEAA--RLAGLHDFIEAlPmgydtvvgegGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 449 FGKLMMEKPNILVMDEPTNHLDMES----IESLNmalEMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfTGNYEDY 523
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETeaiiLENLR---RLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEEL 696
|
....*.
gi 695729787 524 LRSKGI 529
Cdd:COG2274 697 LARKGL 702
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-210 |
2.04e-23 |
|
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: 99.39 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNvsldpnerigklrqdqfafeEFTVLDTV 85
Cdd:COG1119 8 NVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN--------------------DVRLFGER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 iMGHAELWEVKQerdRI-YALAEMSE--------ED-----GYKVAELETQYGEMDgysaEARAGELL--LGVGIPVEQH 149
Cdd:COG1119 68 -RGGEDVWELRK---RIgLVSPALQLrfprdetvLDvvlsgFFDSIGLYREPTDEQ----RERARELLelLGLAHLADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 150 YGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISH 210
Cdd:COG1119 140 FGTLSQ---GEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-506 |
3.29e-23 |
|
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: 96.74 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWS--ENAQ-IGYYAQ 389
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSpkELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 dheyefendltvfdWMSQWKqegddeqaVRSILGRLLFSqddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHL 469
Cdd:cd03214 81 --------------ALELLG--------LAHLADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695729787 470 D-------MESIESLNmalEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:cd03214 129 DiahqielLELLRRLA---RERGKTVVMVLHDLNLAARYADRVI 169
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
3.89e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 11 FGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQ-----DQFAFeefTVLDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPL---TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 IMG---HAELWEVKQERDRIyALAEMSEEDGykVAELETQygemdgysaearagelllgvgipveqhygPMSEVAPGWKL 162
Cdd:NF040873 79 AMGrwaRRGLWRRLTRDDRA-AVDDALERVG--LADLAGR-----------------------------QLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRH 213
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAeehARGATVVVVTHDLE 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
4.78e-23 |
|
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: 97.15 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE----RIGKLRQ----------DQFAFE 77
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklSLKELRRkvglvfqnpdDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 78 efTVLDTVIMGhAELWEVKQErdriyalaemseedgykvaeletqygEMdgysaEARAGELLLGVGIPVEQHYGP--MSE 155
Cdd:cd03225 92 --TVEEEVAFG-LENLGLPEE--------------------------EI-----EERVEEALELVGLEGLRDRSPftLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 156 vapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03225 138 ---GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
1.42e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.02 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGS----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLR 70
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 QDQFAF--------EEFTVLDTVIMGhAELWEVKQErdriyalaemseedgykvaeletqygemdgySAEARAGELLLGV 142
Cdd:cd03255 81 RRHIGFvfqsfnllPDLTALENVELP-LLLAGVPKK-------------------------------ERRERAEELLERV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 143 GIPVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDR 212
Cdd:cd03255 129 GLGDRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
1.92e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 328 GFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFENDLTVFDW--M 405
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLvaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 406 SQWKQEG-------DDEQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLN 478
Cdd:NF040873 81 GRWARRGlwrrltrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|.
gi 695729787 479 --MALEMYQG-TLIFVSHDREFVSSlATRVI 506
Cdd:NF040873 160 alLAEEHARGaTVVVVTHDLELVRR-ADPCV 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-506 |
2.23e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 94.21 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA---QIGY 386
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQDHEyefendltvfdwmsqwkqegddeqavrsilgrlLFS---QDDIkkpakvLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:cd03246 81 LPQDDE---------------------------------LFSgsiAENI------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 464 EPTNHLDMESIESLNMA---LEMYQGTLIFVSHDREFVSSlATRVI 506
Cdd:cd03246 122 EPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLAS-ADRIL 166
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-506 |
3.53e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 93.79 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------------ENAQIGY 386
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQDHeyefendlTVFDWMSqwkqegddeqaVRSILgrllfsqddikkpAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:cd03229 81 VFQDF--------ALFPHLT-----------VLENI-------------ALGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695729787 467 NHLDMESIESLNMAL----EMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:cd03229 129 SALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-508 |
3.81e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 94.86 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSE------- 380
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 381 NAQIGYYAQDHEYefENDLTVFD-----WMSQWKQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMM 454
Cdd:cd03255 81 RRHIGFVFQSFNL--LPDLTALEnvelpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 455 EKPNILVMDEPTNHLD-------MESIESLNmalEMYQGTLIFVSHDREFVsSLATRVIEI 508
Cdd:cd03255 157 NDPKIILADEPTGNLDsetgkevMELLRELN---KEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-259 |
7.49e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 99.04 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpneRIGklrqdqfafeeftvlDTV 85
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI------KIG---------------ETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 IMGHaelweVKQERDRIyalaemseeDGYKvaeleTQYGEMDGysaearaGELLLGVG---IPVEQHYG----------- 151
Cdd:PRK11819 388 KLAY-----VDQSRDAL---------DPNK-----TVWEEISG-------GLDIIKVGnreIPSRAYVGrfnfkggdqqk 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMadLDY-GEL 230
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFeGDS 519
|
250 260 270
....*....|....*....|....*....|.
gi 695729787 231 RV--YPGNYDEYmtaATQARERLLADNAKKK 259
Cdd:PRK11819 520 QVewFEGNFQEY---EEDKKRRLGADAARPH 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-506 |
7.54e-22 |
|
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: 94.32 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENA-----QIGYY 387
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYEFENDlTVFDWMS----QWKQEGDD-EQAVRSILGRLlfsqdDI----KKPAKVLSGGEKGRM-LFGKLMMEkP 457
Cdd:COG1122 81 FQNPDDQLFAP-TVEEDVAfgpeNLGLPREEiRERVEEALELV-----GLehlaDRPPHELSGGQKQRVaIAGVLAME-P 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 458 NILVMDEPTNHLDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVI 506
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVI 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
1.43e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.96 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKLRQDQfafeeftvldtv 85
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-----GKPLSAM------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 imgHAELWevkqeRDRI-YALAEMSEEDGyKVAE-LETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLR 163
Cdd:COG4619 68 ---PPPEW-----RRQVaYVPQEPALWGG-TVRDnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:COG4619 139 LALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-528 |
2.42e-21 |
|
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: 97.53 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIG 385
Cdd:COG4987 333 SLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQDHeYEF-----ENdLTVFdwmsqwKQEGDDEQAVRSI----LGRLLFSQddikkPAKV----------LSGGEKGR 446
Cdd:COG4987 413 VVPQRP-HLFdttlrEN-LRLA------RPDATDEELWAALervgLGDWLAAL-----PDGLdtwlgeggrrLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 447 MLFGKLMMEKPNILVMDEPTNHLDMESIESLnMA--LEMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfTGNYEDY 523
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQAL-LAdlLEALAGrTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEEL 556
|
....*
gi 695729787 524 LRSKG 528
Cdd:COG4987 557 LAQNG 561
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-514 |
2.74e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.02 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--------------AQI 384
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 GYYAQDHE-----YEFENDLT-VFDWMSQWKQ-----EGDDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLM 453
Cdd:cd03256 81 GMIFQQFNlierlSVLENVLSgRLGRRSTWRSlfglfPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 454 MEKPNILVMDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03256 160 MQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
3.31e-21 |
|
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: 90.01 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKLRQDQFAFEEFTVLDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 IMGHaelwevkqerdRIYALaeMSEEDGYKVAELETQYGEMDGysAEARAGElllgvgipveqhygPMSEVAPGWKLRVL 165
Cdd:pfam00005 81 RLGL-----------LLKGL--SKREKDARAEEALEKLGLGDL--ADRPVGE--------------RPGTLSGGQRQRVA 131
|
170
....*....|....*....
gi 695729787 166 LAQALFSNPDILLLDEPTN 184
Cdd:pfam00005 132 IARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-239 |
3.59e-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: 92.56 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQD------------ 72
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAelyrlrrrmgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 -QFA--FEEFTVLDTVImghaelwevkqerdriYALAEMSEEDgykvaelETQYGEmdgysaeaRAGELLLGVGIPVEQH 149
Cdd:cd03261 83 fQSGalFDSLTVFENVA----------------FPLREHTRLS-------EEEIRE--------IVLEKLEAVGLRGAED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 150 YGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMIIISHDRHFLNMVCTHM 222
Cdd:cd03261 132 LYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIADRI 207
|
250
....*....|....*..
gi 695729787 223 ADLDYGELrVYPGNYDE 239
Cdd:cd03261 208 AVLYDGKI-VAEGTPEE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
3.89e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 91.81 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQ----------IGYYAQ 389
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDvtgvpperrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHeyefendlTVFDWMS-----------QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPN 458
Cdd:cd03259 80 DY--------ALFPHLTvaeniafglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE-LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 459 ILVMDEPTNHLDMESIESLNMALEMYQG----TLIFVSHDREFVSSLATRVI 506
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-472 |
5.03e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.42 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-ERIgklrqdqfaFEEF--TVLDTvimghaelwevkqerdriYaLAE 107
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwDEV---------LKRFrgTELQN------------------Y-FKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 108 MSEEDgYKVAeLETQYGEM-----DGysaeaRAGELL---------------LGVGIPVEQHYGPMSevapGWKL-RVLL 166
Cdd:PRK13409 155 LYNGE-IKVV-HKPQYVDLipkvfKG-----KVRELLkkvdergkldevverLGLENILDRDISELS----GGELqRVAI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 167 AQALFSNPDILLLDEPTNNLDI-------DTIRWLEQtlndrDSTMIIISHDRHFLNMvcthMADL---DYGElrvyPGN 236
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDY----LADNvhiAYGE----PGA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 237 Y-------------DEYMtaatqaRERLLADNAkkkaqiadlqsfvsRFsanasksrqatsrarqidkikleevkassRQ 303
Cdd:PRK13409 291 YgvvskpkgvrvgiNEYL------KGYLPEENM--------------RI-----------------------------RP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 304 NPfIRFE----QDKKLFRNALEVEALTKGFDEgplFKnfnllLEV-------GEKIAILGANGVGKSTMLKTLVGELQPD 372
Cdd:PRK13409 322 EP-IEFEerppRDESERETLVEYPDLTKKLGD---FS-----LEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 373 NGTVKWSENaqIGYYAQdheY-EFENDLTVFDWMSQWKQEGDD-----EQAVRSILGRLLfsqddiKKPAKVLSGGEKGR 446
Cdd:PRK13409 393 EGEVDPELK--ISYKPQ---YiKPDYDGTVEDLLRSITDDLGSsyyksEIIKPLQLERLL------DKNVKDLSGGELQR 461
|
490 500
....*....|....*....|....*.
gi 695729787 447 MLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
1.19e-20 |
|
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: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD----PNERIGKLRQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 -QFAFEE-FTVLD---TVimghaelwevkqerDRIyalaemseedgykVAELETQYGEMDgysAEARAGELLLGVGIPVE 147
Cdd:COG1124 81 vQMVFQDpYASLHprhTV--------------DRI-------------LAEPLRIHGLPD---REERIAELLEQVGLPPS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 148 QHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHflnmVCTHMA 223
Cdd:COG1124 131 FLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLA----VVAHLC 206
|
250
....*....|.
gi 695729787 224 D----LDYGEL 230
Cdd:COG1124 207 DrvavMQNGRI 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
2.71e-20 |
|
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: 89.12 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFAF 76
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 EEFTVLDTVimghaelwevkqerdrIYALAEMseedgyKVAELETQygemdgysaeARAGELLLGVGIPVEQHYGPmSEV 156
Cdd:cd03259 85 PHLTVAENI----------------AFGLKLR------GVPKAEIR----------ARVRELLELVGLEGLLNRYP-HEL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDtIRW-----LEQTLNDRDSTMIIISHDR 212
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
4.13e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 89.10 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGS--KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNERIGKLRQD---- 72
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngySIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 -QF--AFEEFTVLDTVimghaelwevkqerdRIYA-LAEMSEEDGYKVAELETQYGEMDGYsAEARAGELllgvgipveq 148
Cdd:cd03263 81 pQFdaLFDELTVREHL---------------RFYArLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTL---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 149 hygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03263 135 --------SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIMS 206
|
....*
gi 695729787 227 YGELR 231
Cdd:cd03263 207 DGKLR 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-230 |
5.66e-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: 87.49 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAfEEFTVLDT 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA-RKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 VImghaELWEVKQERDRiyalaemseedgykvaeletQYGEMDGysaearaGELllgvgipveQhygpmsevapgwklRV 164
Cdd:cd03214 81 AL----ELLGLAHLADR--------------------PFNELSG-------GER---------Q--------------RV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 165 LLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNMV---CTHMADLDYGEL 230
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNLAaryADRVILLKDGRI 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
6.17e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwsPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQD---QFAfeeFTVLDTVIMGHAELWEVKQERDRIYALAeMSEEDgykVAELET-QYGEMDGysaearaGElllgvgip 145
Cdd:PRK13548 82 PQHsslSFP---FTVEEVVAMGRAPHGLSRAEDDALVAAA-LAQVD---LAHLAGrDYPQLSG-------GE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 146 veqhygpmsevapgwKLRVLLAQAL--FSNPD----ILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfL 215
Cdd:PRK13548 140 ---------------QQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---L 201
|
.
gi 695729787 216 N 216
Cdd:PRK13548 202 N 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
7.42e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 7.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA---- 75
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 -----FEEF------TVLDTV-----IMGHAElwevKQERDRIYALAEMseedgykVaELETQygemdgysAEARAGELL 139
Cdd:COG2884 80 rigvvFQDFrllpdrTVYENValplrVTGKSR----KEIRRRVREVLDL-------V-GLSDK--------AKALPHELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 140 LGvgipvEQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLNDRDSTMIIISHDRHFL 215
Cdd:COG2884 140 GG-----EQQ-------------RVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELV 200
|
.
gi 695729787 216 N 216
Cdd:COG2884 201 D 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-506 |
8.61e-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: 92.93 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-ERI-----GKLRQDQFAfeeftvldtvimghaelwevkqerdRIYa 104
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPSwDEVlkrfrGTELQDYFK-------------------------KLA- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 105 laemseEDGYKVAeLETQYGEMDGYSAEARAGELL---------------LGVGIPVEQHYGPMSevapGWKL-RVLLAQ 168
Cdd:COG1245 157 ------NGEIKVA-HKPQYVDLIPKVFKGTVRELLekvdergkldelaekLGLENILDRDISELS----GGELqRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 169 ALFSNPDILLLDEPTNNLDI-------DTIRwleqTLNDRDSTMIIISHDRHFLNMvcthMAD---LDYGElrvyPGNYD 238
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIyqrlnvaRLIR----ELAEEGKYVLVVEHDLAILDY----LADyvhILYGE----PGVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 239 eYMTAATQARErllADNAkkkaqiadlqsFVSRFsanasksrqatsrarqidkIKLEEVKAssRQNPfIRFE----QDKK 314
Cdd:COG1245 294 -VVSKPKSVRV---GINQ-----------YLDGY-------------------LPEENVRI--RDEP-IEFEvhapRREK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 315 LFRNALEVEALTKGFDEgplFKnfnllLEV-------GEKIAILGANGVGKSTMLKTLVGELQPDNGTVkwSENAQIGYY 387
Cdd:COG1245 337 EEETLVEYPDLTKSYGG---FS-----LEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQdheY-EFENDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:COG1245 407 PQ---YiSPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 695729787 467 NHLDMEsiESLNMA------LEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:COG1245 484 AHLDVE--QRLAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
330-514 |
1.33e-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: 87.65 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE-----------NAQIGYYAQDHEYEF--- 395
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIGYVPQDVTLFYgtl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 -ENdLTVFDwmsqwkQEGDDEQAVRS--ILGRLLFSQDD-------IKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:cd03245 95 rDN-ITLGA------PLADDERILRAaeLAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695729787 466 TNHLDMESIESLNMALEMYQG--TLIFVSHdREFVSSLATRVIEITPERVV 514
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-506 |
1.56e-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: 87.25 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGeKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----SENAQ-----IGYYAQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvLKQPQklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DheYEFENDLTVFD------WMSQWKQeGDDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:cd03264 80 E--FGVYPNFTVREfldyiaWLKGIPS-KEVKARVDEVLELVnLG--DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 463 DEPTNHLDMES-IESLNMALEMYQGTLIFVS-HDREFVSSLATRVI 506
Cdd:cd03264 155 DEPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVA 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
274-494 |
1.89e-19 |
|
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: 91.27 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 274 ANASKSRQATSRARqidkikLEEVKASSRQNPFIRFEQDKKLFRNA--LEVEALTKGFDEGP-LFKNFNLLLEVGEKIAI 350
Cdd:TIGR02868 293 AAQQLTRVRAAAER------IVEVLDAAGPVAEGSAPAAGAVGLGKptLELRDLSAGYPGAPpVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 351 LGANGVGKSTMLKTLVGELQPDNGTV--------KWSEN---AQIGYYAQD-HEYefenDLTVFDWMSQWKQEGDDEQAV 418
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVCAQDaHLF----DTTVRENLRLARPDATDEELW 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 419 RSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES----IESLNMALEMYq 485
Cdd:TIGR02868 443 AALervgLADWLRALPDgldtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR- 521
|
....*....
gi 695729787 486 gTLIFVSHD 494
Cdd:TIGR02868 522 -TVVLITHH 529
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
335-514 |
2.90e-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: 86.19 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNLLLEV---GEKIAILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQ----------IGYYAQdhEYEFE 396
Cdd:cd03297 10 LPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRKkinlppqqrkIGLVFQ--QYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 NDLTVFD---WMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES 473
Cdd:cd03297 88 PHLNVREnlaFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 474 ----IESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03297 167 rlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-526 |
3.98e-19 |
|
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: 86.62 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLfKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYAQD 390
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 HeYEFENdLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:cd03299 80 Y-ALFPH-MTVYKNIAyglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 466 TNHLDMES----IESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFtGNYEDYLRS 526
Cdd:cd03299 157 FSALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEEVFKK 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
329-514 |
4.34e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.68 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 329 FDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQP-DNGTVKW------SEN-----AQIGYYAQDHEYEFE 396
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLfgerrgGEDvwelrKRIGLVSPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 NDLTV--------FDWMSQWKQEGD-DEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:COG1119 93 RDETVldvvlsgfFDSIGLYREPTDeQRERARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 467 NHLDMESIESLNMALE--MYQG--TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:COG1119 171 AGLDLGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.43e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.25 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERElar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 -------FAF------EEFTVLDTVIMGHaelwevkqerdrIYAlaemseedGYKVAEletqygemdgysAEARAGELLL 140
Cdd:COG1136 83 lrrrhigFVFqffnllPELTALENVALPL------------LLA--------GVSRKE------------RRERARELLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 141 GVGIP-VEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFL 215
Cdd:COG1136 131 RVGLGdRLDHR-P-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELA 208
|
..
gi 695729787 216 NM 217
Cdd:COG1136 209 AR 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
6.80e-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: 85.33 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKLRQDQFAFEEfTVLDTVI 86
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADlrrNIGYVPQDVTLFYG-TLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 87 MGHAElweVKQERdrIYALAEMSEEDGYkVAE----LETQYGEmdgysaearAGELLLGvgipveqhygpmsevapGWKL 162
Cdd:cd03245 100 LGAPL---ADDER--ILRAAELAGVTDF-VNKhpngLDLQIGE---------RGRGLSG-----------------GQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMV 218
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLLDLV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
7.07e-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: 85.32 E-value: 7.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGnRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNE---RIGKLRQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqPQKlrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVimghaelwevkqerDRIYALAEMSEEDgykvaeletqygemdgysAEARAGELLLGVGipVEQHYG 151
Cdd:cd03264 80 EFGVYPNFTVREFL--------------DYIAWLKGIPSKE------------------VKARVDEVLELVN--LGDRAK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 -PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-DTIRW---LEQTLNDRdsTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03264 126 kKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIRFrnlLSELGEDR--IVILSTHIVEDVESLCNQVAVLN 203
|
....*
gi 695729787 227 YGELR 231
Cdd:cd03264 204 KGKLV 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-214 |
7.21e-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: 85.27 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQD------Q 73
Cdd:cd03262 5 NLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltdDKKNINELRQKvgmvfqQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 FA-FEEFTVLDTVIMGhaeLWEVKQerdriyalaeMSEEDgykvaeletqygemdgysAEARAGELLLGVGIPVEQHYGP 152
Cdd:cd03262 85 FNlFPHLTVLENITLA---PIKVKG----------MSKAE------------------AEERALELLEKVGLADKADAYP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 153 mSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHF 214
Cdd:cd03262 134 -AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaeEGMTMVVVTHEMGF 197
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-235 |
7.22e-19 |
|
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: 85.85 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS---LDPNER-IGKLRQdqfafeeftvlDTVIMG 88
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvagLVPWKRrKKFLRR-----------IGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 89 H-AELWEVKQERDRIYALAEMseedgYKVAELEtqYGE-MDGYSAEARAGELLlgvgipveqhYGPMSEVAPGWKLRVLL 166
Cdd:cd03267 102 QkTQLWWDLPVIDSFYLLAAI-----YDLPPAR--FKKrLDELSELLDLEELL----------DTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 167 AQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLN-DRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPG 235
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-508 |
7.45e-19 |
|
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: 83.97 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaqdheyefeN 397
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 DLTVFDWmsqwkqegdDEQAVRSILGRL-----LFSqDDIKKpaKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:cd03228 63 GVDLRDL---------DLESLRKNIAYVpqdpfLFS-GTIRE--NILSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 695729787 473 SIESLNMALEMYQG--TLIFVSHDREFVsSLATRVIEI 508
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAHRLSTI-RDADRIIVL 167
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-514 |
8.07e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.40 E-value: 8.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 302 RQNPFIRFEQDKKLFRNAL----EVEALTKGF------DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGEL-- 369
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLdlseRVAIVLEAFgvelrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 370 QPDNGTVKWSENaqigyyaqdheyEFENDLTVFDwmsQWKQEGDDEQAVRsILGRL-LFSQDDIKKPAKVLSGGEKGRML 448
Cdd:COG2401 83 TPVAGCVDVPDN------------QFGREASLID---AIGRKGDFKDAVE-LLNAVgLSDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 449 FGKLMMEKPNILVMDEPTNHLDMES--IESLNMALEMYQG--TLIFVSHDREFVSSLAtrvieitPERVV 514
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTakRVARNLQKLARRAgiTLVVATHHYDVIDDLQ-------PDLLI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-508 |
8.11e-19 |
|
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: 86.01 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQ 383
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHEYEFENDLTVFDWMSqwkqE-------GDDEQAVRSIL------GRLLFsqddiKKPAKvLSGGEKGRMLFG 450
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILA----EplrihglPDREERIAELLeqvglpPSFLD-----RYPHQ-LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 451 KLMMEKPNILVMDEPTNHLDMeSI--ESLNMaLEMYQG----TLIFVSHDREFVSSLATRVIEI 508
Cdd:COG1124 151 RALILEPELLLLDEPTSALDV-SVqaEILNL-LKDLREerglTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-229 |
8.19e-19 |
|
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: 84.16 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQD-QFAFE 77
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdLEDELPPLRRRiGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 78 EF------TVLDTVIMGhaelwevkqerdriyalaemseedgykvaeletqygemdgysaearagelLLGvgipveqhyg 151
Cdd:cd03229 84 DFalfphlTVLENIALG--------------------------------------------------LSG---------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 pmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDS-TMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03229 104 -------GQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
..
gi 695729787 228 GE 229
Cdd:cd03229 177 GK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
1.47e-18 |
|
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: 85.03 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQD-------- 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 -----QFA--FEEFTVLDTVIMGhaeLWEvkqerdriyaLAEMSEEDgykvaeletqygemdgysAEARAGELLLGVGIP 145
Cdd:COG1127 84 igmlfQGGalFDSLTVFENVAFP---LRE----------HTDLSEAE------------------IRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 146 -VEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-------IRwleqTLNDR-DSTMIIISHDRHFLN 216
Cdd:COG1127 133 gAADKM-P-SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavidelIR----ELRDElGLTSVVVTHDLDSAF 206
|
250 260
....*....|....*....|...
gi 695729787 217 MVCTHMADLDYGELRVYpGNYDE 239
Cdd:COG1127 207 AIADRVAVLADGKIIAE-GTPEE 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-493 |
2.21e-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: 82.75 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSenaqiGYYAQDHEYEFEN 397
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-----GVPVSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 DLTVFDwmsqwkqegddeQAVRsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES-IES 476
Cdd:cd03247 76 LISVLN------------QRPY------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQL 137
|
170
....*....|....*...
gi 695729787 477 LNMALEMYQG-TLIFVSH 493
Cdd:cd03247 138 LSLIFEVLKDkTLIWITH 155
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-249 |
2.41e-18 |
|
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: 88.28 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEP-----TLGNVSL---DPNE---RIGK 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqsgsiTLGGVDLrdlDEDDlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQDQFAFEEfTVLDTVIMG-----HAELWEVkQERDRIYALAEmSEEDGykvaeLETQYGEmdgysaearAGELLLGvG 143
Cdd:COG4987 414 VPQRPHLFDT-TLRENLRLArpdatDEELWAA-LERVGLGDWLA-ALPDG-----LDTWLGE---------GGRRLSG-G 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 144 ipvEQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVcTH 221
Cdd:COG4987 476 ---ERR-------------RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGRTVLLITHRLAGLERM-DR 538
|
250 260
....*....|....*....|....*...
gi 695729787 222 MADLDYGELRVyPGNYDEYMTAATQARE 249
Cdd:COG4987 539 ILVLEDGRIVE-QGTHEELLAQNGRYRQ 565
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
320-508 |
2.50e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.42 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK-WSENAQIGYYAQDH-----EY 393
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRigaliEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 394 -EFENDLTVFDWMSQW-KQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM 471
Cdd:cd03268 81 pGFYPNLTARENLRLLaRLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695729787 472 ESIESLN---MALEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03268 160 DGIKELReliLSLRDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-250 |
2.85e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.99 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMK-------ILGGDLepTLGNVS-LDPNERIGKLRQD 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDL--IVDGLKvNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 ------QF-AFEEFTVLDTVIMGHaelwevKQERDriyalaeMSEEDgykvaeletqygemdgysAEARAGELLLGVGIP 145
Cdd:PRK09493 79 agmvfqQFyLFPHLTALENVMFGP------LRVRG-------ASKEE------------------AEKQARELLAKVGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 146 VEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID---TIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHM 222
Cdd:PRK09493 128 ERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
250 260
....*....|....*....|....*...
gi 695729787 223 ADLDYGELRVyPGNYDEYMTAATQARER 250
Cdd:PRK09493 207 IFIDKGRIAE-DGDPQVLIKNPPSQRLQ 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-514 |
2.89e-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: 87.65 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGeLQPDNGTV------------KWSEN--- 381
Cdd:COG1123 4 LLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllELSEAlrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 382 AQIGYYAQDHEYEFeNDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKV----LSGGEKGRMLFGKLMMEKP 457
Cdd:COG1123 83 RRIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRyphqLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 458 NILVMDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:COG1123 162 DLLIADEPTTALDvttqaeiLDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
1.00e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 82.24 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLE-PTLGNVSLDpNERIGKLRQDQ-- 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVD-GTDLTLLSGKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 -------FAFEEFTVLD--TVimghaelwevkqeRDRI-YALaemsEEDGYKVAELEtqygemdgysaeARAGELLLGVG 143
Cdd:cd03258 79 karrrigMIFQHFNLLSsrTV-------------FENVaLPL----EIAGVPKAEIE------------ERVLELLELVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 144 IPVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDR-DSTMIIISHDRHFLNMVC 219
Cdd:cd03258 130 LEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRElGLTIVLITHEMEVVKRIC 208
|
250
....*....|.
gi 695729787 220 THMADLDYGEL 230
Cdd:cd03258 209 DRVAVMEKGEV 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-506 |
1.22e-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: 81.81 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQIGyyaqdheyeFENDLTVFD----- 403
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvsSLLGLGGG---------FNPELTGREniyln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 404 --WMSQWKQEGDdeQAVRSILGrllFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD-------ME 472
Cdd:cd03220 109 grLLGLSRKEID--EKIDEIIE---FSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafqekcQR 183
|
170 180 190
....*....|....*....|....*....|....
gi 695729787 473 SIESLNMAlemyQGTLIFVSHDREFVSSLATRVI 506
Cdd:cd03220 184 RLRELLKQ----GKTVILVSHDPSSIKRLCDRAL 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-515 |
1.67e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 81.36 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------KWSENAQIGYYAQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHeyefendlTVFDWMS-----------QWKQEGDDEQAVRSILGRL-L--FSQddiKKPAKvLSGGEKGRMLFGKLMME 455
Cdd:cd03293 81 QD--------ALLPWLTvldnvalglelQGVPKAEARERAEELLELVgLsgFEN---AYPHQ-LSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 456 KPNILVMDEPTNHLDMESIESLNMAL-EMYQG---TLIFVSHDREFVSSLATRVIEIT--PERVVD 515
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELlDIWREtgkTVLLVTHDIDEAVFLADRVVVLSarPGRIVA 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
1.82e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 81.36 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMGhaelwevkqerdriyalaemseedgykvaeLETQygEMDGYSAEARAGELLLGVGIP-VEQHY 150
Cdd:cd03293 81 QDALLPWLTVLDNVALG------------------------------LELQ--GVPKAEARERAEELLELVGLSgFENAY 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 151 gPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03293 129 -P-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
1.88e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 79.95 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFafeef 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNEL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 tvldtvimghaelwevkqeRDRIYALAEmseEDgykvaELetqygeMDGYSAEArageLLLGvgipveqhygpmsevapG 159
Cdd:cd03246 75 -------------------GDHVGYLPQ---DD-----EL------FSGSIAEN----ILSG-----------------G 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 160 WKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAHRPETLASA 162
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.90e-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: 81.14 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQD 72
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgedvnrlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 -QFAFEEF------TVLDTVimghaelwevkqerdriyALAemseedgykvaeLETQYGEMDGYsaEARAGELLLGVGIP 145
Cdd:TIGR02673 81 iGVVFQDFrllpdrTVYENV------------------ALP------------LEVRGKKEREI--QRRVGAALRQVGLE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 146 VEQHYGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHDRH 213
Cdd:TIGR02673 129 HKADAFPE-QLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
319-528 |
2.64e-17 |
|
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: 84.81 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN-----------AQIGY 386
Cdd:COG4988 336 SIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQdHEYEFEndLTVFDWMSQWKQEGDDEQAVRSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMEKP 457
Cdd:COG4988 416 VPQ-NPYLFA--GTIRENLRLGRPDASDEELEAALeaagLDEFVAALPDgldtpLGEGGRGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 458 NILVMDEPTNHLDMESIESLNMAL-EMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfTGNYEDYLRSKG 528
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALrRLAKGrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-506 |
4.76e-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: 83.88 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGF-DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIGY 386
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladADADSwrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQdHEYEFENdlTVFDWMSQWKQEGDDEQAVRSI-----------LGRLLFSQddIKKPAKVLSGGEKGRMLFGKLMME 455
Cdd:TIGR02857 401 VPQ-HPFLFAG--TIAENIRLARPDASDAEIREALeragldefvaaLPQGLDTP--IGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695729787 456 KPNILVMDEPTNHLDMESIESLNMALEMY-QG-TLIFVSHDREfVSSLATRVI 506
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRLA-LAALADRIV 527
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
5.96e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQD-QFAFEeFTVLDTVIMGHAElwevkqERDRiyaLAEMSEEDGYKVAEletqygEMDGYSAEARAGElllgvgipveq 148
Cdd:PRK09536 83 PQDtSLSFE-FDVRQVVEMGRTP------HRSR---FDTWTETDRAAVER------AMERTGVAQFADR----------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 149 hygPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID-TIRWLE--QTLNDRDSTMIIISHDrhfLNM 217
Cdd:PRK09536 136 ---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHD---LDL 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
321-514 |
6.47e-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: 80.07 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALtkgfdegplfKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSEN----AQIGY-YAQ 389
Cdd:cd03267 33 EVEAL----------KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRkkflRRIGVvFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHEYEFenDLTVFDWMSQWKQ--EGDDEQAVRSI--LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:cd03267 103 KTQLWW--DLPVIDSFYLLAAiyDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695729787 466 TNHLDMESIESLNMALEMY----QGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
8.27e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpismlsSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVLDTVIMG---HAELWevkqerdriyalAEMSEEDGYKV--AELETQYGEMdgysAEARAGELllgvgi 144
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspWLSLW------------GRLSAEDNARVnqAMEQTRINHL----ADRRLTDL------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 145 pveqhygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID---TIRWLEQTLNDRDSTMIIISHDrhfLNMV--- 218
Cdd:PRK11231 140 ------------SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD---LNQAsry 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 695729787 219 CTHMADLDYGELrVYPGNYDEYMTaatqarERLLADNAKKKAQI 262
Cdd:PRK11231 205 CDHLVVLANGHV-MAQGTPEEVMT------PGLLRTVFDVEAEI 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
8.98e-17 |
|
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: 79.53 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DL---EPTLGNVSLD----------PNE---R 65
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLipgAPDEGEVLLDgkdiydldvdVLElrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 66 IGKLRQDQFAFEeFTVLDTVIMGhaelwevkqerDRIYALAEMSEEDgykvaeletqygemdgysaeARAGELLLGVGIP 145
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYG-----------LRLHGIKLKEELD--------------------ERVEEALRKAALW 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 146 VE----QHYGPMSevaPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN--DRDSTMIIISHD 211
Cdd:cd03260 131 DEvkdrLHALGLS---GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-505 |
1.64e-16 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 78.45 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE--FEN 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAmvFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 -----DLTVFDWMS---QWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:cd03301 81 yalypHMTVYDNIAfglKLRKVPKDEidERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 468 HLD------MES-IESLNMALEMyqgTLIFVSHDREFVSSLATRV 505
Cdd:cd03301 160 NLDaklrvqMRAeLKRLQQRLGT---TTIYVTHDQVEAMTMADRI 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-506 |
2.18e-16 |
|
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: 76.70 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYEFENDL 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----------DGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 tvfdwmsqwkqegddeQAVRsiLGRLLFSQddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNM 479
Cdd:cd03216 71 ----------------DARR--AGIAMVYQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|
gi 695729787 480 ALEMY--QG-TLIFVSHDREFVSSLATRVI 506
Cdd:cd03216 124 VIRRLraQGvAVIFISHRLDEVFEIADRVT 153
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-511 |
2.23e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 294 LEEVKASSRQNPFIRFEQDkklfrNALEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG----- 367
Cdd:COG4178 342 LEAADALPEAASRIETSED-----GALALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpyg 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 368 ----ELQPDN-------------GTVKwsenAQIGYYAQDHEYefendltvfdwmsqwkqegdDEQAVRSI-----LGRL 425
Cdd:COG4178 417 sgriARPAGArvlflpqrpylplGTLR----EALLYPATAEAF--------------------SDAELREAleavgLGHL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 426 LFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLnMAL---EMYQGTLIFVSHdREFVSSLA 502
Cdd:COG4178 473 AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL-YQLlreELPGTTVISVGH-RSTLAAFH 550
|
....*....
gi 695729787 503 TRVIEITPE 511
Cdd:COG4178 551 DRVLELTGD 559
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-506 |
2.38e-16 |
|
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: 78.32 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLF----KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE- 394
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 ------FENDLTVFD-WMS--------QWKQEGDDEQAVRSILGRLLFSQddIKKPAKV-------LSGGEKGRMLFGKL 452
Cdd:cd03257 82 keiqmvFQDPMSSLNpRMTigeqiaepLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVlnrypheLSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 453 MMEKPNILVMDEPTNHLDMES----IESLNMALEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-514 |
2.66e-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: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQDH------EY 393
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRigylpeER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 394 EFENDLTVFD---WMSQWKQEGDDEQA--VRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNH 468
Cdd:cd03269 80 GLYPKMKVIDqlvYLAQLKGLKKEEARrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 469 LDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-506 |
3.45e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.59 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENAQIGYYA 388
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDHeyefendlTVFDWMS-----------QWKQEGDDEQAVRSILGR--LLFSQDdiKKPaKVLSGGEK-----GRMLfg 450
Cdd:COG1116 87 QEP--------ALLPWLTvldnvalglelRGVPKAERRERARELLELvgLAGFED--AYP-HQLSGGMRqrvaiARAL-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 451 klmMEKPNILVMDEPTNHLDMESIESLN-MALEMYQG---TLIFVSHD-REFVsSLATRVI 506
Cdd:COG1116 154 ---ANDPEVLLMDEPFGALDALTRERLQdELLRLWQEtgkTVLFVTHDvDEAV-FLADRVV 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
4.13e-16 |
|
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: 77.55 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 17 FENISVKFGGGNRY-----------------GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAFEE- 78
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 79 --------FTVLDTVImghaelwevkqerdRIY-ALAEMseedgykvaeLETQYGEMDGYSAEARAGELLLGVGIPvEQH 149
Cdd:cd03257 84 iqmvfqdpMSSLNPRM--------------TIGeQIAEP----------LRIHGKLSKKEARKEAVLLLLVGVGLP-EEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 150 YG--PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISHDRHFLNMVCTHMA 223
Cdd:cd03257 139 LNryP-HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVA 217
|
....*..
gi 695729787 224 DLDYGEL 230
Cdd:cd03257 218 VMYAGKI 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-213 |
4.84e-16 |
|
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: 77.47 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGS--KPL--FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG4181 8 IIELRGLTKTVGTgaGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDArar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 -------FAFEEF------TVLDTVIMGhAELwevKQERDriyalaemseedgykvaeletqygemdgysAEARAGELLL 140
Cdd:COG4181 87 lrarhvgFVFQSFqllptlTALENVMLP-LEL---AGRRD------------------------------ARARARALLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 141 GVGI-PVEQHY-GPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLN-DRDSTMIIISHDRH 213
Cdd:COG4181 133 RVGLgHRLDHYpAQLSG---GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFE-LNrERGTTLVLVTHDPA 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-514 |
5.71e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 77.48 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFdeGPL--FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWS---------- 379
Cdd:cd03219 1 LEVRGLTKRF--GGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPpheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 380 ---------------ENAQIGYYAQDHEYefendltvFDWMSQWKQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGE 443
Cdd:cd03219 79 rtfqiprlfpeltvlENVMVAAQARTGSG--------LLLARARREEREARERAEELLERVgL--ADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 444 KGRMLFGKLMMEKPNILVMDEPT---NHLD----MESIESLNMalemyQG-TLIFVSHDREFVSSLATRVI--------- 506
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAaglNPEEteelAELIRELRE-----RGiTVLLVEHDMDVVMSLADRVTvldqgrvia 223
|
....*...
gi 695729787 507 EITPERVV 514
Cdd:cd03219 224 EGTPDEVR 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
7.21e-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: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE--------------RIGKLRQDQFAFE 77
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 78 EFTVLDTVIMGhaelwevkqerdriyALAEMSeedgyKVAELETQYGEMDgysaEARAGELLLGVGIpVEQHYGPMSEVA 157
Cdd:cd03256 92 RLSVLENVLSG---------------RLGRRS-----TWRSLFGLFPKEE----KQRALAALERVGL-LDKAYQRADQLS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
7.46e-16 |
|
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: 76.68 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQD-QFAF 76
Cdd:cd03292 5 NVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKiGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 EEF------TVLDTVimghaelwevkqerdriyALA-EMSEEDGYKVAEletqygemdgysaeaRAGELLLGVGIPVEQH 149
Cdd:cd03292 85 QDFrllpdrNVYENV------------------AFAlEVTGVPPREIRK---------------RVPAALELVGLSHKHR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 150 YGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHDRHFLN 216
Cdd:cd03292 132 ALPA-ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVD 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
320-515 |
8.06e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS-ENAQIGYYAQD-----HEY 393
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 394 EFENDLTVFDWMSQWKQ--EGDDEQAVRSI----LGRLLfsqdDIkkPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:PRK13539 83 AMKPALTVAENLEFWAAflGGEELDIAAALeavgLAPLA----HL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 468 HLDMESIEslnMALEMYQ------GTLIFVSHdrefvSSLAT---RVIEITPERVVD 515
Cdd:PRK13539 157 ALDAAAVA---LFAELIRahlaqgGIVIAATH-----IPLGLpgaRELDLGPFAAED 205
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
345-514 |
8.51e-16 |
|
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: 77.16 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENAQIGYYAQ-DHEYEFENDLTVFD--------WMSQ 407
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARARRVALvEQDSDTAVPLTVRDvvalgripHRSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 408 WKQE-GDDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES-IESLNMALEMY- 484
Cdd:TIGR03873 107 WAGDsPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAqLETLALVRELAa 185
|
170 180 190
....*....|....*....|....*....|.
gi 695729787 485 -QGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:TIGR03873 186 tGVTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
8.67e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.64 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLG-------NVSLDPNE---RIGKLRQ 71
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREvrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMgHAelwevkqerdRIYalaemseedGYKVAELETqygemdgysaeaRAGELLLGVGIpVEQHYG 151
Cdd:cd03265 81 DLSVDDELTGWENLYI-HA----------RLY---------GVPGAERRE------------RIDELLDFVGL-LEAADR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03265 128 LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH 207
|
....
gi 695729787 228 GELR 231
Cdd:cd03265 208 GRII 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
1.15e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV-----SLDP----------NERIGKLRQDQFAFEEFTVLD 83
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKlssaakaelrNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 TVIMghaelwevkqerdriyalaemseedgykvaelETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPmSEVAPGWKLR 163
Cdd:PRK11629 107 NVAM--------------------------------PLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDRDST-MIIISHD 211
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
1.22e-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: 74.73 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQDQFAFEeft 80
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkNIAYVPQDPFLFS--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 vlDTVimghaelwevkqeRDRIyalaeMSeedgykvaeletqygemdgysaearAGElllgvgipveqhygpmsevapgw 160
Cdd:cd03228 90 --GTI-------------RENI-----LS-------------------------GGQ----------------------- 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRH 213
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
1.30e-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: 79.64 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKL 69
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEfTVLDTVIMGhaelwevkqerdRIYALAEMSEEdgykVAELetqyGEMDGYSAEARAG-ELLLGVGipveq 148
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA------------RPDASDAEIRE----ALER----AGLDEFVAALPQGlDTPIGEG----- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 149 hyGpmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTirwlEQTLND------RDSTMIIISHDRHflnmvctHM 222
Cdd:TIGR02857 456 --G--AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEalralaQGRTVLLVTHRLA-------LA 520
|
....*
gi 695729787 223 ADLDY 227
Cdd:TIGR02857 521 ALADR 525
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
320-515 |
1.35e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.86 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW--------SENA------QI 384
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlKRREipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 GYYAQDHEyeFENDLTVFDWMS-----QWKQEGDDEQAVRSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMEKPN 458
Cdd:COG2884 82 GVVFQDFR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVgLSDKAK-ALPHE-LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 459 ILVMDEPTNHLD-------MESIESLNMalemyQG-TLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:COG2884 158 LLLADEPTGNLDpetsweiMELLEEINR-----RGtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
415-527 |
1.40e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.90 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 415 EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQGTLIFVSHD 494
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHA 400
|
90 100 110
....*....|....*....|....*....|...
gi 695729787 495 REFVSSLATRVIEITPERVVDFTGNYEDYLRSK 527
Cdd:PLN03073 401 REFLNTVVTDILHLHGQKLVTYKGDYDTFERTR 433
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-466 |
1.66e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKlrqdqfafeEFT 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GE---------PVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDT-------VIMGHAELwevkqerdriyALA-EMSeedgykVAE------LETQYGEMDGYSAEARAGELL--LGVGI 144
Cdd:COG1129 70 FRSPrdaqaagIAIIHQEL-----------NLVpNLS------VAEniflgrEPRRGGLIDWRAMRRRARELLarLGLDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 145 PVEQhygPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIIShdrHFLN- 216
Cdd:COG1129 133 DPDT---PVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverlFRIIR----RLKAQGVAIIYIS---HRLDe 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 217 ---------------MVCTH-MADLDYGELrVypgnydEYMTaatqARErlladnakkkaqiadlqsFVSRFSAnasksr 280
Cdd:COG1129 203 vfeiadrvtvlrdgrLVGTGpVAELTEDEL-V------RLMV----GRE------------------LEDLFPK------ 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 281 qatsRARQIDKIkleevkassrqnpfirfeqdkklfrnALEVEALTKgfdeGPLFKNFNLLLEVGEKIAILGANGVGKST 360
Cdd:COG1129 248 ----RAAAPGEV--------------------------VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 361 MLKTLVGELQPDNGTVKWSE------------NAQIGYYAQDHEYE--------FEN-DLTVFDWMSQWK--QEGDDEQA 417
Cdd:COG1129 294 LARALFGADPADSGEIRLDGkpvrirsprdaiRAGIAYVPEDRKGEglvldlsiRENiTLASLDRLSRGGllDRRRERAL 373
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 695729787 418 VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:COG1129 374 AEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-510 |
2.09e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE---NAQIGYYAQD-----H 391
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHQDllylgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLTVF---DWMSQWKQEGDDEqAVRSILGRL-LFSQDDIkkPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:PRK13538 82 QPGIKTELTALenlRFYQRLHGPGDDE-ALWEALAQVgLAGFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 468 HLDMESIESLNMALEMYQ---GTLIFVSHDREFVSSLATRVIEITP 510
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAeqgGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-509 |
2.21e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---QIGYYAQD-----H 391
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGllylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIkkPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM 471
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 472 ESIESLNMALEMYQ---GTLIFVSHDREFVSSLATRVIEIT 509
Cdd:cd03231 159 AGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-505 |
2.75e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 313 KKLFRNALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS--ENAQIGYYAQD 390
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 HEYEFENdLTVFDWMS-------QWKQE----GDDEQAVRSILGrLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNI 459
Cdd:PRK11607 93 INMMFQS-YALFPHMTveqniafGLKQDklpkAEIASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695729787 460 LVMDEPTNHLDMESIESLNMA----LEMYQGTLIFVSHDREFVSSLATRV 505
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-233 |
2.82e-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: 74.88 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLRQDQFAFE-EFTVLDTVIMGHAELW-- 93
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLGGGFNpELTGRENIYLNGRLLGls 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 94 --EVKQERDRIYALaemseedgykvAELEtQYGEMdgysaearagelllgvgipveqhygPMSEVAPGWKLRVLLAQALF 171
Cdd:cd03220 116 rkEIDEKIDEIIEF-----------SELG-DFIDL-------------------------PVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 172 SNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03220 159 LEPDILLIDEVLAVGDaafqekcQRRLR----ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-498 |
3.39e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFEN 397
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 DLTVFDWMSQwkQEGDDEQAVRSILGRLLfSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESL 477
Cdd:PRK09544 83 PLTVNRFLRL--RPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|....*.
gi 695729787 478 -----NMALEMYQGTLIfVSHDREFV 498
Cdd:PRK09544 160 ydlidQLRRELDCAVLM-VSHDLHLV 184
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
6.69e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.47 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAFeeftvldtv 85
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-GKPLDIAARNRIGY--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 imghaelwevkqerdriyalaeMSEEDG----YKVAELETQYGEMDGYS---AEARAGELLLGVGIpVEQHYGPMSEVAP 158
Cdd:cd03269 75 ----------------------LPEERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWLERLEL-SEYANKRVEELSK 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
6.79e-15 |
|
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: 74.01 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF-----GSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------------SLD 61
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 62 PNErIGKLRQD------QFafeeftvLDTVimghaelwevkqerDRIYALAEMSE---EDGYKVAEletqygemdgysAE 132
Cdd:COG4778 84 PRE-ILALRRRtigyvsQF-------LRVI--------------PRVSALDVVAEpllERGVDREE------------AR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 133 ARAGELLLGVGIPVEQHygpmsEVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLND 200
Cdd:COG4778 130 ARARELLARLNLPERLW-----DLPPatfsgGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIE----EAKA 200
|
250 260
....*....|....*....|....*.
gi 695729787 201 RDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:COG4778 201 RGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
7.59e-15 |
|
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: 74.30 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNER-IGKLRQD 72
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEEFTVLDTVIMGhaelWEVKQERDRIYAlAEMSEedgyKVAELeTQYGEMDGYsaearagelllgvgipvEQHYgP 152
Cdd:cd03296 83 YALFRHMTVFDNVAFG----LRVKPRSERPPE-AEIRA----KVHEL-LKLVQLDWL-----------------ADRY-P 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 153 mSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 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 |
8.26e-15 |
|
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: 73.91 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV---------KWSENAQIGYYAQ 389
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 dhEYEFENDLTVFDWMS-----QWKQEGDDEQAVRSILGRLL-FSQDDI---KKPAKvLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:cd03296 82 --HYALFRHMTVFDNVAfglrvKPRSERPPEAEIRAKVHELLkLVQLDWladRYPAQ-LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695729787 461 VMDEPTNHLDMESIESLNMAL-----EMYQgTLIFVSHDREFVSSLATRVI 506
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLrrlhdELHV-TTVFVTHDQEEALEVADRVV 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-511 |
9.02e-15 |
|
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: 72.19 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLvGELQP-DNGTVKWSENAQIGYYAQdHEYefen 397
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQ-RPY---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 dltvfdwMSQwkqegddeqavrsilGRLlfsQDDIKKP-AKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIES 476
Cdd:cd03223 75 -------LPL---------------GTL---REQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180 190
....*....|....*....|....*....|....*
gi 695729787 477 LNMALEMYQGTLIFVSHdREFVSSLATRVIEITPE 511
Cdd:cd03223 130 LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-514 |
9.20e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.30 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 324 ALTKGFD-EGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGtvkwsenaQIGYYAQDHEYE-------- 394
Cdd:cd03298 2 RLDKIRFsYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG--------RVLINGVDVTAAppadrpvs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 --F-END----LTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGK-LMMEKPnILV 461
Cdd:cd03298 74 mlFqENNlfahLTVEQNVGlglspGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALARvLVRDKP-VLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 462 MDEPTNHLD-MESIESLNMALEMY---QGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03298 152 LDEPFAALDpALRAEMLDLVLDLHaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
1.10e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPT-----LGNVSLDPNERIGK------- 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirVGDITIDTARSLSQqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQD-QFAFEEF------TVLDTVIMGHAElweVKQE-RDriyalaemseedgykvaeletqygemdgySAEARAGELLL 140
Cdd:PRK11264 83 LRQHvGFVFQNFnlfphrTVLENIIEGPVI---VKGEpKE-----------------------------EATARARELLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 141 GVGIPVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlndRDSTMIIISHDRH 213
Cdd:PRK11264 131 KVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQ----EKRTMVIVTHEMS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 695729787 214 FLNMVCTHMADLDYGELrVYPGNYDEYMTAATQARERLLAD 254
Cdd:PRK11264 206 FARDVADRAIFMDQGRI-VEQGPAKALFADPQQPRTRQFLE 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-230 |
1.27e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.07 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNERIGKLRQDQFAFEeftvld 83
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRRDVQLVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 tvimghaelwevkqerDRIYAL-AEMSEEdgYKVAELETQYGEMDGYSAEARAGELLLGVGIPVE--QHYGPmsEVAPGW 160
Cdd:TIGR02769 96 ----------------DSPSAVnPRMTVR--QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdaDKLPR--QLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 161 KLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.32e-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: 76.25 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-----------PNERIGKLRQDQFAFEEfT 80
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGH-----AELWEVkQERDRIYALAEmSEEDGykvaeLETQYGEMdgysaearaGELLLGvgipveqhygpmse 155
Cdd:TIGR02868 425 VRENLRLARpdatdEELWAA-LERVGLADWLR-ALPDG-----LDTVLGEG---------GARLSG-------------- 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 156 vapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS--TMIIISHD 211
Cdd:TIGR02868 475 ---GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-466 |
1.78e-14 |
|
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: 72.47 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW----------SENAQ--IGYY 387
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglppHERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYeFENdLTVFD--WMSQWKQEGDDEQAvrsILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMEKPNIL 460
Cdd:cd03224 81 PEGRRI-FPE-LTVEEnlLLGAYARRRAKRKA---RLERVyeLFPrlKERRKQLAGTLSGGEQ-QMLaIARALMSRPKLL 154
|
....*.
gi 695729787 461 VMDEPT 466
Cdd:cd03224 155 LLDEPS 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-516 |
1.79e-14 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 72.60 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTL-----VGELQPDNGTV--------KWSEN----- 381
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVlldgkdiyDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 382 AQIGYYAQdHEYEFenDLTVFDWMS--------QWKQEGDDEqaVRSILGR-LLFSQDDIKKPAKVLSGGEKGRMLFGKL 452
Cdd:cd03260 81 RRVGMVFQ-KPNPF--PGSIYDNVAyglrlhgiKLKEELDER--VEEALRKaALWDEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 453 MMEKPNILVMDEPTNHLDMES---IESLNMALEMyQGTLIFVSHDREFVSSLATRVIEITPERVVDF 516
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-496 |
2.05e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNvsldpnerigklRQDQF------AFEEFTVLdtvimghaelweVKQE-- 98
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGE------------RQSQFshitrlSFEQLQKL------------VSDEwq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 99 RDRIYALAEMSEEDGYKVAELEtqygeMDGYSAEARAGEL--LLGVGIPVEQHYGPMSEvapGWKLRVLLAQALFSNPDI 176
Cdd:PRK10938 85 RNNTDMLSPGEDDTGRTTAEII-----QDEVKDPARCEQLaqQFGITALLDRRFKYLST---GETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 177 LLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrvypgnydeymtAATQARERLLA 253
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAEllaSLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTL------------AETGEREEILQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 254 DnakkkAQIADLqsfvsrfsanasksrqatSRARQIDKIKLEEvKASSRQNPFIRFEQDKKLFRNAlevealTKGFDEGP 333
Cdd:PRK10938 225 Q-----ALVAQL------------------AHSEQLEGVQLPE-PDEPSARHALPANEPRIVLNNG------VVSYNDRP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 334 LFKNFNLLLEVGEKIAILGANGVGKSTMLK--------------TLVGElQPDNGTVKWSENAQIGYYAQDHEYEFENDL 399
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndlTLFGR-RRGSGETIWDIKKHIGYVSSSLHLDYRVST 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 TV--------FDWMSQWKQEGDDEQA-VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:PRK10938 354 SVrnvilsgfFDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
490 500 510
....*....|....*....|....*....|....*
gi 695729787 471 mesieSLNMALEMY---------QGTLIFVSHDRE 496
Cdd:PRK10938 434 -----PLNRQLVRRfvdvlisegETQLLFVSHHAE 463
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-506 |
2.24e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 72.18 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSE-NAQIGY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQdHEYEFENdLTVFDWMS---QWKQEGDDEQAV---RSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMEKPNI 459
Cdd:cd03262 81 VFQ-QFNLFPH-LTVLENITlapIKVKGMSKAEAEeraLELLEKVgLADKAD-AYPAQ-LSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695729787 460 LVMDEPTNHLDMESI-ESLNMALEMYQG--TLIFVSHDREFVSSLATRVI 506
Cdd:cd03262 157 MLFDEPTSALDPELVgEVLDVMKDLAEEgmTMVVVTHEMGFAREVADRVI 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-230 |
2.29e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQ--------DQ 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-GQTINLVRDkdgqlkvaDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 FAFEEFTVLDTVIMGHAELWevkqerdriyalAEMSEEDgyKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPM 153
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLW------------SHMTVLE--NVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-512 |
2.65e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 72.47 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFD-------EGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------KWSENAQ--- 383
Cdd:COG4778 5 LEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdgGWVDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 ----------IGYYAQdheyeFendLTV------FDWMSQ--WKQEGDDEQA---VRSILGRLlfsqdDIKK------PA 436
Cdd:COG4778 85 reilalrrrtIGYVSQ-----F---LRViprvsaLDVVAEplLERGVDREEArarARELLARL-----NLPErlwdlpPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 437 kVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES----IESLNMALEmyQGT-LIFVSHDREFVSSLATRVIEITPE 511
Cdd:COG4778 152 -TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGTaIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 695729787 512 R 512
Cdd:COG4778 229 S 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-515 |
3.24e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.48 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE----------------- 380
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 381 --NAQIGYYAQD-----HEYEFENdltVFDWMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGK 451
Cdd:PRK11264 82 qlRQHVGFVFQNfnlfpHRTVLEN---IIEGPVIVKGEPKEEatARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 452 LMMEKPNILVMDEPTNHLDMESI-ESLNM--ALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-514 |
3.36e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQD--------- 390
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKevarrigll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 -HEYEFENDLTVFDWMS-----------QWKQEgdDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPN 458
Cdd:PRK10253 87 aQNATTPGDITVQELVArgryphqplftRWRKE--DEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 459 ILVMDEPTNHLDM-ESIESLNMALEM--YQG-TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10253 164 IMLLDEPTTWLDIsHQIDLLELLSELnrEKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-505 |
3.44e-14 |
|
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: 71.88 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---------QIGYYAQD 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 heYEFENDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:cd03300 81 --YALFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695729787 466 TNHLDMESIESLNMALEMYQG----TLIFVSHDREFVSSLATRV 505
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-494 |
4.05e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDH---EyefenDLTVFD--------WMSQW-KQEGDDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMEK 456
Cdd:PRK11231 83 QHHltpE-----GITVRElvaygrspWLSLWgRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 457 PNILVMDEPTNHLDM-ESIESLNMALEMYQG--TLIFVSHD 494
Cdd:PRK11231 157 TPVVLLDEPTTYLDInHQVELMRLMRELNTQgkTVVTVLHD 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-505 |
4.06e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNER----IGKLRQD 72
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcarLTPAKAhqlgIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEEFTVLDTVIMGHAelwevKQERDriyaLAEMSEedgyKVAELETQygemdgYSAEARAGELllgvgipveqhygp 152
Cdd:PRK15439 95 PLLFPNLSVKENILFGLP-----KRQAS----MQKMKQ----LLAALGCQ------LDLDSSAGSL-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 153 msEVAPGWKLRVLlaQALFSNPDILLLDEPTNNLD-IDTIRWLEQ--TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:PRK15439 142 --EVADRQIVEIL--RGLMRDSRILILDEPTASLTpAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRISVMRDGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 230 LrVYPGNYDEYMTAATqarerlladnakkkaqiadlqsfvsrFSANASKSRQATSRARQidKIKLeEVKASSRQNPfirf 309
Cdd:PRK15439 218 I-ALSGKTADLSTDDI--------------------------IQAITPAAREKSLSASQ--KLWL-ELPGNRRQQA---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 310 eQDKKLfrnaLEVEALTkgfDEGplFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGeLQPDNGTVKWSENAQIGYYA- 388
Cdd:PRK15439 264 -AGAPV----LTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARGGRIMLNGKEINALSt 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 ---------------QDHEYEFENDLT------VFDWMSQWKQEGdDEQAV----RSILGrLLFSQDDikKPAKVLSGGE 443
Cdd:PRK15439 333 aqrlarglvylpedrQSSGLYLDAPLAwnvcalTHNRRGFWIKPA-RENAVleryRRALN-IKFNHAE--QAARTLSGGN 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 444 KGRMLFGKLMMEKPNILVMDEPTNHLD----------MESIESLNMAlemyqgtLIFVSHDREFVSSLATRV 505
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDvsarndiyqlIRSIAAQNVA-------VLFISSDLEEIEQMADRV 473
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-514 |
4.30e-14 |
|
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: 71.63 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGT--------VKWSEN--AQIGYYAQ 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DheYEFENDLTVFD---WMSQ---WKQEGDDEQAVRSILGRLLFSQDDikKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:cd03265 81 D--LSVDDELTGWEnlyIHARlygVPGAERRERIDELLDFVGLLEAAD--RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 464 EPTNHLDMES-------IESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03265 157 EPTIGLDPQTrahvweyIEKLKEEFGM---TILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
318-519 |
4.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGP-LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV---------------KWSEN 381
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 382 AQIGYYAQDHE------YEfenDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMME 455
Cdd:PRK13636 84 VGMVFQDPDNQlfsasvYQ---DVS-FGAVNLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 456 KPNILVMDEPTNHLDMESI-ESLNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVVdFTGN 519
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
320-506 |
4.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLF-----KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGT------------VKWSE-N 381
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkVKLSDiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 382 AQIGYYAQDHEYE-FENDL---TVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIK-KPAKVLSGGEKGRMLFGKLMMEK 456
Cdd:PRK13637 83 KKVGLVFQYPEYQlFEETIekdIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 457 PNILVMDEPTNHLD-------MESIESLNmalEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:PRK13637 163 PKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-506 |
6.02e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.67 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQDHEYEFEndLTVFDWMSQwkqegddeqaVRSILGR 424
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYE--GTVRDLLSS----------ITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 425 LLFSQDDIKKPAKV----------LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME----SIESLNMALEMYQGTLIF 490
Cdd:cd03237 92 HPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFV 171
|
170
....*....|....*.
gi 695729787 491 VSHDREFVSSLATRVI 506
Cdd:cd03237 172 VEHDIIMIDYLADRLI 187
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-505 |
6.12e-14 |
|
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: 71.00 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTK--GFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----------AQIGYY 387
Cdd:cd03263 1 LQIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQdHEYEFENdLTVFD---WMSQWK-QEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:cd03263 81 PQ-FDALFDE-LTVREhlrFYARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695729787 464 EPTNHLDMESIESL-NMALEMYQG-TLIFVSHDREFVSSLATRV 505
Cdd:cd03263 159 EPTSGLDPASRRAIwDLILEVRKGrSIILTTHSMDEAEALCDRI 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
6.66e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.38 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLG-------NVSLDPNERIGKLRQDQFAFeeftvldtvimgha 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLRREHFGF-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 91 elweVKQerdRIYALAEMSEEDGYKVAELetqYGEMDGYSAEARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQAL 170
Cdd:PRK10535 91 ----IFQ---RYHLLSHLTAAQNVEVPAV---YAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 171 FSNPDILLLDEPTNNLD----IDTIRWLEQtLNDRDSTMIIISHD 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
6.94e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 69.38 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpnerigklrqdqfafeeftv 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 ldtvimghaelwevkqerdriyalaemseeDGYKVAELETqygemdgysAEARAgellLGVGIpVEQhygpMSevaPGWK 161
Cdd:cd03216 60 ------------------------------DGKEVSFASP---------RDARR----AGIAM-VYQ----LS---VGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND-RDS--TMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRlRAQgvAVIFISH 140
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-515 |
1.04e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.47 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDegPLFKNFNLLLEV------GEKIAILGANGVGKSTMLKTLVGELQPDNGtvkwseNAQI-GYYAQDHE 392
Cdd:cd03266 2 ITADALTKRFR--DVKKTVQAVDGVsftvkpGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVdGFDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 393 YE-------FENDLTVFDWMSQWKQ----------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMME 455
Cdd:cd03266 74 AEarrrlgfVSDSTGLYDRLTARENleyfaglyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 456 KPNILVMDEPTNHLDMESIESLNMALEMY---QGTLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
1.10e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIG----KLRQDqfaf 76
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGyvpqKLYLD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 eefTVLDTVIMGHAELWEVKQERDRIYALAEMseedgykvaeletqygemdgysaeaRAGELLlgvgipvEQhygPMSEV 156
Cdd:PRK09544 80 ---TTLPLTVNRFLRLRPGTKKEDILPALKRV-------------------------QAGHLI-------DA---PMQKL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDRHFLnmvcthMADLD 226
Cdd:PRK09544 122 SGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLRRELD---CAVLMVSHDLHLV------MAKTD 189
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-527 |
1.10e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--AQIGYYAQdheyeFENDLTVfdwmsqwkqeg 412
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLELGAG-----FHPELTG----------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 413 ddEQAVRSIlGRLL-FSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESI 474
Cdd:COG1134 106 --RENIYLN-GRLLgLSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 475 ESLNMALEMYQ---GTLIFVSHDREFVSSLATRVIEI---------TPERVVDFtgnYEDYLRSK 527
Cdd:COG1134 183 KKCLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLekgrlvmdgDPEEVIAA---YEALLAGR 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-470 |
1.27e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----------AQIGYYA 388
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 Q----DHEYEFENDLTVFDwmsqwKQEGDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMEKPNILV 461
Cdd:PRK13537 87 QfdnlDPDFTVRENLLVFG-----RYFGLSAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLV 161
|
....*....
gi 695729787 462 MDEPTNHLD 470
Cdd:PRK13537 162 LDEPTTGLD 170
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
339-527 |
1.33e-13 |
|
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: 72.07 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 339 NLLLEVGEKIAILGANGVGKSTMLKTLVGELQPD------NGTVkWSENAQ----------IGYYAQDheyefendLTVF 402
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDegeivlNGRT-LFDSRKgiflppekrrIGYVFQE--------ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 403 DWMS--------QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES- 473
Cdd:TIGR02142 88 PHLSvrgnlrygMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRk 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 474 ------IESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVVDFtGNYEDYLRSK 527
Cdd:TIGR02142 168 yeilpyLERLHAEFGI---PILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWASP 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-210 |
1.69e-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: 69.95 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKLRQD 72
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 qfafeefTVL--DTVimghaelwevkqeRDRI-YALAEMSEEDGY---KVAELETQYGEM-DGYsaEARAGELLLgvgip 145
Cdd:cd03253 84 -------TVLfnDTI-------------GYNIrYGRPDATDEEVIeaaKAAQIHDKIMRFpDGY--DTIVGERGL----- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 146 veqhygpmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03253 137 ---------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-245 |
1.75e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAfeeftvldtv 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 86 imghaelwevkqeRDRIYALAEMSEEDGYKVAELET-----QYGEMDGYSAEARAG--ELLLGVGI-PVEQHYgpMSEVA 157
Cdd:PRK10575 85 -------------RKVAYLPQQLPAAEGMTVRELVAigrypWHGALGRFGAADREKveEAISLVGLkPLAHRL--VDSLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNMV---CTHMADLDYGEL 230
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD---INMAaryCDYLVALRGGEM 226
|
250
....*....|....*
gi 695729787 231 rVYPGNYDEYMTAAT 245
Cdd:PRK10575 227 -IAQGTPAELMRGET 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
1.83e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLrqdqfaFE-------EFTVLDTV-----I 86
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVSAL------LElgagfhpELTGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 87 MGHAElWEVKQERDRIYALAEMSEedgykvaeletqYGEMdgysaearagelllgvgiPVeQHYgpmSevaPGWKLRVLL 166
Cdd:COG1134 116 LGLSR-KEIDEKFDEIVEFAELGD------------FIDQ------------------PV-KTY---S---SGMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 167 AQALFSNPDILLLDEptnNL---DID----TIRWLEQtLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:COG1134 158 AVATAVDPDILLVDE---VLavgDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-242 |
2.17e-13 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 70.02 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNE---RIGKLRQD 72
Cdd:cd03295 4 ENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPVElrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEEFTVLDTVIMghaelwevkqerdrIYALAEMSEEdgykvaeletqygemdgySAEARAGELLLGVGIPvEQHYG- 151
Cdd:cd03295 84 IGLFPHMTVEENIAL--------------VPKLLKWPKE------------------KIRERADELLALVGLD-PAEFAd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 --PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDRHFLNMVCTHM 222
Cdd:cd03295 131 ryP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELG---KTIVFVTHDIDEAFRLADRI 206
|
250 260
....*....|....*....|
gi 695729787 223 ADLDYGELRVYpGNYDEYMT 242
Cdd:cd03295 207 AIMKNGEIVQV-GTPDEILR 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-212 |
3.35e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 70.95 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD---------PNER-IGKLRQDqFA 75
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlpPRERrVGFVFQH-YA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 -FEEFTVLDTVIMGhaeLwevkqeRDRIYALAEmseedgykvaeletqygemdgysAEARAGELLLGVGIP-VEQHYgPm 153
Cdd:COG1118 86 lFPHMTVAENIAFG---L------RVRPPSKAE-----------------------IRARVEELLELVQLEgLADRY-P- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI---DTIR-WLEQTLNDRDSTMIIISHDR 212
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
330-510 |
4.51e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYAQ------DHE 392
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqQVSYCAQtptlfgDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 393 YefenDLTVFDWmsQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:PRK10247 98 Y----DNLIFPW--QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695729787 473 SIESLNMALEMY----QGTLIFVSHDREFVSSlATRVIEITP 510
Cdd:PRK10247 172 NKHNVNEIIHRYvreqNIAVLWVTHDKDEINH-ADKVITLQP 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
4.55e-13 |
|
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: 71.69 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP----NERIGKLR------ 70
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRqfinyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 -QDQFAFEEfTVLDTVIMGHAElwevKQERDRIYALAEMSEEDgykvAELEtqygemdgysaearagELLLGVGIPVEQH 149
Cdd:TIGR01193 554 pQEPYIFSG-SILENLLLGAKE----NVSQDEIWAACEIAEIK----DDIE----------------NMPLGYQTELSEE 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 150 YGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-IRWLEQTLNDRDSTMIIISH 210
Cdd:TIGR01193 609 GSSISG---GQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH 667
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-528 |
4.56e-13 |
|
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: 68.79 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 321 EVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQIGYYA 388
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDhEYEFENdlTVFDWMSQWKQEGDDEQAVrsILGRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMEKP 457
Cdd:cd03254 84 QD-TFLFSG--TIMENIRLGRPNATDEEVI--EAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 458 NILVMDEPTNHLDMESIESLNMALE--MYQGTLIFVSHdREFVSSLATRVIEITPERVVDfTGNYEDYLRSKG 528
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEklMKGRTSIIIAH-RLSTIKNADKILVLDDGKIIE-EGTHDELLAKKG 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
4.81e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnERIGKLRQDQFAFEEF 79
Cdd:PRK13651 6 KNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI-----EWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 -TVLDTVIMGHA---ELWEVKQERDRI--------YALAEMS-EEDgykVAELETQYGeMDGYSAEARAGELLLGVGIPV 146
Cdd:PRK13651 81 eKVLEKLVIQKTrfkKIKKIKEIRRRVgvvfqfaeYQLFEQTiEKD---IIFGPVSMG-VSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 EqhYGPMS--EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-IDTIRWLE--QTLNDRDSTMIIISHD 211
Cdd:PRK13651 157 S--YLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
5.08e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.35 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE---RIGKLRQDQFAFEEfT 80
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirdltLESlrrQIGVVPQDTFLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGH-----AELWEVKQE---RDRIYALaemseEDGYkvaelETQYGEmdgysaearAGELLLGvgipveqhygp 152
Cdd:COG1132 430 IRENIRYGRpdatdEEVEEAAKAaqaHEFIEAL-----PDGY-----DTVVGE---------RGVNLSG----------- 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 153 msevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:COG1132 480 ------GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-239 |
5.67e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS---LDPNErigklRQDQFAFEEftvldTVIMGHaelwe 94
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPFK-----RRKEFARRI-----GVVFGQ----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 95 vKQE-------RDRIYALAEMseedgYKVAELEtqygemdgysAEARAGEL--LLGVG----IPVEQhygpMSEvapGWK 161
Cdd:COG4586 104 -RSQlwwdlpaIDSFRLLKAI-----YRIPDAE----------YKKRLDELveLLDLGelldTPVRQ----LSL---GQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLN-DRDSTMIIISHDrhflnmvcthMAD----------LDY 227
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNrERGTTILLTSHD----------MDDiealcdrvivIDH 230
|
250
....*....|..
gi 695729787 228 GELrVYPGNYDE 239
Cdd:COG4586 231 GRI-IYDGSLEE 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-231 |
5.85e-13 |
|
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: 68.09 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------------PNER-IGKLRQDQFAFEEFTVLDTVIMGhAE 91
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlpPQQRkIGLVFQQYALFPHLNVRENLAFG-LK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 92 LWEVKQERDRIyalAEMSEedgykvaeletqygemdgysaearagelLLGVGIPVEQHYGPMSEvapGWKLRVLLAQALF 171
Cdd:cd03297 102 RKRNREDRISV---DELLD----------------------------LLGLDHLLNRYPAQLSG---GEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 172 SNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03297 148 AQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
6.68e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNE----RIGK 68
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaialGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQDqFA-FEEFTVLDTVIMGHAELWEVKQERDRIYAlaemseedgyKVAELETQYG-EMDgysAEARAGEllLGVGipv 146
Cdd:COG3845 85 VHQH-FMlVPNLTVAENIVLGLEPTKGGRLDRKAARA----------RIRELSERYGlDVD---PDAKVED--LSVG--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 147 EQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIISH 210
Cdd:COG3845 146 EQQ-------------RVEILKALYRGARILILDEPTAVLTpqeadelFEILR----RLAAEGKSIIFITH 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-514 |
9.54e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGP-LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSENaQI 384
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRS-KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 GYYAQDheyefeNDLTVFDwMSQWkqegDD---------------EQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRM-L 448
Cdd:PRK13647 82 GLVFQD------PDDQVFS-STVW----DDvafgpvnmgldkdevERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVaI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 449 FGKLMMEkPNILVMDEPTNHLDMESIESLNMALEMY--QG-TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13647 150 AGVLAMD-PDVIVLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-231 |
1.46e-12 |
|
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: 67.01 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNE---RIGKLRQDQFAFEEFTVldtvim 87
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkePAEarrRLGFVSDSTGLYDRLTA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 88 ghaelWEVKQERDRIYALAemseedgykvaeletqygemdGYSAEARAGEL--LLGVGIPVEQHYGPMSEvapGWKLRVL 165
Cdd:cd03266 96 -----RENLEYFAGLYGLK---------------------GDELTARLEELadRLGMEELLDRRVGGFST---GMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 166 LAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
320-508 |
1.58e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-------QIGYYAQD- 390
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 ----HEYEFENDLTVFDWMS---QWKQEGDDEQAVR-SILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:cd03292 81 gvvfQDFRLLPDRNVYENVAfalEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 463 DEPTNHLD-------MESIESLNMAlemyqGTLIFVS-HDREFVSSLATRVIEI 508
Cdd:cd03292 161 DEPTGNLDpdttweiMNLLKKINKA-----GTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
1.81e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.42 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVLDTVIMG---HAelwevkQERdriyalaeMSEEDGYKVAEletqygemdgysaearAGELL-LGvgiP 145
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpYS------KGR--------LTAEDREIIDE----------------AIAYLdLE---D 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 146 VEQHYgpMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG4604 128 LADRY--LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-244 |
2.07e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQDQF 74
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 AFEEFTVLDTVIMG---HAELWEVKQERDriyalaemseEDGYKVAELETQYGEMDGYSAEARAGelllgvgipveqhyg 151
Cdd:PRK10253 92 TPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKAMQATGITHLADQSVDTLSG--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 pmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDrhfLNMVC---THMAD 224
Cdd:PRK10253 147 -------GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQACryaSHLIA 216
|
250 260
....*....|....*....|
gi 695729787 225 LDYGELrVYPGNYDEYMTAA 244
Cdd:PRK10253 217 LREGKI-VAQGAPKEIVTAE 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-211 |
2.78e-12 |
|
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: 67.28 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 10 QFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNERIGKLRQDQFA--FEEF- 79
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamSRKELRELRRKKISmvFQSFa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 -----TVLDTVIMGhAELWEV-KQERdriyalaemseedgykvaeletqygemdgysaEARAGELLLGVGI-PVEQHYgp 152
Cdd:cd03294 113 llphrTVLENVAFG-LEVQGVpRAER--------------------------------EERAAEALELVGLeGWEHKY-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDiDTIRWLEQTL-----NDRDSTMIIISHD 211
Cdd:cd03294 158 PDELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRREMQDEllrlqAELQKTIVFITHD 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-216 |
2.84e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSkplF---ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL-----DPNE-----RIGKLRQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDiatrrRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 qfAF---EEFTV---LDTvimgHAelwevkqerdRIYALAEmsEEDGYKVAELETQYGEMDgySAEARAGELLLGVgipv 146
Cdd:NF033858 347 --AFslyGELTVrqnLEL----HA----------RLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSLPLGI---- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 eqhygpmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLD-----------IDtirwleqtLNDRDSTMIIIShdRHFL 215
Cdd:NF033858 403 --------------RQRLSLAVAVIHKPELLILDEPTSGVDpvardmfwrllIE--------LSREDGVTIFIS--THFM 458
|
.
gi 695729787 216 N 216
Cdd:NF033858 459 N 459
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-470 |
3.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK----------WSENAQIGYYA 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 Q----DHEYEFENDLTVFDwmsqwKQEGDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMEKPNILV 461
Cdd:PRK13536 121 QfdnlDLEFTVRENLLVFG-----RYFGMSTREIEAVIPSLLeFARLESKADARVsdLSGGMKRRLTLARALINDPQLLI 195
|
....*....
gi 695729787 462 MDEPTNHLD 470
Cdd:PRK13536 196 LDEPTTGLD 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
3.44e-12 |
|
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: 66.21 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFAFEEFTVLDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 89 HAELWEVKQERDRiyALAEMSEEDGykVAELetqygeMDGYSAEARAGElllgvgipveqhygpmsevapgwKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAEMLG--IDHL------LNRKPETLSGGE-----------------------QQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695729787 169 ALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
3.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 11 FGSKPLFEnISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpneRIGklrqdqfafeeftvlDTVIMGHA 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVG---------------DIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 91 ELWEVKQERDRI-----YALAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRVL 165
Cdd:PRK13643 75 KQKEIKPVRKKVgvvfqFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 166 LAQALFSNPDILLLDEPTNNLD----IDTIRWLEqTLNDRDSTMIIISH 210
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFE-SIHQSGQTVVLVTH 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-509 |
3.79e-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: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQDHEYEFENdLTVFDWMSQWKQ----- 410
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQN-YSLLPWLTVRENialav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 411 --------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMAL- 481
Cdd:TIGR01184 80 drvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELm 158
|
170 180 190
....*....|....*....|....*....|.
gi 695729787 482 ---EMYQGTLIFVSHDREFVSSLATRVIEIT 509
Cdd:TIGR01184 159 qiwEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
4.20e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKL-RQDQFAFEEftvldTVIMgha 90
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLnRAQRKAFRR-----DIQM--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 91 elweVKQE-------RDRIYALaemseedgykVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLR 163
Cdd:PRK10419 94 ----VFQDsisavnpRKTVREI----------IREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-187 |
4.48e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.14 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL--DP--------NERIGKLRQDQFA 75
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvpsrarhaRQRVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 FEEFTVLDTV-IMGHAELWEVKQERDRIYALAEMseedgykvAELETQygemdgysAEARAGELllgvgipveqhygpms 154
Cdd:PRK13537 92 DPDFTVRENLlVFGRYFGLSAAAARALVPPLLEF--------AKLENK--------ADAKVGEL---------------- 139
|
170 180 190
....*....|....*....|....*....|...
gi 695729787 155 evAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13537 140 --SGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
4.75e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdqfafeeftvlDTVIMGHAELWEVKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD---------------------DITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 99 RDRIYALAEMSE----EDGykvAELETQYG----EMDGYSAEARAGELLLGVGIP---VEQHYGPMSevapGWKLR-VLL 166
Cdd:PRK13646 84 RKRIGMVFQFPEsqlfEDT---VEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMS----GGQMRkIAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 167 AQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-210 |
5.11e-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: 65.71 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQD 72
Cdd:cd03251 5 NVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEEfTVLDTVIMGHAElwevkQERDRIYALAE--------MSEEDGYkvaelETQYGEmdgysaearAGELLLGvgi 144
Cdd:cd03251 85 VFLFND-TVAENIAYGRPG-----ATREEVEEAARaanahefiMELPEGY-----DTVIGE---------RGVKLSG--- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 145 pveqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03251 142 --------------GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAH 195
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
5.12e-12 |
|
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: 68.14 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQDQFAFEeft 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfGKHIGYLPQDVELFP--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 vlDTVIMGHAELWEVKQERDRIYA--LAEMSE-----EDGYkvaelETQYGEmdgysaearAGELLLGvgipveqhygpm 153
Cdd:TIGR01842 406 --GTVAENIARFGENADPEKIIEAakLAGVHElilrlPDGY-----DTVIGP---------GGATLSG------------ 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 154 sevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMV 218
Cdd:TIGR01842 458 -----GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlkaRGITVVVITHRPSLLGCV 520
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-218 |
5.33e-12 |
|
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: 68.24 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER---IGK 68
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwdREELgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQDQFAFEeftvlDTVimghaelwevkqeRDRIyalAEMSEEDGYKVAEletqygemdgysAEARAG--ELLL----GV 142
Cdd:COG4618 411 LPQDVELFD-----GTI-------------AENI---ARFGDADPEKVVA------------AAKLAGvhEMILrlpdGY 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 143 GIPVEQHYGPMSevaPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:COG4618 458 DTRIGEGGARLS---GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalkARGATVVVITHRPSLLAAV 533
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
317-494 |
5.72e-12 |
|
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: 68.24 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGF--DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---Q 383
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqWDREElgrH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHEYeFENdlTV------FDwmsqwkqEGDDEQAVRS---------ILgRLlfsqddikkP----------AKV 438
Cdd:COG4618 408 IGYLPQDVEL-FDG--TIaeniarFG-------DADPEKVVAAaklagvhemIL-RL---------PdgydtrigegGAR 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 439 LSGGEK-----GRMLFGKlmmekPNILVMDEPTNHLDMESIESLNMALEM--YQG-TLIFVSHD 494
Cdd:COG4618 468 LSGGQRqriglARALYGD-----PRLVVLDEPNSNLDDEGEAALAAAIRAlkARGaTVVVITHR 526
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-513 |
6.19e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW---------SENAQIGYYAQ 389
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 dhEYEFENDLTVFDWMSQW-----KQEGDDEQAVRSILGRLL----FSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:PRK10851 82 --HYALFRHMTVFDNIAFGltvlpRRERPNAAAIKAKVTQLLemvqLAHLADRYPAQ-LSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 461 VMDEPTNHLDMESIESLNMAL----EMYQGTLIFVSHDREFVSSLATRV-------IEI--TPERV 513
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVvvmsqgnIEQagTPDQV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
317-513 |
6.26e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK-----------WSENAQ 383
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHEYEF-------------ENDLTVFDWMSQWKQEGDDEQAVRSILGRllfsqddikKPAKvLSGGEKGRMLFG 450
Cdd:PRK13635 83 VGMVFQNPDNQFvgatvqddvafglENIGVPREEMVERVDQALRQVGMEDFLNR---------EPHR-LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 451 KLMMEKPNILVMDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSlATRVI---------EITPERV 513
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHDLDEAAQ-ADRVIvmnkgeileEGTPEEI 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
7.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIG 67
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeirkKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 68 KLRQD---QFAfeEFTVLDTVIMGhaelWEVKQErDRiyalAEMSEedgyKVAELETQYGeMDGYsaearagelllgvgI 144
Cdd:PRK13632 87 IIFQNpdnQFI--GATVEDDIAFG----LENKKV-PP----KKMKD----IIDDLAKKVG-MEDY--------------L 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 145 PVEQHYgpmseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13632 137 DKEPQN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
7.45e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 66.66 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DqFA-FEEFTVLDTVimghaelwevkqerdriyalaemseedgykvaeletQYG-EMDGYSAE---ARAGELLLGVGIpv 146
Cdd:COG3842 85 D-YAlFPHLTVAENV------------------------------------AFGlRMRGVPKAeirARVAELLELVGL-- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 147 eQHYG---PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDR 212
Cdd:COG3842 126 -EGLAdryP-HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
320-505 |
8.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.87 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPL-FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV-------KWSENA------QIG 385
Cdd:PRK13639 2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepiKYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQDHEYEF-----ENDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:PRK13639 82 IVFQNPDDQLfaptvEEDVA-FGPLNLGLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695729787 461 VMDEPTNHLD-MESIESLNMALEM-YQG-TLIFVSHDREFVSSLATRV 505
Cdd:PRK13639 160 VLDEPTSGLDpMGASQIMKLLYDLnKEGiTIIISTHDVDLVPVYADKV 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-187 |
1.14e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL----DPNE------RIGKLRQDQF 74
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpVPARarlaraRIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 AFEEFTVLDT-VIMGHAELWEVKQERDRIYALAEMseedgykvAELETQygemdgysAEARagelllgvgipveqhygpM 153
Cdd:PRK13536 125 LDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEF--------ARLESK--------ADAR------------------V 170
|
170 180 190
....*....|....*....|....*....|....
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13536 171 SDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-504 |
1.18e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDHEYEFEND------------LTVFDWMSQwkqegDDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMEK 456
Cdd:PRK09536 84 QDTSLSFEFDvrqvvemgrtphRSRFDTWTE-----TDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 695729787 457 PNILVMDEPTNHLDM-ESIESLNMALEMYQG--TLIFVSHDREfvssLATR 504
Cdd:PRK09536 158 TPVLLLDEPTASLDInHQVRTLELVRRLVDDgkTAVAAIHDLD----LAAR 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-239 |
1.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.52 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGklrqdqfafEEFT 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-----G---------EPLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDtvimghaelwevkqeRDRI-YalaeMSEEDGY----KVAELETQYGEMDGYS---AEARAGELL--LGVGipvEQHY 150
Cdd:COG4152 67 PED---------------RRRIgY----LPEERGLypkmKVGEQLVYLARLKGLSkaeAKRRADEWLerLGLG---DRAN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 151 GPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDrhfLNMV---CTHMAD 224
Cdd:COG4152 125 KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVireLAAKGTTVIFSSHQ---MELVeelCDRIVI 201
|
250
....*....|....*
gi 695729787 225 LDYGELRVYpGNYDE 239
Cdd:COG4152 202 INKGRKVLS-GSVDE 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
1.30e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD------PNERIGKLRQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 AFEEFTVLDTVIMGhaelwevkqerdriYALAEMSEEDgykvaeletqygemdgysAEARAGELLLGVGIP-VEQHYgpM 153
Cdd:PRK11248 81 LLPWRNVQDNVAFG--------------LQLAGVEKMQ------------------RLEIAHQMLKKVGLEgAEKRY--I 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTiRWLEQTL-----NDRDSTMIIISHD 211
Cdd:PRK11248 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-REQMQTLllklwQETGKQVLLITHD 188
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
1.80e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.01 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltalpPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMG-HAELWEVKQERDRIYALAEmseedgykvaeletQYGeMDGYsaEARAGELLLGvgipveqhy 150
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlRPGLKLTAEQRAQVEQALE--------------RVG-LAGL--LDRLPGQLSG--------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 151 gpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG3840 133 --------GQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-508 |
1.91e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQDHEYEFEnDL 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMFQ-DA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 TVFDWMS-----------QWKQEGddEQAVRSIlGRLLFSQDdikKPAkVLSGGEKGRMLFGKLMMEKPNILVMDEPTNH 468
Cdd:PRK11247 91 RLLPWKKvidnvglglkgQWRDAA--LQALAAV-GLADRANE---WPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695729787 469 LD------MES-IESLnmaLEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK11247 164 LDaltrieMQDlIESL---WQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
2.01e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIgklrqDQFAFEEFT 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-----DPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLdtvimGHaelwevkqeRDriyAL-AEMSeedgykVAE-LE---TQYGEMDGYSAEAragelLLGVGIPVEQH--YGPM 153
Cdd:PRK13539 77 YL-----GH---------RN---AMkPALT------VAEnLEfwaAFLGGEELDIAAA-----LEAVGLAPLAHlpFGYL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 695729787 154 SEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIR 192
Cdd:PRK13539 129 SA---GQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
320-466 |
2.02e-11 |
|
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: 63.85 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW----------SENAQ--IGYY 387
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditglppHRIARlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYeFENdLTVFD--WMSQWKqeGDDEQAVRSILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMEKPNIL 460
Cdd:COG0410 84 PEGRRI-FPS-LTVEEnlLLGAYA--RRDRAEVRADLERVyeLFPrlKERRRQRAGTLSGGEQ-QMLaIGRALMSRPKLL 158
|
....*.
gi 695729787 461 VMDEPT 466
Cdd:COG0410 159 LLDEPS 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
2.15e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 32 LIGANGSGKSTFMKILGGDLEPTLGNVSL--------DPNERiGKLRQDQ--FAFEEFTVLDTVimghaelweVKQERDR 101
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEAR-AKLRAKHvgFVFQSFMLIPTL---------NALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 102 IYALAEmseedgykvaeletqyGEMDGYSAEaRAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
Cdd:PRK10584 111 LPALLR----------------GESSRQSRN-GAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 695729787 182 PTNNLDIDT---IRWLEQTLN-DRDSTMIIISHD 211
Cdd:PRK10584 173 PTGNLDRQTgdkIADLLFSLNrEHGTTLILVTHD 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-514 |
2.45e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLF---------KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------ENAQ 383
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHEYEFENDLTVFdwmsqwkqegDDEQAVRSILG---RLLFSQDDIKKPAKV--------------------LS 440
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAV----------NPRKTVREIIReplRHLLSLDKAERLARAsemlravdlddsvldkrppqLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 441 GGEKGRMLFGKLMMEKPNILVMDEPTNHLDM---ESIESLNMALEMYQGT-LIFVSHDREFVSSLATRVI-----EITPE 511
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMvmdngQIVET 233
|
...
gi 695729787 512 RVV 514
Cdd:PRK10419 234 QPV 236
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-511 |
2.67e-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: 63.01 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 349 AILGANGVGKSTMLK----TLVGELQPDNGTVKWS-----ENAQIGYYaqdhEYEFENDltvfdwmsqwkqEGDDEQAVR 419
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDpklirEGEVRAQV----KLAFENA------------NGKKYTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 420 S--ILGRLLF-SQDDIKKPA----KVLSGGEKgrMLFG--------KLMMEKPNILVMDEPTNHLDMESIE-SLNMALEM 483
Cdd:cd03240 90 SlaILENVIFcHQGESNWPLldmrGRCSGGEK--VLASliirlalaETFGSNCGILALDEPTTNLDEENIEeSLAEIIEE 167
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 484 YQGTLIF----VSHDREFVsSLATRVIEITPE 511
Cdd:cd03240 168 RKSQKNFqlivITHDEELV-DAADHIYRVEKD 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
3.05e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 11 FGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnerigklrqdqfafeeftvlDTVIMGHA 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD---------------------DTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 91 ELWEVKQERDRI-----YALAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYGPMSEVAPGWKLRVL 165
Cdd:PRK13649 76 KNKDIKQIRKKVglvfqFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180
....*....|....*....|..
gi 695729787 166 LAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-514 |
4.14e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ-----IGYYAQDHEYEF-----ENDL 399
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENIRevrkfVGLVFQNPDDQIfsptvEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 TvFDWMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESL-- 477
Cdd:PRK13652 101 A-FGPINLGLDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELid 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 695729787 478 --NMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13652 179 flNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-470 |
4.22e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WS--ENAQI-GYY 387
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSpaELARRrAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYEFenDLTVFD--WM--SQWKQ-EGDDEQAVRSIL---------GRLLfsqddikkPAkvLSGGEKGRMLFGKLM 453
Cdd:PRK13548 82 PQHSSLSF--PFTVEEvvAMgrAPHGLsRAEDDALVAAALaqvdlahlaGRDY--------PQ--LSGGEQQRVQLARVL 149
|
170 180
....*....|....*....|...
gi 695729787 454 M------EKPNILVMDEPTNHLD 470
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALD 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-210 |
4.84e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 62.89 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErIGKL------RQDQFAFEEFTVLDTVIMGHAE 91
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD-LALAdpawlrRQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 92 LWEVKQERDRIYALAEMSEEDGYkVAELETQYGEMDGYSaearagelllGVGIpveqhygpmsevAPGWKLRVLLAQALF 171
Cdd:cd03252 98 LADPGMSMERVIEAAKLAGAHDF-ISELPEGYDTIVGEQ----------GAGL------------SGGQRQRIAIARALI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 172 SNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDicAGRTVIIIAH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-508 |
5.10e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 313 KKLF-RNALEVEALtkgfdegplfKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSenaqiGYYAQDH 391
Cdd:COG4586 25 KGLFrREYREVEAV----------DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVPFKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLT-VFDWMSQ--WkqegD----------------DEQAVRSILGRL--LFSQDDI-KKPAKVLSGGEKGRMLF 449
Cdd:COG4586 90 RKEFARRIGvVFGQRSQlwW----DlpaidsfrllkaiyriPDAEYKKRLDELveLLDLGELlDTPVRQLSLGQRMRCEL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 450 GKLMMEKPNILVMDEPTNHLDMES-------IESLNmalEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSkeairefLKEYN---RERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-212 |
5.14e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErigklrqdqfafeeftV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED----------------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 LDTVImghaelwevkQERD-----RIYAL-AEMS--EEDGYKVAELETQYGEMDGYSAEARAGELLLGVgipvEQHYgpM 153
Cdd:PRK11432 71 THRSI----------QQRDicmvfQSYALfPHMSlgENVGYGLKMLGVPKEERKQRVKEALELVDLAGF----EDRY--V 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDR 212
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFN---ITSLYVTHDQ 197
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-506 |
5.24e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PL----FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA------------ 382
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 383 -----------------------QIGYYAQDHEYEF-----ENDLtVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKK 434
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrRVGVVFQFAEYQLfeqtiEKDI-IFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 435 PAKVLSGGEKGRM-LFGKLMMEkPNILVMDEPTNHLDME-SIESLNMALEMYQG--TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13651 162 SPFELSGGQKRRVaLAGILAME-PDFLVFDEPTAGLDPQgVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRTI 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-235 |
5.48e-11 |
|
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: 62.67 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 3 VTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEP---TLGNVSLDPNER--------IGKLRQ 71
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRkpdqfqkcVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVimghaelwevkqerdriyalaemseedgYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQHYg 151
Cdd:cd03234 89 DDILLPGLTVRETL----------------------------TYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGN- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHD------RHFlnmvcTHM 222
Cdd:cd03234 140 LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlarRNRIVILTIHQprsdlfRLF-----DRI 214
|
250
....*....|...
gi 695729787 223 ADLDYGELrVYPG 235
Cdd:cd03234 215 LLLSSGEI-VYSG 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-243 |
5.59e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPneRIGKLRQDQFAFEEFTVLDT 84
Cdd:PRK14246 14 SRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 VIMghaelweVKQERDriyALAEMSEEDgyKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQH---YGPMSEVAPGWK 161
Cdd:PRK14246 92 VGM-------VFQQPN---PFPHLSIYD--NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVARVADYVAFLYNGEL-VEWGSSNE 238
|
....
gi 695729787 240 YMTA 243
Cdd:PRK14246 239 IFTS 242
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-210 |
6.30e-11 |
|
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: 62.24 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKLRQDQ 73
Cdd:cd03254 7 NVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 FAFEEfTVLDTVIMGH--AELWEVKQERDRIYALAE-MSEEDGYkvaelETQYGEmdgysaearAGELLlgvgipveqhy 150
Cdd:cd03254 87 FLFSG-TIMENIRLGRpnATDEEVIEAAKEAGAHDFiMKLPNGY-----DTVLGE---------NGGNL----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 151 gpmSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRdsTMIIISH 210
Cdd:cd03254 141 ---SQ---GERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGR--TSIIIAH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
7.63e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.56 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL---DPNERIGKLRQDQFAFEEF-- 79
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtDVSRLHARDRKVGFVFQHYal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 ----TVLDTVIMGHAELweVKQERDRIYALAemseedgYKVaeleTQYGEMDGYSAEAragelllgvgipveQHYgPmSE 155
Cdd:PRK10851 86 frhmTVFDNIAFGLTVL--PRRERPNAAAIK-------AKV----TQLLEMVQLAHLA--------------DRY-P-AQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDR 212
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-506 |
7.73e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYAQd 390
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaENRHVNTVFQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 hEYEFENDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:PRK09452 94 -SYALFPHMTVFENVAfglrmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 466 TNHLDMESIESLNMALEMYQGTL----IFVSHDREFVSSLATRVI 506
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLgitfVFVTHDQEEALTMSDRIV 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
326-506 |
7.75e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 326 TKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG-------ELQPDNGTVKWSENAQ--IGYYAQdhEYEFE 396
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDLFIGEKRMNDVPPAErgVGMVFQ--SYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 NDLTVFDWMS-------QWKQEGDD--EQAVRSI-LGRLLfsqddIKKPaKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:PRK11000 88 PHLSVAENMSfglklagAKKEEINQrvNQVAEVLqLAHLL-----DRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695729787 467 NHLD------MES-IESLNMALemyQGTLIFVSHDREFVSSLATRVI 506
Cdd:PRK11000 162 SNLDaalrvqMRIeISRLHKRL---GRTMIYVTHDQVEAMTLADKIV 205
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-493 |
8.42e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 303 QNPFIRF--EQDKKLFRNALEVEALTKGFDEG--PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK- 377
Cdd:PRK11160 320 QKPEVTFptTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 378 -------WSENA---QIGYYAQdHEYEFENdlTVFDWMSQWKQEGDDEQAVRSI----LGRLLfsQDD------IKKPAK 437
Cdd:PRK11160 400 ngqpiadYSEAAlrqAISVVSQ-RVHLFSA--TLRDNLLLAAPNASDEALIEVLqqvgLEKLL--EDDkglnawLGEGGR 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 438 VLSGGEKGRM-LFGKLMMEKPnILVMDEPTNHLDMESiESLNMAL--EMYQG-TLIFVSH 493
Cdd:PRK11160 475 QLSGGEQRRLgIARALLHDAP-LLLLDEPTEGLDAET-ERQILELlaEHAQNkTVLMITH 532
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-514 |
8.91e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 338 FNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENaqigyyaQDHEYE----------F-ENDLtvFDWMS 406
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG-------QDHTTTppsrrpvsmlFqENNL--FSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 407 QW-----------KQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGK-LMMEKPnILVMDEPTNHLD---- 470
Cdd:PRK10771 88 VAqniglglnpglKLNAAQREKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARcLVREQP-ILLLDEPFSALDpalr 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695729787 471 MESIESLNMALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-210 |
1.01e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPTlGNVSldpneriGKLRQDQFAFEEFTVLDT- 84
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYE-------GEIIFEGEELQASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 ----VIMgHAELWEVKqerdriyalaEMS-EEDGYKVAELeTQYGEMDGYSAEARAGELL--LGVGIPVEQhygPMSEVA 157
Cdd:PRK13549 81 ragiAII-HQELALVK----------ELSvLENIFLGNEI-TPGGIMDYDAMYLRAQKLLaqLKLDINPAT---PVGNLG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-211 |
1.06e-10 |
|
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: 62.45 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------SLDPnERIGKLRQ------ 71
Cdd:TIGR04520 5 NVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVtvdgldTLDE-ENLWEIRKkvgmvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 ----DQF--AfeefTVLDTVIMGhAELWEVKQE--RDRIY-ALAEMseedgykvaeletqygEMDGYsaEARAGELLLGv 142
Cdd:TIGR04520 84 qnpdNQFvgA----TVEDDVAFG-LENLGVPREemRKRVDeALKLV----------------GMEDF--RDREPHLLSG- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 143 gipveqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHD 211
Cdd:TIGR04520 140 ----------------GQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNK---EEGITVISITHD 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-514 |
1.23e-10 |
|
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: 63.67 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG--ELQPDNGTVKWS------------------ 379
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 380 ---------ENAQIGYYAQDHEYE-----------------FENDLT---VFDWMSQWKQEGDDEQAVRSILGRLLFSQD 430
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRrrirkriaimlqrtfalYGDDTVldnVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 431 DIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEM----YQGTLIFVSHDREFVSSLATRVI 506
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*..
gi 695729787 507 ---------EITPERVV 514
Cdd:TIGR03269 241 wlengeikeEGTPDEVV 257
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-505 |
1.25e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPL----FKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------------E 380
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 381 NAQIGYYAQDHEyeFENDLTVFDWMSQ-----WKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMME 455
Cdd:PRK11629 86 NQKLGFIYQFHH--LLPDFTALENVAMplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 456 KPNILVMDEPTNHLDM---ESIESLNMALEMYQGT-LIFVSHDREFVSSLATRV 505
Cdd:PRK11629 163 NPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHDLQLAKRMSRQL 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-529 |
1.35e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.48 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDhEYEFeND 398
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaSLRRQIGLVSQD-VFLF-ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 lTVFDWMSQWKQEGDDEQAVRSilGRLLFSQDDIKK-PAKV----------LSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:cd03251 91 -TVAENIAYGRPGATREEVEEA--ARAANAHEFIMElPEGYdtvigergvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 468 HLDMESIESLNMALE--MYQGTLIFVSHDREFVSSlATRVIEITPERVVDfTGNYEDYLRSKGI 529
Cdd:cd03251 168 ALDTESERLVQAALErlMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE-RGTHEELLAQGGV 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
319-516 |
1.57e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaQIGyyaqDHEYEFEND 398
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------NIA----GHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 LT-------------VFDWMSQW--------------------KQEGDDEQAvrSILGRLLFSQDDIKKPAKvLSGGEKG 445
Cdd:COG4161 72 PSekairllrqkvgmVFQQYNLWphltvmenlieapckvlglsKEQAREKAM--KLLARLRLTDKADRFPLH-LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 446 RMLFGKLMMEKPNILVMDEPTNHLDME-SIESLNMALEMYQG--TLIFVSHDREFVSSLATRVIEITPERVVDF 516
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-473 |
1.73e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNG----------TVKWS---------E 380
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREgrlardirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 381 NAQIGYYAQdhEYEFENDLTVFD------------WMS--QWKQEGDDEQAVRSI--LGRLLFSQDDIkkpaKVLSGGEK 444
Cdd:PRK09984 85 RANTGYIFQ--QFNLVNRLSVLEnvligalgstpfWRTcfSWFTREQKQRALQALtrVGMVHFAHQRV----STLSGGQQ 158
|
170 180
....*....|....*....|....*....
gi 695729787 445 GRMLFGKLMMEKPNILVMDEPTNHLDMES 473
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.87e-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: 60.23 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNVSLDpNERIGKLRQDqfafeef 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK-GEDITDLPPE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 tvldtvimghaelwevkqERDR--IYALAEMSEE-DGYKVAELETQYGEmdGYSAearaGElllgvgipveqhygpmsev 156
Cdd:cd03217 73 ------------------ERARlgIFLAFQYPPEiPGVKNADFLRYVNE--GFSG----GE------------------- 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 157 apgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:cd03217 110 ----KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINklrEEGKSVLIITHYQRLLDYI 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-526 |
2.13e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.16 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIGYY 387
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgedireQDPVElrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQD-----HEYEFENDLTVFDwMSQWKQEGDDEQAVRSI----LGRLLFSQddiKKPAKvLSGGEKGRMLFGKLMMEKPN 458
Cdd:cd03295 81 IQQiglfpHMTVEENIALVPK-LLKWPKEKIRERADELLalvgLDPAEFAD---RYPHE-LSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 459 ILVMDEPTNHLDMESIESLNMALEMYQ----GTLIFVSHDREFVSSLATRVIEITPERVVDFtGNYEDYLRS 526
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILRS 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-210 |
2.41e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 60.63 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKP---LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN-----------ERIGKLR 70
Cdd:cd03249 4 KNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 QDQFAFEEfTVLDTVIMGHAElwEVKQERDRIYALAE-----MSEEDGYkvaelETQYGEmdgysaearAGELLLGvgip 145
Cdd:cd03249 84 QEPVLFDG-TIAENIRYGKPD--ATDEEVEEAAKKANihdfiMSLPDGY-----DTLVGE---------RGSQLSG---- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 146 veqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03249 143 -------------GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRamKGRTTIVIAH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-219 |
2.45e-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: 62.92 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG-------------DLEPtLGNVSLDPNER-- 65
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSP-LKASNIRDTERag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 66 IGKLRQDQFAFEEFTVLDTVIMGHaelwevkqerdriyalaemseedgykvaELETQYGEMDGYSAEARAGELLLGVGIP 145
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGN----------------------------EITLPGGRMAYNAMYLRAKNLLRELQLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 146 VEQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlndRDSTMIIISHDRHFLNMV 218
Cdd:TIGR02633 132 ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTeketeilLDIIRDLKA----HGVACVYISHKLNEVKAV 207
|
.
gi 695729787 219 C 219
Cdd:TIGR02633 208 C 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
316-529 |
2.53e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.87 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 316 FRNALEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQ 383
Cdd:COG1132 336 VRGEIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleSLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHeyefendlTVFDwmsqwkqegddeqavRSI-----LGRLLFSQDDIKKPAKV-------------------- 438
Cdd:COG1132 416 IGVVPQDT--------FLFS---------------GTIrenirYGRPDATDEEVEEAAKAaqahefiealpdgydtvvge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 439 ----LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMAL-EMYQG-TLIFVSHdRefVSSL--ATRVIEITP 510
Cdd:COG1132 473 rgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALeRLMKGrTTIVIAH-R--LSTIrnADRILVLDD 549
|
250
....*....|....*....
gi 695729787 511 ERVVDfTGNYEDYLRSKGI 529
Cdd:COG1132 550 GRIVE-QGTHEELLARGGL 567
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-211 |
2.66e-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: 60.71 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFA 75
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 FEEFTVLDTVIMGhaelwevkqerdriYALAEMSEEDgykvaeletqygemdgysAEARAGELLLGVGIPVEQHYGPmSE 155
Cdd:cd03300 84 FPHLTVFENIAFG--------------LRLKKLPKAE------------------IKERVAEALDLVQLEGYANRKP-SQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLE---QTLNDR-DSTMIIISHD 211
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKElGITFVFVTHD 190
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-242 |
3.02e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFafeeftvldtvimgHAEL 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVQYDHHYL--------------HRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 93 WEVKQE--------RDRI-YALAEMSEEDGYKVAELEtqygemdgySAEARAGELLLGVGIPVEQHYGPMSevaPGWKLR 163
Cdd:TIGR00958 558 ALVGQEpvlfsgsvRENIaYGLTDTPDEEIMAAAKAA---------NAHDFIMEFPNGYDTEVGEKGSQLS---GGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMvCTHMADLDYGELrVYPGNYDEYMT 242
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGTHKQLME 702
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-529 |
3.46e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 60.32 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG-PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYY 387
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDheyefendlTV-FDwmsqwkqegddeqavRSIL-----GRLLFSQDDIKKPAKV----------------------- 438
Cdd:cd03253 81 PQD---------TVlFN---------------DTIGyniryGRPDATDEEVIEAAKAaqihdkimrfpdgydtivgergl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 439 -LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD----MESIESLNmalEMYQG-TLIFVSHDREFVSSlATRVIEITPER 512
Cdd:cd03253 137 kLSGGEKQRVAIARAILKNPPILLLDEATSALDthteREIQAALR---DVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
250
....*....|....*..
gi 695729787 513 VVDfTGNYEDYLRSKGI 529
Cdd:cd03253 213 IVE-RGTHEELLAKGGL 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
318-504 |
3.93e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENAQIG 385
Cdd:PRK10584 5 NIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQDHEYEFENDLTV----------FDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMME 455
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIptlnalenveLPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695729787 456 KPNILVMDEPTNHLDM---ESIESLNMALEM-YQGTLIFVSHDrefvSSLATR 504
Cdd:PRK10584 164 RPDVLFADEPTGNLDRqtgDKIADLLFSLNReHGTTLILVTHD----LQLAAR 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-506 |
3.96e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.90 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFD---EGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQ 383
Cdd:PRK13650 3 NIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQDHEYEF-----ENDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPN 458
Cdd:PRK13650 83 IGMVFQNPDNQFvgatvEDDVA-FGLENKGIPHEEMKERVNEALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 459 ILVMDEPTNHLD----MESIESLNMALEMYQGTLIFVSHDREFVsSLATRVI 506
Cdd:PRK13650 161 IIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
4.45e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 17 FENISVKFGGGNR-----------------YGLIGANGSGKSTFMKILGGdLE-PTLGNV--------SLDPNERIgKLR 70
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINL-LErPTSGSVlvdgvdltALSERELR-AAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 QD------QFA-FEEFTVLDTVimghA---ELWEV-KQERdriyalaemseedgykvaeletqygemdgysaEARAGELL 139
Cdd:COG1135 82 RKigmifqHFNlLSSRTVAENV----AlplEIAGVpKAEI--------------------------------RKRVAELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 140 LGVGIPVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IrwLE--QTLNDR-DSTMIIISHDRH 213
Cdd:COG1135 126 ELVGLSDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LDllKDINRElGLTIVLITHEMD 202
|
250
....*....|....*..
gi 695729787 214 FLNMVCTHMADLDYGEL 230
Cdd:COG1135 203 VVRRICDRVAVLENGRI 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-210 |
5.37e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 17 FENISVKFGG-------------GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERigklrqdQFAFEEFTVLD 83
Cdd:PRK11288 7 FDGIGKTFPGvkalddisfdcraGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-------RFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 TVIMGHAELWEVkqerdriyalAEMSeedgykVAE------LETQYGEMDGYSAEARAGELLLGVGIPVEQHyGPMSEVA 157
Cdd:PRK11288 80 GVAIIYQELHLV----------PEMT------VAEnlylgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPD-TPLKYLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-211 |
5.58e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 7 VTMQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQDQFAF----EE---- 78
Cdd:PRK15056 14 VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpqsEEvdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 79 FTVL--DTVIM---GHAELWEVKQERDRiyalaemseedgykvaeletqygemdgysaeARAGELLLGVGIpVEQHYGPM 153
Cdd:PRK15056 93 FPVLveDVVMMgryGHMGWLRRAKKRDR-------------------------------QIVTAALARVDM-VEFRHRQI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK15056 141 GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-187 |
5.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP--------NERIGKLRQD-----QFA----FEEfTV 81
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkkNKKLKPLRKKvgivfQFPehqlFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 LDTVIMGHAELwevkqerdriyalaEMSEEDgykvaeletqygemdgysAEARAGELLLGVGIPVE-QHYGPMsEVAPGW 160
Cdd:PRK13634 104 EKDICFGPMNF--------------GVSEED------------------AKQKAREMIELVGLPEElLARSPF-ELSGGQ 150
|
170 180
....*....|....*....|....*..
gi 695729787 161 KLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-210 |
5.79e-10 |
|
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: 59.43 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--PNERIG--KLR-------QD 72
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvDISKIGlhDLRsrisiipQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEeftvlDTVimghaelwevkqeRDRIYALAEMSEEDGYKVAE-------LETQYGEMDGYSAEaraGELLLGVGIp 145
Cdd:cd03244 87 PVLFS-----GTI-------------RSNLDPFGEYSDEELWQALErvglkefVESLPGGLDTVVEE---GGENLSVGQ- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 146 veqhygpmsevapgwklRVL--LAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03244 145 -----------------RQLlcLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
318-506 |
5.82e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYA 388
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDHEYEFENDLT-VFDWMSQW--------------------KQEGDdEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRM 447
Cdd:PRK10619 84 KNQLRLLRTRLTmVFQHFNLWshmtvlenvmeapiqvlglsKQEAR-ERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 448 LFGKLMMEKPNILVMDEPTNHLDMESI-ESLNMALEMYQ--GTLIFVSHDREFVSSLATRVI 506
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVI 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-514 |
6.83e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 307 IRFEQDKKLF---RNALEvealtkgfdegplfkNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------- 376
Cdd:PRK10908 2 IRFEHVSKAYlggRQALQ---------------GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 377 ---KWSE----NAQIGYYAQDHEYEFenDLTVFDWMS-----QWKQEGDDEQAVRSILGR--LLfsqDDIKKPAKVLSGG 442
Cdd:PRK10908 67 trlKNREvpflRRQIGMIFQDHHLLM--DRTVYDNVAipliiAGASGDDIRRRVSAALDKvgLL---DKAKNFPIQLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 443 EKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-471 |
7.01e-10 |
|
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: 61.85 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSenAQIGYYAQdheyefendltvFDWMSQWKQEG 412
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--GRISFSPQ------------TSWIMPGTIKD 505
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 413 D-------DEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM 471
Cdd:TIGR01271 506 NiifglsyDEYRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-514 |
7.12e-10 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 59.52 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA----- 382
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 383 -QIGYYAQdhEYEFENDLTVFD----WMSQWKQEGDD-EQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEK 456
Cdd:cd03258 82 rRIGMIFQ--HFNLLSSRTVFEnvalPLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQ-LSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 457 PNILVMDEPTNHLDMESIES-LNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSiLALLRDINRElglTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-470 |
7.95e-10 |
|
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: 58.33 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEV------GEKIAILGANGVGKSTMLKTLVGELQP--DNGTV--------KWSENAQ 383
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVsgkakpGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 384 IGYYAQD---HEYefendLTVfdwmsqwkqegddEQAvrsilgrLLFSqddikkpAKV--LSGGEKGRMLFGKLMMEKPN 458
Cdd:cd03213 84 IGYVPQDdilHPT-----LTV-------------RET-------LMFA-------AKLrgLSGGERKRVSIALELVSNPS 131
|
170
....*....|..
gi 695729787 459 ILVMDEPTNHLD 470
Cdd:cd03213 132 LLFLDEPTSGLD 143
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-528 |
8.26e-10 |
|
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: 59.42 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQIGYYAQdheyefEND 398
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGVVLQ------ENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 L---TVFDWMSQwkqeGDDEQAVRSIL--GRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:cd03252 87 LfnrSIRDNIAL----ADPGMSMERVIeaAKLAGAHDFISElpegydtivgeQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 463 DEPTNHLDMESIESL--NMALEMYQGTLIFVSHDREFVSSlATRVIEITPERVVDfTGNYEDYLRSKG 528
Cdd:cd03252 163 DEATSALDYESEHAImrNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAENG 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-514 |
8.57e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 318 NALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQDHEYE--- 394
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 -----FEN-----DLTVFDWMSQWKQEGDD--EQAVRS-ILGRL----LFSQDDIkKPAKvLSGGEKGRMLFGKLMMEKP 457
Cdd:PRK11831 85 rmsmlFQSgalftDMNVFDNVAYPLREHTQlpAPLLHStVMMKLeavgLRGAAKL-MPSE-LSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 458 NILVMDEP-------TNHLDMESIESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK11831 163 DLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-210 |
8.79e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNER------------IGKLRQDQ 73
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaaqlgIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 74 FAFEEFTVLDTVIMGHAELWEVKqerdriyalaemseedGYKVAEletqYGEMdgysaEARAGELLLGVGIPVEQHYgPM 153
Cdd:PRK09700 90 SVIDELTVLENLYIGRHLTKKVC----------------GVNIID----WREM-----RVRAAMMLLRVGLKVDLDE-KV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK09700 144 ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-210 |
8.85e-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: 58.66 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQDQFA 75
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 FEEFTVLDTVIMGHA---ELWEVKQERDRIyALAEMSeedgykVAELETQygemdgysaeaRAGELllgvgipveqhygp 152
Cdd:cd03298 82 FAHLTVEQNVGLGLSpglKLTAEDRQAIEV-ALARVG------LAGLEKR-----------LPGEL-------------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 153 msevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISH 210
Cdd:cd03298 130 ----SGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhaeTKMTVLMVTH 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
9.52e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 57.71 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--PNERIGKLRQDQFAFe 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDgvPVSDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 78 eftvldtvimghaelweVKQerdRIYALaemseedgykvaeletqygemdgysaearAGELLLGVGIPveqhygpmseVA 157
Cdd:cd03247 80 -----------------LNQ---RPYLF-----------------------------DTTLRNNLGRR----------FS 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITH 155
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
9.52e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpnERIGKLRQdqfafeeft 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR--MRDGQLRD--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 vldtvimghaelwevkqerdriyaLAEMSEedgykvAE----LETQYG-----EMDGY----SAEARAGELLLGVGipvE 147
Cdd:PRK11701 75 ------------------------LYALSE------AErrrlLRTEWGfvhqhPRDGLrmqvSAGGNIGERLMAVG---A 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 148 QHYGPMSEVAPGWKLRVLLAQA----------------------LFSNPDILLLDEPTNNLDI-------DTIRWLEQTL 198
Cdd:PRK11701 122 RHYGDIRATAGDWLERVEIDAAriddlpttfsggmqqrlqiarnLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL 201
|
250
....*....|...
gi 695729787 199 ndrDSTMIIISHD 211
Cdd:PRK11701 202 ---GLAVVIVTHD 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-525 |
9.74e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDrhfLNMVcthmadldygelr 231
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilQLLRELQQELN---MGLLFITHN---LSIV------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 232 vypgnydeymtaatqareRLLADNakkkaqIADLQS--FVSRFSANASKSRQATSRARQIdkikleeVKASSRQNPFIRF 309
Cdd:PRK15134 221 ------------------RKLADR------VAVMQNgrCVEQNRAATLFSAPTHPYTQKL-------LNSEPSGDPVPLP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 310 EQDKKLfrnaLEVEALTKGF-----------DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLV------GELQPD 372
Cdd:PRK15134 270 EPASPL----LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIWFD 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 373 NGTV-KWSENA------QIGYYAQDHEYEFENDLTVFdwmsQWKQEG-----------DDEQAVRSILGRLLFSQDDIKK 434
Cdd:PRK15134 346 GQPLhNLNRRQllpvrhRIQVVFQDPNSSLNPRLNVL----QIIEEGlrvhqptlsaaQREQQVIAVMEEVGLDPETRHR 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 435 PAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD---MESIESLNMAL-EMYQGTLIFVSHDREFVSSLATRVIEITP 510
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
410 420
....*....|....*....|..
gi 695729787 511 ERVVD-------FTGNYEDYLR 525
Cdd:PRK15134 502 GEVVEqgdcervFAAPQQEYTR 523
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-471 |
1.12e-09 |
|
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: 59.49 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSenAQIGYYAQdheyefendltvFDW-MSQWKQE 411
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--GRISFSSQ------------FSWiMPGTIKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 412 G------DDEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM 471
Cdd:cd03291 117 NiifgvsYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-493 |
1.30e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGelqpdngtvkwsenaqigyyaqDHEYEFENDL 399
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------------------HPKYEVTEGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 TVFDwmsqwkqeGDD----EQAVRSILGRLLFSQDDIKKPA-KV----------LSGGEKGRMLFGKLMMEKPNILVMDE 464
Cdd:cd03217 59 ILFK--------GEDitdlPPEERARLGIFLAFQYPPEIPGvKNadflryvnegFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 465 PTNHLDMESIESLNMALEMYQG---TLIFVSH 493
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-210 |
1.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.29 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 9 MQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV---SLDPNERIGKLRQDQ------FAFEEF 79
Cdd:PRK13637 16 TPFEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidGVDITDKKVKLSDIRkkvglvFQYPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 tvldtvimghaELWEVKQERDRIYALAEMSEEDGykvaELETqygemdgysaeaRAGELLLGVGIPVEQhYGPMS--EVA 157
Cdd:PRK13637 95 -----------QLFEETIEKDIAFGPINLGLSEE----EIEN------------RVKRAMNIVGLDYED-YKDKSpfELS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDR-DSTMIIISH 210
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKEyNMTIILVSH 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
339-506 |
1.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.26 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 339 NLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---------------QIGYYAQDHEYE-FENdlTV- 401
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQlFEE--TVe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 ----FDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRM-LFGKLMMEkPNILVMDEPTNHLD------ 470
Cdd:PRK13634 105 kdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVaIAGVLAME-PEVLVLDEPTAGLDpkgrke 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 695729787 471 -MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:PRK13634 184 mMEMFYKLHKEKGL---TTVLVTHSMEDAARYADQIV 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-521 |
1.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 337 NFNLLLEVGEKIAILGANGVGKSTMLK------------TLVGELQPDNGTVKWSE----NAQIGYYAQDHEYEFENDLT 400
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEvkrlRKEIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 VFDWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIES 476
Cdd:PRK13645 109 EKDIAFGPVNLGENKQEAYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 477 -LNMALEM---YQGTLIFVSHDREFVSSLATRVIEITPERVVDFTGNYE 521
Cdd:PRK13645 189 fINLFERLnkeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-187 |
1.87e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvpPYQRpINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMGhaelweVKQERdriYALAEMSeedgykvaeletqygemdgysaeARAGELLLGVGIPVEQHYG 151
Cdd:PRK11607 99 SYALFPHMTVEQNIAFG------LKQDK---LPKAEIA-----------------------SRVNEMLGLVHMQEFAKRK 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 695729787 152 PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK11607 147 P-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
2.01e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.48 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV-----SLDPNER-IGKLRQdqf 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRgLLALRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 afeeftvldtvimghaELWEVKQERDRIYALAEMSEEDGYKVAELETQYGEMdgysaEARAGELLLGVGipvEQHY--GP 152
Cdd:PRK13638 78 ----------------QVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEI-----TRRVDEALTLVD---AQHFrhQP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNDrdstMIIISHDRHFLNMVCTHMADL 225
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVL 209
|
250
....*....|..
gi 695729787 226 DYGELRVY--PG 235
Cdd:PRK13638 210 RQGQILTHgaPG 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
2.62e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLEPTL---GNVSLD------PNERIGKL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVtitGSIVYNghniysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQD-QFAFEE-----FTVLDTVIMGhaelWEVKQERDRiyALAEMSEEDGYKVAELETQYGEMDGYSAEARAGelllgvg 143
Cdd:PRK14239 85 RKEiGMVFQQpnpfpMSIYENVVYG----LRLKGIKDK--QVLDEAVEKSLKGASIWDEVKDRLHDSALGLSG------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 144 ipveqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK14239 152 ---------------GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGlkDDYTMLLVTR 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
320-495 |
2.70e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW---SENAQIGYYAQD-----H 391
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKQlcfvgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLTV-----FDWMSQWKQEGDDEqavrsiLGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:PRK13540 82 RSGINPYLTLrenclYDIHFSPGAVGITE------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 467 NHLDMESIESLNMALEMYQ---GTLIFVSHDR 495
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
2.74e-09 |
|
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: 57.55 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER----IGKL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpMHKRarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVldtvimghaelwevkqeRDRIYALAEMSEED-GYKVAELETQYGEMDGYSAEARAGELLLGvgipveq 148
Cdd:cd03218 81 PQEASIFRKLTV-----------------EENILAVLEIRGLSkKEREEKLEELLEEFHITHLRKSKASSLSG------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 149 hygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISH 210
Cdd:cd03218 137 ----------GERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-480 |
2.94e-09 |
|
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: 56.89 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 327 KGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPD---NGTVKWS--ENAQIGYYAQdHEYEF--END- 398
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNgiPYKEFAEKYP-GEIIYvsEEDv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 ----LTVFDWMS-QWKQEGDdeQAVRSIlgrllfsqddikkpakvlSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDmeS 473
Cdd:cd03233 94 hfptLTVRETLDfALRCKGN--EFVRGI------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD--S 151
|
....*..
gi 695729787 474 IESLNMA 480
Cdd:cd03233 152 STALEIL 158
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-233 |
3.10e-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: 57.06 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnERIGKLRQDQFA-------------FEEFTVLDTVIMG--HAELWEV 95
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-RDITGLPPHERAragigyvpegrriFPELTVEENLLLGayARRRAKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 96 KQERDRIYA----LAEMSeedgykvaeletqygemdgysaEARAGELLLGvgipvEQHygpMsevapgwklrVLLAQALF 171
Cdd:cd03224 109 KARLERVYElfprLKERR----------------------KQLAGTLSGG-----EQQ---M----------LAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 172 SNPDILLLDEPTNNL------DI-DTIRwleqTLNDRDSTMIIISHDRHFlnmvCTHMADldygelRVY 233
Cdd:cd03224 149 SRPKLLLLDEPSEGLapkiveEIfEAIR----ELRDEGVTILLVEQNARF----ALEIAD------RAY 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-515 |
3.26e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 334 LFkNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA----------QIGYYAQD-----HEYEFEND 398
Cdd:PRK11124 18 LF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkAIRELRRNvgmvfQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 LTVFDWMSQ--WKQEG-DDEQAV---RSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:PRK11124 97 LTVQQNLIEapCRVLGlSKDQALaraEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 695729787 473 -SIESLNMALEMYQG--TLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:PRK11124 176 iTAQIVSIIRELAETgiTQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
320-465 |
3.57e-09 |
|
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: 57.28 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS----------ENAQ--IGYY 387
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmhERARlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQdhEYEFENDLTVFD-WMSQWK-QEGDDEQAVRSILGRLL--FSQDDIKK-PAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:TIGR04406 82 PQ--EASIFRKLTVEEnIMAVLEiRKDLDRAEREERLEALLeeFQISHLRDnKAMSLSGGERRRVEIARALATNPKFILL 159
|
...
gi 695729787 463 DEP 465
Cdd:TIGR04406 160 DEP 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
326-506 |
3.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.92 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 326 TKGFDegplfkNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK---WSENAQ------------IGYYAQD 390
Cdd:PRK13641 20 KKGLD------NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPEtgnknlkklrkkVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 391 HEYE-FENdlTVF-DWMSQWKQEGDDEQAVRSI----LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDE 464
Cdd:PRK13641 94 PEAQlFEN--TVLkDVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 465 PTNHLDMESIESLNMALEMYQG---TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVL 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-211 |
4.12e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL-----------DPNERIGKLRQD---QFAFEe 78
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvwDVRRQVGMVFQNpdnQFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 79 fTVLDTVIMGhaeLWEVKQERDriyalaEMSEedgykvaeletqygemdgysaeaRAGELLLGVGIPVEQHYGPmSEVAP 158
Cdd:PRK13635 98 -TVQDDVAFG---LENIGVPRE------EMVE-----------------------RVDQALRQVGMEDFLNREP-HRLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMIIISHD 211
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKG---ITVLSITHD 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-515 |
4.23e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.40 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAqDHEYEFEND 398
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 399 -----LTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDI----KKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHL 469
Cdd:PRK11248 80 gllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLegaeKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 470 DMESIESLN-MALEMYQGT---LIFVSHDREFVSSLATRVIEITPE--RVVD 515
Cdd:PRK11248 160 DAFTREQMQtLLLKLWQETgkqVLLITHDIEEAVFMATELVLLSPGpgRVVE 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
320-493 |
4.41e-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: 56.65 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGF--DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE-----------NAQIGY 386
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQDHEY---EFENDLTVFDwmsqwkqEGDDEQavrsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:cd03369 87 IPQDPTLfsgTIRSNLDPFD-------EYSDEE---------IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 464 EPTNHLDMESIESLNMAL--EMYQGTLIFVSH 493
Cdd:cd03369 151 EATASIDYATDALIQKTIreEFTNSTILTIAH 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-231 |
5.05e-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: 59.26 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE---RIGKLRQDQFAFEEFTVLDTVIMGh 89
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTG- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 90 aelwevkqeRDRIYALAEMSeedGYKVAELEtqygEMDGYSAEAragellLGVGIPVEQHYGPMSEvapGWKLRVLLAQA 169
Cdd:TIGR01257 2030 ---------REHLYLYARLR---GVPAEEIE----KVANWSIQS------LGLSLYADRLAGTYSG---GNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 170 LFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiirEGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-514 |
5.44e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNERIGKLRQdqfaf 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 eeftVLDTVIMGHAELWEVKQERDRIYALAEMSEED-----GYKVAELETQYGEMDGYSAEARAGELLLGVGIPVEQ--- 148
Cdd:PRK10261 87 ----VIELSEQSAAQMRHVRGADMAMIFQEPMTSLNpvftvGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 149 ----HygpmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQtlnDRDSTMIIISHDRHFLNM 217
Cdd:PRK10261 163 srypH-----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQK---EMSMGVIFITHDMGVVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 218 VCTHMADLDYGElRVYPGNYDEYMTAATQARER-LLAdnAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEE 296
Cdd:PRK10261 235 IADRVLVMYQGE-AVETGSVEQIFHAPQHPYTRaLLA--AVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 297 VKASSRqNPFIRFEQDKKLF-RNALEVEALTK-GFDEGPlfknfnlllevGEKIAILGANGVGKSTMLKTLVGELQPDNG 374
Cdd:PRK10261 312 PILQVR-NLVTRFPLRSGLLnRVTREVHAVEKvSFDLWP-----------GETLSLVGESGSGKSTTGRALLRLVESQGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 375 TVKWseNAQ----------------IGYYAQDHEYEFENDLTV-FDWMSQWKQEG--DDEQAVRSI---LGRLLFSQDDI 432
Cdd:PRK10261 380 EIIF--NGQridtlspgklqalrrdIQFIFQDPYASLDPRQTVgDSIMEPLRVHGllPGKAAAARVawlLERVGLLPEHA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 433 KKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMeSIES--LNMALEMYQG---TLIFVSHDREFVSSLATRV-- 505
Cdd:PRK10261 458 WRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDLQRDfgiAYLFISHDMAVVERISHRVav 536
|
570
....*....|....*
gi 695729787 506 ------IEITPERVV 514
Cdd:PRK10261 537 mylgqiVEIGPRRAV 551
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
338-505 |
6.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 338 FNLLLEV--GEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE---------------NAQIGYYAQDHEYEFENDLT 400
Cdd:PRK13643 23 FDIDLEVkkGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQFPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 VFDWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES-IE 475
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArIE 182
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 476 SLNMALEMYQG--TLIFVSHDREFVSSLATRV 505
Cdd:PRK13643 183 MMQLFESIHQSgqTVVLVTHLMDDVADYADYV 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
320-514 |
6.82e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.58 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGP----LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------ENAQIGYYA 388
Cdd:PRK10535 5 LELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgqdvatlDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 389 QDH------EYEFENDLT---------VFDWMSQWKQEgddeQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLM 453
Cdd:PRK10535 85 REHfgfifqRYHLLSHLTaaqnvevpaVYAGLERKQRL----LRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 454 MEKPNILVMDEPTNHLDMESIESLNMALEMY--QG-TLIFVSHDREfVSSLATRVIEITPERVV 514
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLrdRGhTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-389 |
7.16e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.94 E-value: 7.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWseNAQIGYYAQ 389
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQ 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-504 |
7.71e-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: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaqigyyaqdheyeFENDLTVFDWMSqwkqegddeqavrsilgR 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------IYIDGEDILEEV-----------------L 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 425 LLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQG---------TLIFVSHDR 495
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTTNDE 126
|
....*....
gi 695729787 496 EFVSSLATR 504
Cdd:smart00382 127 KDLGPALLR 135
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
7.73e-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: 56.11 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVS--------LDPNER-IGKLRQDQFAF 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 EEFTVLDTVIMGhaeLWEVKQERDRIyalaemsEEDGYKVAELetqygemdgysaeARAGELLlgvgipveQHYgPmSEV 156
Cdd:cd03301 85 PHMTVYDNIAFG---LKLRKVPKDEI-------DERVREVAEL-------------LQIEHLL--------DRK-P-KQL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHD 211
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklrvqmrAELKRLQQRLG---TTTIYVTHD 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-508 |
7.92e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTL-------VGELQPDNGTVKwsenaqiGYYAQDHE 392
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-------DPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 393 YEFENDLtVFDWMSQWKQ------------------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMM 454
Cdd:PRK09493 75 IRQEAGM-VFQQFYLFPHltalenvmfgplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 455 EKPNILVMDEPTNHLD----------MESIESLNMalemyqgTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK09493 153 VKPKLMLFDEPTSALDpelrhevlkvMQDLAEEGM-------TMVIVTHEIGFAEKVASRLIFI 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-513 |
8.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaqigyYAQDHEYEFENDLtvfdWMSQWKQ----E 411
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----------YVDGLDTSDEENL----WDIRNKAgmvfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 412 GDDEQAVRSILGR--------LLFSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:PRK13633 93 NPDNQIVATIVEEdvafgpenLGIPPEEIRErvdeslkkvgmyeyrrhAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 467 NHLD-------MESIESLNmalEMYQGTLIFVSH--------DREFVSSLATRVIEITPERV 513
Cdd:PRK13633 173 AMLDpsgrrevVNTIKELN---KKYGITIILITHymeeaveaDRIIVMDSGKVVMEGTPKEI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-514 |
9.98e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYEFEN- 397
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL----------DGEPVRFRSp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 -------------DLTVFDWMS-----------------QWKQEgddEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRM 447
Cdd:COG1129 74 rdaqaagiaiihqELNLVPNLSvaeniflgreprrggliDWRAM---RRRARELLARLGLD-IDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 448 LFGKLMMEKPNILVMDEPTNHLDMESIESLnmaLEM-----YQG-TLIFVSH---------DR-------EFVSSLATRv 505
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERL---FRIirrlkAQGvAIIYISHrldevfeiaDRvtvlrdgRLVGTGPVA- 225
|
....*....
gi 695729787 506 iEITPERVV 514
Cdd:COG1129 226 -ELTEDELV 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-465 |
1.07e-08 |
|
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: 55.63 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KW--SENAQ--IGYY 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLpmHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEYeFEnDLTVFD-WMSQWKQEGDDEQAVRSILGRLL--FSQDDI-KKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:cd03218 81 PQEASI-FR-KLTVEEnILAVLEIRGLSKKEREEKLEELLeeFHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 695729787 464 EP 465
Cdd:cd03218 159 EP 160
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-198 |
1.17e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRqDQFAfeeft 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRRQR-DEYH----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 vLDTVIMGHA-----EL--WevkqERDRIY-ALAEMSEEDgykvaeletqygemDGYSAEARAGelLLGV-GIPVEQhyg 151
Cdd:PRK13538 74 -QDLLYLGHQpgiktELtaL----ENLRFYqRLHGPGDDE--------------ALWEALAQVG--LAGFeDVPVRQ--- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695729787 152 pMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTL 198
Cdd:PRK13538 130 -LSA---GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-506 |
1.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE---------------NAQIGYYAQDHEYEFENDLT 400
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 VFDWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES--- 473
Cdd:PRK13646 104 EREIIFGPKNFKMNLDEVKNYAHRLLmdlgFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrq 183
|
170 180 190
....*....|....*....|....*....|....
gi 695729787 474 IESLNMALEMYQG-TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13646 184 VMRLLKSLQTDENkTIILVSHDMNEVARYADEVI 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
330-514 |
1.60e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.76 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQI-GYYAQDHEYEF-- 395
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLvGIVFQNPETQFvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 ---ENDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPaKVLSGGE-KGRMLFGKLMMEkPNILVMDEPTNHLDM 471
Cdd:PRK13644 93 rtvEEDLA-FGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQgQCVALAGILTME-PECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 472 ESIES-LNMALEMYQ--GTLIFVSH--------DREFVSSLATRVIEITPERVV 514
Cdd:PRK13644 170 DSGIAvLERIKKLHEkgKTIVYITHnleelhdaDRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
1.82e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKIL------------GGDLepTLGNVS-------LDP 62
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDV--LLGGRSifnyrdvLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 63 NERIGKLRQDQFAFEeFTVLDTVIMGHaelwevkqerdRIYALAEMSEEDGYkvaeletqygemdgysAEARAGELLLGV 142
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGV-----------RAHKLVPRKEFRGV----------------AQARLTEVGLWD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 143 GIPVEQHYGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRdSTMIIISHD 211
Cdd:PRK14271 152 AVKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEfirSLADR-LTVIIVTHN 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
310-470 |
2.82e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.59 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 310 EQDKKLFRNALEVEALTKGfdegpLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG------ELQPD---NGT-VKWS 379
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKH-----LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspkgvKGSGSvllNGMpIDAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 380 ENAQIGYYAQDHEYeFENDLTVFD---WMSQWK---QEGDDE--QAVRSILGRL-LFSQDD--IKKPA--KVLSGGEKGR 446
Cdd:TIGR00955 96 EMRAISAYVQQDDL-FIPTLTVREhlmFQAHLRmprRVTKKEkrERVDEVLQALgLRKCANtrIGVPGrvKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 695729787 447 MLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
320-505 |
2.95e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA----------QIGYYAQ 389
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarltpakahQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 390 DHEYEFENDLTVfdwmsqwkQEG---------DDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNIL 460
Cdd:PRK15439 92 PQEPLLFPNLSV--------KENilfglpkrqASMQKMKQLL-AALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695729787 461 VMDEPTNHLDMESIESLNMALEMYQGT---LIFVSHDREFVSSLATRV 505
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADRI 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
330-506 |
2.95e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.00 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------SEN-----AQIGYYAQDHEYEF--- 395
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitisKENlkeirKKIGIIFQNPDNQFiga 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 ----------ENDLTVFDWMSQWKQEGDDEQAVRSILgrllfsqddiKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:PRK13632 100 tveddiafglENKKVPPKKMKDIIDDLAKKVGMEDYL----------DKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 466 TNHLD----MESIESLNMALEMYQGTLIFVSHDREFVsSLATRVI 506
Cdd:PRK13632 170 TSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-494 |
3.11e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNL-LLEVGEKIAILGANGVGKSTMLKTLVGELQPD----NGTVKWSEnaQIGYYA----QDHEYEF-ENDLTVfdw 404
Cdd:PRK13409 88 FKLYGLpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyEEEPSWDE--VLKRFRgtelQNYFKKLyNGEIKV--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 405 mSQWKQ-----------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:PRK13409 163 -VHKPQyvdlipkvfkgkvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|.
gi 695729787 468 HLDMEsiESLNMAL---EMYQG-TLIFVSHD 494
Cdd:PRK13409 242 YLDIR--QRLNVARlirELAEGkYVLVVEHD 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-470 |
3.28e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 329 FDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-------------QIGYYAQDHEYE- 394
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVATVFQDPEQQi 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 395 FENDL---TVFDWMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:PRK13638 91 FYTDIdsdIAFSLRNLGVPEAEITRRVDEAL-TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-183 |
3.43e-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: 54.22 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFA-------------FEEFTVLDTVIMG---HAELWE 94
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRIArlgigyvpegrriFPSLTVEENLLLGayaRRDRAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 95 VKQERDRIYA----LAEMseedgykvaeletqygemdgysAEARAGELLLGvgipvEQHygpMseVApgwklrvlLAQAL 170
Cdd:COG0410 112 VRADLERVYElfprLKER----------------------RRQRAGTLSGG-----EQQ---M--LA--------IGRAL 151
|
170
....*....|...
gi 695729787 171 FSNPDILLLDEPT 183
Cdd:COG0410 152 MSRPKLLLLDEPS 164
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-241 |
3.45e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.81 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnerigklrqdqfafeeftvLDTVIMGHAELWEVKq 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 98 eRDRIYALAEMSEEDGYKVAELETQYG-EMDGYSAEAR---AGELLLGVGIPVEQHYGPmSEVAPGWKLRVLLAQALFSN 173
Cdd:PRK10070 105 -RKKIAMVFQSFALMPHMTVLDNTAFGmELAGINAEERrekALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 174 PDILLLDEPTNNLDIDTIRWLEQTL----NDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYM 241
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV-VQVGTPDEIL 253
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
3.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.71 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF------GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPnerigklrqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 75 afeeftvLDTVIMGHaeLWEVKQERDRIYA------LAEMSEEDgykVAeletqYG-EMDGYSAE---ARAGELLLGVGI 144
Cdd:PRK13633 72 -------LDTSDEEN--LWDIRNKAGMVFQnpdnqiVATIVEED---VA-----FGpENLGIPPEeirERVDESLKKVGM 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 145 PVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDS-TMIIISH 210
Cdd:PRK13633 135 YEYRRHAP-HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIK----ELNKKYGiTIILITH 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-493 |
4.54e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAqigYYAQDHEYEFEN-- 397
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLAAQLgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 -----DLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKV-----------------LSGGEKGRMLFGKLMME 455
Cdd:PRK09700 83 giiyqELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMmllrvglkvdldekvanLSISHKQMLEIAKTLML 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 456 KPNILVMDEPTNHLDMESIESLNMALEMYQG---TLIFVSH 493
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-506 |
4.72e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 54.73 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-------SENAQIGY----- 386
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYlpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 --YAqdheyefenDLTVFD---WMSQWK--QEGDDEQAVRSILGRLlfsqdDI----KKPAKVLSGGEKGRMLFGKLMME 455
Cdd:COG4152 81 glYP---------KMKVGEqlvYLARLKglSKAEAKRRADEWLERL-----GLgdraNKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 456 KPNILVMDEPTNHLDMESIESLNMAL--EMYQG-TLIFVSHDREFVSSLATRVI 506
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIreLAAKGtTVIFSSHQMELVEELCDRIV 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-230 |
4.90e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV--------SLDPNERIGKLRQDQFAFEEF------TVLDT 84
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKELRKARRQIGMIFQHFnllssrTVFDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 85 VimghaelwevkqerdriyALAemseedgykvaeLEtqygeMDGYSA---EARAGELLLGVGIPVEQHYGPmSEVAPGWK 161
Cdd:PRK11153 103 V------------------ALP------------LE-----LAGTPKaeiKARVTELLELVGLSDKADRYP-AQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RD--STMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinRElgLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
5.40e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.24 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLdpNERIGKLRQDQFAFEEfTVLDTVIMG---- 88
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQEPWIQNG-TIRENILFGkpfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 89 HAELWEVKQ----ERDriyaLAEMSEEDgykvaelETQYGEMdgysaearaGELLLGvgipveqhygpmsevapGWKLRV 164
Cdd:cd03250 94 EERYEKVIKacalEPD----LEILPDGD-------LTEIGEK---------GINLSG-----------------GQKQRI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWL-EQTLND---RDSTMIIISHDRHFL 215
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGlllNNKTRILVTHQLQLL 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-473 |
5.86e-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: 53.70 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSENaQIGYYAQdheyefENDL- 399
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlRWLRS-QIGLVSQ------EPVLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 400 --TVFDWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:cd03249 90 dgTIAENIRYGKPDATDEEVEEAA--KKANIHDFIMSlPdgydtlvgerGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
....*..
gi 695729787 467 NHLDMES 473
Cdd:cd03249 168 SALDAES 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
6.17e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.84 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE----------RIGKLR 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 --QDQFAFEEFTVLDTVImghaelweVKQERD-RIYALAEMSEEDGYKVAELEtqygemdgysAEARAGELLLGVGIpVE 147
Cdd:PRK11300 85 tfQHVRLFREMTVIENLL--------VAQHQQlKTGLFSGLLKTPAFRRAESE----------ALDRAATWLERVGL-LE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 148 QHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEP--------TNNLD--IDTIRwleqtlNDRDSTMIIISHD 211
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELDelIAELR------NEHNVTVLLIEHD 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-224 |
6.44e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 13 SKPLF--ENISVKFGGGNRY-----------------GLIGANGSGKS-TFMKILG----GDLEPTlGNVSLD------- 61
Cdd:COG4172 3 SMPLLsvEDLSVAFGQGGGTveavkgvsfdiaagetlALVGESGSGKSvTALSILRllpdPAAHPS-GSILFDgqdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 62 PNERIGKLRQDQFA--FEE--------FTVldtvimghaelwevkqerdriyalaemseedGYKVAE-LETQYGeMDGYS 130
Cdd:COG4172 82 SERELRRIRGNRIAmiFQEpmtslnplHTI-------------------------------GKQIAEvLRLHRG-LSGAA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 131 AEARAGELLLGVGIP-VEQHYG--PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIdTIRwlEQTLN-------D 200
Cdd:COG4172 130 ARARALELLERVGIPdPERRLDayP-HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQ--AQILDllkdlqrE 205
|
250 260
....*....|....*....|....
gi 695729787 201 RDSTMIIISHDrhfLNMVcTHMAD 224
Cdd:COG4172 206 LGMALLLITHD---LGVV-RRFAD 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-502 |
8.60e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTL--VGELQpdnGTVKwsENAQIGYYAQDhEYEFE 396
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVR--VEGRVEFFNQN-IYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 NDL-------------------TVFD----------WMSQWKQEGDDEQAVRSilGRLLfsqDDIK----KPAKVLSGGE 443
Cdd:PRK14258 81 VNLnrlrrqvsmvhpkpnlfpmSVYDnvaygvkivgWRPKLEIDDIVESALKD--ADLW---DEIKhkihKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 444 KGRMLFGKLMMEKPNILVMDEPTNHLD------MES-IESLNMALEMyqgTLIFVSHDREFVSSLA 502
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESlIQSLRLRSEL---TMVIVSHNLHQVSRLS 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-505 |
1.04e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 330 DEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKwsENAQIGYYAQD--------------HEYEF 395
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKDifqidaiklrkevgMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 EN---DLTVFDWMS-QWKQEG-DDEQAVRSILGRLLFS-------QDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMD 463
Cdd:PRK14246 99 PNpfpHLSIYDNIAyPLKSHGiKEKREIKKIVEECLRKvglwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 464 EPTNHLDM---ESIESLNMALEMyQGTLIFVSHDREFVSSLATRV 505
Cdd:PRK14246 179 EPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-211 |
1.18e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP--------NER----IGKL 69
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVLDTvIMGHAELWEVKQERDRIYALAEMSEEdgYKVAELETQYGEmdgysaearagelllgvgipveqh 149
Cdd:PRK10895 84 PQEASIFRRLSVYDN-LMAVLQIRDDLSAEQREDRANELMEE--FHIEHLRDSMGQ------------------------ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 150 ygpmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDtIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK10895 137 -----SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvID-IKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
1.20e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQDqfafeEFTVLDTvi 86
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrSQRIRMIFQD-----PSTSLNP-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 87 mghaelwevkqeRDRIYALAEMSeedgykvAELETqygEMDGYSAEARAGELLLGVGI-PVEQHYGPMSeVAPGWKLRVL 165
Cdd:PRK15112 103 ------------RQRISQILDFP-------LRLNT---DLEPEQREKQIIETLRQVGLlPDHASYYPHM-LAPGQKQRLG 159
|
170 180
....*....|....*....|...
gi 695729787 166 LAQALFSNPDILLLDEPTNNLDI 188
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDM 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-210 |
1.22e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.41 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDP-----------NERIGKLRQDQfafeeftvld 83
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTIIPQDP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 TVIMGhaelwEVKQERDRiyaLAEMSEEDGYKVAELetqygemdgysaeARAGELLlgvgipveqhygpmsevAPGWKLR 163
Cdd:cd03369 92 TLFSG-----TIRSNLDP---FDEYSDEEIYGALRV-------------SEGGLNL-----------------SQGQRQL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAH 182
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-218 |
1.69e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVslDPNERIG----KLRQDQfafeEFTVLDtVIMGHAELWE---VKQERDRIY 103
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISykpqYIKPDY----DGTVED-LLRSITDDLGssyYKSEIIKPL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 104 ALAEMseedgykvaeLETQYGEMDGysaearaGELllgvgipveQhygpmsevapgwklRVLLAQALFSNPDILLLDEPT 183
Cdd:PRK13409 442 QLERL----------LDKNVKDLSG-------GEL---------Q--------------RVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 184 NNLDIdtirwlEQTLN----------DRDSTMIIISHDRHFLNMV 218
Cdd:PRK13409 482 AHLDV------EQRLAvakairriaeEREATALVVDHDIYMIDYI 520
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
320-508 |
1.69e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV----KWSENAQ----IGYYAqdH 391
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDrsrfMAYLG--H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 392 EYEFENDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKpakvLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:PRK13543 90 LPGLKADLSTLENLHflcglHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 467 NHLDMESIESLNMALEMY---QGTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-493 |
1.73e-07 |
|
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: 52.09 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYyaqDHEYEFE------NDLTVFD--- 403
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYLHSkvslvgQEPVLFArsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 404 ------WMSQWKQEGDDEQAVRS-----ILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:cd03248 105 qdniayGLQSCSFECVKEAAQKAhahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|....*
gi 695729787 473 SIESLNMALemYQG----TLIFVSH 493
Cdd:cd03248 185 SEQQVQQAL--YDWperrTVLVIAH 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
1.80e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.88 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPtlgnvSLDPNERIgklrqdqfafeeftVLDTVIMGHAELW 93
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-----DDNPNSKI--------------TVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 94 EVK-------QERDRIYALAEMSEEDGYKVAELETQYGEMDGYSAEAragelLLGVGIPVEQHYGPmSEVAPGWKLRVLL 166
Cdd:PRK13640 81 DIRekvgivfQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDV-----LADVGMLDYIDSEP-ANLSGGQKQRVAI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 167 AQALFSNPDILLLDEPTNNLD-------IDTIRWLEqtlNDRDSTMIIISHD 211
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDpagkeqiLKLIRKLK---KKNNLTVISITHD 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-506 |
1.87e-07 |
|
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: 53.18 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 349 AILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQ----------IGYYAQD-----HeyefendLTVFD----- 403
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARgiflpphrrrIGYVFQEarlfpH-------LSVRGnllyg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 404 -WMSQWKQEGDDEQAVRSILG--RLLfsqdDiKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES------- 473
Cdd:COG4148 102 rKRAPRAERRISFDEVVELLGigHLL----D-RRPAT-LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeilpy 175
|
170 180 190
....*....|....*....|....*....|...
gi 695729787 474 IESLNMALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG4148 176 LERLRDELDI---PILYVSHSLDEVARLADHVV 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-198 |
1.91e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 51.72 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNerigklrqdqfafeeftv 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 ldtvimghaelwEVKQERDRIY-ALAEMSEEDGYKV---AELETQYGEMDGysAEARAGELLLGVGIPVEQHYgPMSEVA 157
Cdd:cd03231 63 ------------PLDFQRDSIArGLLYLGHAPGIKTtlsVLENLRFWHADH--SDEQVEEALARVGLNGFEDR-PVAQLS 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTL 198
Cdd:cd03231 128 AGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
2.36e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.99 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsLDPNERIGKLRQD-QFAFEEF- 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDtRLMFQDAr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 -----TVLDTVIMGHAELWEVKQERdriyALAEMSEEDgykvaeletqygemdgysaeaRAGELllgvgipveqhygPmS 154
Cdd:PRK11247 92 llpwkKVIDNVGLGLKGQWRDAALQ----ALAAVGLAD---------------------RANEW-------------P-A 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----------IDTIrWLEQTLndrdsTMIIISHD 211
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdlIESL-WQQHGF-----TVLLVTHD 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
320-530 |
2.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.40 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFN---LLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK-----------WSENAQIG 385
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQDHEYEFENDLTVFDWMSQWKQEG-DDEQAVRSILGRLL-FSQDDIK--KPAKvLSGGEKGRMLFGKLMMEKPNILV 461
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDVAFGMENQGiPREEMIKRVDEALLaVNMLDFKtrEPAR-LSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 462 MDEPTNHLD----MESIESLNMALEMYQGTLIFVSHDREFVSS----LATRVIEITPERV-----------------VDF 516
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAASsdriLVMKAGEIIKEAApselfatsedmveigldVPF 243
|
250
....*....|....
gi 695729787 517 TGNYEDYLRSKGID 530
Cdd:PRK13642 244 SSNLMKDLRKNGFD 257
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-217 |
2.68e-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: 2.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRW-----LEQTLNDRDSTMIIISHDRHFLNM 217
Cdd:cd03240 128 IRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA 188
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
3.03e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.38 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGklrq 71
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtdlpPKDRnIA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 dqFAFEEF------TVLDTV-----IMGHAelwevKQERD-RIYALAEMseedgykvaeLEtqygeMDGYsAEARAGELl 139
Cdd:COG3839 79 --MVFQSYalyphmTVYENIafplkLRKVP-----KAEIDrRVREAAEL----------LG-----LEDL-LDRKPKQL- 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 140 lgvgipveqhygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG3839 135 -----------------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-376 |
3.26e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 3.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV 376
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-514 |
3.43e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTL--VGELQPD---NGTVK------WSENA--- 382
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEarvEGEVRlfgrniYSPDVdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 383 ----QIGYYAQ-----DHEYEFENDLTVFDWMSQWKQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKGRMLFG 450
Cdd:PRK14267 82 evrrEVGMVFQypnpfPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 451 KLMMEKPNILVMDEPTNHLD---MESIESLNMALEMyQGTLIFVSHDREFVSSLATRV--------IEITPERVV 514
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVaflylgklIEVGPTRKV 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-269 |
3.55e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPL----FENISVKFGGGNRYGLIGANGSGKS-TFMKILGGDLEPtlgnvsldpneriGKLRQDQFA 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------------GRVMAEKLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 76 FEEFTVLDTvimghaelwEVKQERDRIYALAEMSEED-----------GYKVAE-LETQYGemdGYSAE--ARAGELLLG 141
Cdd:PRK11022 70 FNGQDLQRI---------SEKERRNLVGAEVAMIFQDpmtslnpcytvGFQIMEaIKVHQG---GNKKTrrQRAIDLLNQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 142 VGIPveqhyGPMS--EVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMII 207
Cdd:PRK11022 138 VGIP-----DPASrlDVYPhqlsgGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQKEN---MALVL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 208 ISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYMTAA----TQARERLLADNAKKKAQIADLQSFV 269
Cdd:PRK11022 210 ITHDLALVAEAAHKIIVMYAGQV-VETGKAHDIFRAPrhpyTQALLRALPEFAQDKARLASLPGVV 274
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-216 |
3.76e-07 |
|
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: 51.49 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGD--LEPTLGNVSLD--------PNERIgklRQ 71
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKgqdllelePDERA---RA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQF-AF---EEFTVLDTVIMGHAELWEVKQERDRiyalAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGvgipve 147
Cdd:TIGR01978 78 GLFlAFqypEEIPGVSNLEFLRSALNARRSARGE----EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSG------ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 148 qhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLN 216
Cdd:TIGR01978 148 -----------GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINrlrEPDRSFLIITHYQRLLN 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-505 |
3.97e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 319 ALEVEALTKGFdeGPLF--KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYEFE 396
Cdd:COG3845 5 ALELRGITKRF--GGVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI----------DGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 397 N--------------------DLTVFD-----------WMSQWKQEgddEQAVRSILGRLLFSQDdikkP-AKV--LSGG 442
Cdd:COG3845 73 SprdaialgigmvhqhfmlvpNLTVAEnivlgleptkgGRLDRKAA---RARIRELSERYGLDVD----PdAKVedLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 443 EKGR--MLfgKLMMEKPNILVMDEPTNHLDMESIESL-----NMALEmyQGTLIFVSHD-REfVSSLATRV 505
Cdd:COG3845 146 EQQRveIL--KALYRGARILILDEPTAVLTPQEADELfeilrRLAAE--GKSIIFITHKlRE-VMAIADRV 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-210 |
4.07e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE------------RIGKLRQDQFAFEEfTVLD 83
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrsKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 TVimgHAELWEVKQerdrIYALAEMSEEDGYKVAE--------LETQYGEMDGYSAEARAGELL--------------LG 141
Cdd:PTZ00265 479 NI---KYSLYSLKD----LEALSNYYNEDGNDSQEnknkrnscRAKCAGDLNDMSNTTDSNELIemrknyqtikdsevVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 142 VGIPVEQH---------YGPM-----SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN----DRDS 203
Cdd:PTZ00265 552 VSKKVLIHdfvsalpdkYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR 631
|
....*..
gi 695729787 204 TMIIISH 210
Cdd:PTZ00265 632 ITIIIAH 638
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-210 |
4.57e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 50.24 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPT-------LGNVSLDPNE---RIGKLRQDQFAFEEFTV 81
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvsgevlINGRPLDKRSfrkIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 LDTvimghaeLWevkqerdriyalaemseedgykvaeletqygemdgYSAEARagelllgvGIPVEQhygpmsevapgwK 161
Cdd:cd03213 100 RET-------LM-----------------------------------FAAKLR--------GLSGGE------------R 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTlndrDSTMIIISH 210
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
4.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.62 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNErigkLRQDQfafeeftvldtvimghAELWEVKQE 98
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP----IKYDK----------------KSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 99 --------RDRIYAlaEMSEEDgykVAeletqYGEMD-GYS---AEARAGELLLGVGIPVEQHYGPmSEVAPGWKLRVLL 166
Cdd:PRK13639 80 vgivfqnpDDQLFA--PTVEED---VA-----FGPLNlGLSkeeVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695729787 167 AQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-493 |
4.76e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLvgelqpdNGTVKWSENAQI-GYYAQDHEYEF 395
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-------NRLIELYPEARVsGEVYLDGQDIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 ENDLT--------VFDW------MSQW-------------KQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKG 445
Cdd:PRK14247 74 KMDVIelrrrvqmVFQIpnpipnLSIFenvalglklnrlvKSKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695729787 446 RMLFGKLMMEKPNILVMDEPTNHLDMES---IESLNMAL--EMyqgTLIFVSH 493
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELkkDM---TIVLVTH 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
4.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.39 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 19 NISVKfgGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpneriGKlrqdqfafeeftVLDTVIMGHAELWE---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----GK------------PIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 95 VKQERDRIYALAEMSEEDGYKVAELETQYGEMdgysaEARAGELLLGVGIPVEQHyGPMSEVAPGWKLRVLLAQALFSNP 174
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 175 DILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNPKE 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
345-506 |
5.19e-07 |
|
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: 49.88 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYyaqdheyefendltvfdwmsqwkqegddeqavrsilgr 424
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY-------------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 425 llfsqddikKPAKV-LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMEsiESLNMA------LEMYQGTLIFVSHDREF 497
Cdd:cd03222 66 ---------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE--QRLNAArairrlSEEGKKTALVVEHDLAV 134
|
....*....
gi 695729787 498 VSSLATRVI 506
Cdd:cd03222 135 LDYLSDRIH 143
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-233 |
5.25e-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: 51.21 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNerigklrqdqfafeeftvLDTVImghaelwevkqerdRIYALAEMSE 110
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD------------------WDEIL--------------DEFRGSELQN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 111 ------EDGYKVAeLETQYGEMDGYSAEARAGELL---------------LGVGIPVEQHygpMSEVAPGWKLRVLLAQA 169
Cdd:cd03236 78 yftkllEGDVKVI-VKPQYVDLIPKAVKGKVGELLkkkdergkldelvdqLELRHVLDRN---IDQLSGGELQRVAIAAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 170 LFSNPDILLLDEPTNNLDID---TIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLdYGELRVY 233
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAY 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
335-480 |
5.89e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNL-LLEVGEKIAILGANGVGKSTMLKTLVGELQPD----NGTVKWSEnaQIGYYA----QDHEYE-FENDLTVfdw 404
Cdd:COG1245 88 FRLYGLpVPKKGKVTGILGPNGIGKSTALKILSGELKPNlgdyDEEPSWDE--VLKRFRgtelQDYFKKlANGEIKV--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 405 mSQWKQ-----------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTN 467
Cdd:COG1245 163 -AHKPQyvdlipkvfkgtvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170
....*....|...
gi 695729787 468 HLDMEsiESLNMA 480
Cdd:COG1245 242 YLDIY--QRLNVA 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-196 |
6.31e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN------------ERIGK 68
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQDQFAFEEFTVLDTVIMG--HAELWEVKQERDRIYALAEmseedgyKVAELETQygemdgysaeaRAGELLLGvgipv 146
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELFP-------RLHERRIQ-----------RAGTMSGG----- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 147 EQHYgpmsevapgwklrVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQ 196
Cdd:PRK11614 142 EQQM-------------LAIGRALMSQPRLLLLDEPSLGLApiiiqqiFDTIEQLRE 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
331-514 |
6.42e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 331 EGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENAQI-------GYYAQDHEYE- 394
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitsTSKNKDIkqirkkvGLVFQFPESQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 FENdlTVFDWMSQWKQ-----EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRM-LFGKLMMEkPNILVMDEPTNH 468
Cdd:PRK13649 99 FEE--TVLKDVAFGPQnfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVaIAGILAME-PKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695729787 469 LDMESIESLnMAL--EMYQG--TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13649 176 LDPKGRKEL-MTLfkKLHQSgmTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-230 |
8.45e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSL--------DPNERIGKLRQD-----QFA----FEEfT 80
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpeTGNKNLKKLRKKvslvfQFPeaqlFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGHAELWEVKQErdriyalaemseedgykvaeletqygemdgysAEARAGELLLGVGIPVEQHYGPMSEVAPGW 160
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDE--------------------------------AKEKALKWLKKVGLSEDLISKSPFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS---TMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-218 |
1.28e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 49.68 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNVSLD--------PNER----IG 67
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDgedilelsPDERaragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 68 klrqdqFAF---EEF---TVLDTVimghaelwevkqerdRIyALAEMSEEdgykvaeletqygEMDGYSAEARAGELLLG 141
Cdd:COG0396 81 ------LAFqypVEIpgvSVSNFL---------------RT-ALNARRGE-------------ELSAREFLKLLKEKMKE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 142 VGIPVEqhygpM--SEVAPGW----KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDR 212
Cdd:COG0396 126 LGLDED-----FldRYVNEGFsggeKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNklrSPDRGILIITHYQ 200
|
....*.
gi 695729787 213 HFLNMV 218
Cdd:COG0396 201 RILDYI 206
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
350-493 |
1.53e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 350 ILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQ------DHEYEFENDLTVFDWMSQWKQEGDDEQAVRSILG 423
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNI-YYKNCNINNIAKpyctyiGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIH 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 424 RLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMYQ---GTLIFVSH 493
Cdd:PRK13541 110 YFKL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKAnsgGIVLLSSH 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
337-466 |
1.70e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 337 NFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE----------------FENDLT 400
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmtVEENLA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 401 VFDWMSQWKQEGDDEQAVRSILGRLlfsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPT 466
Cdd:PRK11614 103 MGGFFAERDQFQERIKWVYELFPRL---HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
1.80e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.58 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdleptL-----GNVSLDPNERI-----------GKLRQ------ 71
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-----LwpygsGRIARPAGARVlflpqrpylplGTLREallypa 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 --DQFAFEEF-TVLDTVIMGHaelwevkqerdriyaLAEMSEEdgykvaeletqygemdgysaEARAGELL-LGvgipvE 147
Cdd:COG4178 451 taEAFSDAELrEALEAVGLGH---------------LAERLDE--------------------EADWDQVLsLG-----E 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 148 QHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDR--DSTMIIISHdRHFLNMVCTHMADL 225
Cdd:COG4178 491 QQ-------------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLEL 556
|
.
gi 695729787 226 D 226
Cdd:COG4178 557 T 557
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-242 |
1.93e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFL-NMVCTHMadLDYGELRVYpGNYDE 239
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLeQFDRICV--MDNGQIIEQ-GTHQE 559
|
...
gi 695729787 240 YMT 242
Cdd:PRK11160 560 LLA 562
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.96e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.42 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsLDPNERIGKlrqdqfafeef 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 tvldtvimghAELWEVKQ--------ERDRIYalAEMSEEDgykVAELETQYGeMDGYSAEARAGELLLGVGIPVEQHYG 151
Cdd:PRK13652 71 ----------ENIREVRKfvglvfqnPDDQIF--SPTVEQD---IAFGPINLG-LDEETVAHRVSSALHMLGLEELRDRV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 152 PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDST--MIIIsHDRHFLNMVcTHMADLDY 227
Cdd:PRK13652 135 P-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVI-FSTHQLDLV-PEMADYIY 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-493 |
1.99e-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: 50.52 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 334 LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLvGELQPD-NGTVKWSENAQIGYYAQdHEY----EFENDLTVFDWMSQW 408
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQ-RPYmtlgTLRDQIIYPDSSEDM 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 409 KQEGDDEQAVRSIL-----GRLL---FSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMA 480
Cdd:TIGR00954 545 KRRGLSDKDLEQILdnvqlTHILereGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170
....*....|...
gi 695729787 481 LEMYQGTLIFVSH 493
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-210 |
2.01e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 50.61 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLePTLGNV--------SLDPN---ERIGKLRQDQFAFEEfTVL 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielrELDPEswrKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 83 DTVIMGHAELWEvkQERDRIYALAEMSE-----EDGykvaeLETQYGEmdgysaeaRAGelllgvGIPVEQhygpmseva 157
Cdd:PRK11174 441 DNVLLGNPDASD--EQLQQALENAWVSEflpllPQG-----LDTPIGD--------QAA------GLSVGQ--------- 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 158 pgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK11174 491 ---AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTH 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
116-253 |
2.01e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 116 VAE-LETQYGEMDGYSAEARAGELLLGVGI-PVEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD------ 187
Cdd:PRK15134 385 IEEgLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaq 463
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 188 -IDTIRWLEQTlndRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYMTAATQARER-LLA 253
Cdd:PRK15134 464 iLALLKSLQQK---HQLAYLFISHDLHVVRALCHQVIVLRQGEV-VEQGDCERVFAAPQQEYTRqLLA 527
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-211 |
2.07e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQD---QFAFEef 79
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNpdnQFVGA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 80 TVLDTVIMGhaelwevkqerdriyalaemseedgykvaeLETQ---YGEMdgysaEARAGELLLGVGIPVEQHYGPmSEV 156
Cdd:PRK13650 98 TVEDDVAFG------------------------------LENKgipHEEM-----KERVNEALELVGMQDFKEREP-ARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
2.15e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLE-----PTLGNVSLDpNERIGKL------R 70
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLD-GQDIFKMdvielrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 71 QDQFAFE------EFTVLDTVIMGhAELWEVKQERDRIYALAEMSEEDGYKVAELETQYGemdgysaearagelllgvgi 144
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVALG-LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLD-------------------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 145 pveqhyGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK14247 142 ------APAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLElkKDMTIVLVTH 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
2.20e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 12 GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE-----------RIGKLRQDQ----FAF 76
Cdd:PRK13647 17 GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsKVGLVFQDPddqvFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 77 eefTVLDTVIMGHAELwevkqerdriyalaemseedgykvaeletqygEMDGYSAEARAGELLLGVGIPVEQHYGPMsEV 156
Cdd:PRK13647 96 ---TVWDDVAFGPVNM--------------------------------GLDKDEVERRVEEALKAVRMWDFRDKPPY-HL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13647 140 SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-187 |
2.30e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTL---GNVSLDpNERIGK---------LRQDQFAFEEFTV 81
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLN-GMPIDAkemraisayVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 LDTVI------MGHAELWEVKQERdriyalaemseedgykVAELETQYGEMDgysaearAGELLLGVGipveqhyGPMSE 155
Cdd:TIGR00955 117 REHLMfqahlrMPRRVTKKEKRER----------------VDEVLQALGLRK-------CANTRIGVP-------GRVKG 166
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
320-504 |
2.43e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTL--VGELQPD---NGTVKWSEN------------- 381
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 382 AQIGY-YAQDHEYEF---ENDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMME 455
Cdd:PRK14239 86 KEIGMvFQQPNPFPMsiyENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEvkDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 456 KPNILVMDEPTNHLDMES---IESLNMALEmYQGTLIFVSHDREFVSSLATR 504
Cdd:PRK14239 166 SPKIILLDEPTSALDPISagkIEETLLGLK-DDYTMLLVTRSMQQASRISDR 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
320-514 |
2.58e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGEL---QPDNG-------TVKWSENAQI----- 384
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGarvtgdvTLNGEPLAAIdaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 ----GYYAQDHEYEFE---NDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDD---IKKPAKVLSGGEKGRMLFGKLM- 453
Cdd:PRK13547 82 arlrAVLPQAAQPAFAfsaREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 454 --------MEKPNILVMDEPTNHLDMESIESL-----NMALEMYQGTLIFVsHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRIAMLADGAIV 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
333-498 |
2.75e-06 |
|
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: 48.48 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE------------------ 394
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysvayaaqkpwllnat 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 FENDLTVFDWMSQWKQEG-DDEQAVRSILGRLLF-SQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDME 472
Cdd:cd03290 95 VEENITFGSPFNKQRYKAvTDACSLQPDIDLLPFgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180
....*....|....*....|....*.
gi 695729787 473 SIESLnmaleMYQGTLIFVSHDREFV 498
Cdd:cd03290 175 LSDHL-----MQEGILKFLQDDKRTL 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-210 |
2.89e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKIL----------------------------GGDLEPTLG--NVSLDPNE 64
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyQGDEEQNVGmkNVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 65 RIGKLRQDQFAFEEF--TVLDTVIMGHAELWE-------VKQERdriyALAEMSEEDGYKVAELETQYGEMDGYSAEARA 135
Cdd:PTZ00265 1262 KEGGSGEDSTVFKNSgkILLDGVDICDYNLKDlrnlfsiVSQEP----MLFNMSIYENIKFGKEDATREDVKRACKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 136 GELLLGVGIPVEQHYGPMSE-VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISH 210
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADKTIITIAH 1417
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-210 |
3.12e-06 |
|
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: 49.08 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKST----FMKILGGDLEPTLGNVSLDP------NERIGKL 69
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNTEGDIQIDGVSWNSvplqkwRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 RQDQFAFEEFTVLDTVIMGH---AELWEVkqerdriyalaemSEEDGYKVAeLETQYGEMDgysaearageLLLGVGIPV 146
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKwsdEEIWKV-------------AEEVGLKSV-IEQFPGQLD----------FVLVDGGCV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 147 EQHygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03289 139 LSH---------GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
343-493 |
3.29e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 343 EVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQD----------HEYEFENDLTVFD--WMSQWKQ 410
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagvaiiyQELHLVPEMTVAEnlYLGQLPH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 411 EG---DDEQAVRSILGRLLFSQDDIKKPAKV--LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMALEMY- 484
Cdd:PRK11288 108 KGgivNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELr 187
|
170
....*....|.
gi 695729787 485 -QGT-LIFVSH 493
Cdd:PRK11288 188 aEGRvILYVSH 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
3.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLEPTL---GNVSL---DPNER---IGKLR-QD 72
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESEVrveGRVEFfnqNIYERrvnLNRLRrQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 73 QFAFEE-----FTVLDTVIMGHAEL-WEVKQERDRIYalaemseEDGYKVAELETQygemdgysaearagelllgvgIPV 146
Cdd:PRK14258 91 SMVHPKpnlfpMSVYDNVAYGVKIVgWRPKLEIDDIV-------ESALKDADLWDE---------------------IKH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 147 EQHYGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDS-TMIIISHDRHFLNMVCTHM 222
Cdd:PRK14258 143 KIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFT 221
|
250
....*....|
gi 695729787 223 ADLDYGELRV 232
Cdd:PRK14258 222 AFFKGNENRI 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
3.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDL-----EPTLGNVSLDPN----ERIG 67
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 68 KLRQD---QFAFEEFTVLDTVImghaelwevkqERDRIYALAEMSE--EDGYKvaeletqygemdgysaeaRAGELLLGV 142
Cdd:PRK13645 87 RLRKEiglVFQFPEYQLFQETI-----------EKDIAFGPVNLGEnkQEAYK------------------KVPELLKLV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695729787 143 GIPVEQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13645 138 QLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
320-477 |
4.22e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------------SENAQIGYY 387
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpksSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQDHEY--------------EFENDLTVFDWmSQWKQEGDDeqavrsILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLM 453
Cdd:PRK10762 85 HQELNLipqltiaeniflgrEFVNRFGRIDW-KKMYAEADK------LLARLNLRFSS-DKLVGELSIGEQQMVEIAKVL 156
|
170 180
....*....|....*....|....*
gi 695729787 454 MEKPNILVMDEPTNHL-DMESiESL 477
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTET-ESL 180
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
158-226 |
4.61e-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: 46.76 E-value: 4.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:cd03223 94 GGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-367 |
5.73e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 5.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG 367
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-470 |
6.26e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.62 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 338 FNLLLEVGEKIAILGANGVGKSTMLKTLVGeLQPDNGTV--------KWSENAQI---GYYAQDHEYEFENDltVFDWMS 406
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleAWSAAELArhrAYLSQQQTPPFAMP--VFQYLT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 407 QWKQEGDDEQAVRSILGRL---LFSQDDIKKPAKVLSGGEKGRM-LFGKLMMEKPNI------LVMDEPTNHLD 470
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVaeaLGLDDKLGRSVNQLSGGEWQRVrLAAVVLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-261 |
6.87e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVsldpnERIGklrqdqfafeEFTVLDTVIMGHAELWEVKQ 97
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----DRNG----------EVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 98 ERDRIYALaemseedGYKVAELETQYGEMDGYSaeaRAGELLlgvgipveqhYGPMSEVAPGWKLRVLLAQALFSNPDIL 177
Cdd:PRK13546 106 IEFKMLCM-------GFKRKEIKAMTPKIIEFS---ELGEFI----------YQPVKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 178 LLDEPTNNLD-------IDTIrwleQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYpGNYDEYMtaatQARER 250
Cdd:PRK13546 166 VIDEALSVGDqtfaqkcLDKI----YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVL----PKYEA 236
|
250
....*....|..
gi 695729787 251 LLADNAKK-KAQ 261
Cdd:PRK13546 237 FLNDFKKKsKAE 248
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-254 |
7.06e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdleptlgnVSLDpNERIgklRQDQFAFEEFTV 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKD-NWRV---TADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 82 LDTV------IMGHaELWEVKQERDriyALAEMSEEDGYKVAEletqygEMDGYSAEA-----------RAGELLLGVGI 144
Cdd:PRK15093 76 LRLSprerrkLVGH-NVSMIFQEPQ---SCLDPSERVGRQLMQ------NIPGWTYKGrwwqrfgwrkrRAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 145 pvEQHYGPMS----EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLN 216
Cdd:PRK15093 146 --KDHKDAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 695729787 217 MVCTHMADLDYGElRVYPGNYDEYMTAA----TQARERLLAD 254
Cdd:PRK15093 224 QWADKINVLYCGQ-TVETAPSKELVTTPhhpyTQALIRAIPD 264
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
7.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.82 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLF--ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIgklrqDQFAFEEftvld 83
Cdd:PRK13648 12 NVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN-NQAI-----TDDNFEK----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 84 tvIMGHAELweVKQERDRIYALAEMSeedgYKVA-ELETQ---YGEMdgysaEARAGELLLGVGIPVEQHYGPMSeVAPG 159
Cdd:PRK13648 81 --LRKHIGI--VFQNPDNQFVGSIVK----YDVAfGLENHavpYDEM-----HRRVSEALKQVDMLERADYEPNA-LSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 160 WKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHD 211
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDpdarqnlLDLVRKVKS---EHNITIISITHD 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-474 |
7.92e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.20 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV----------KWSENAQ--IGYY 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllPLHARARrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 388 AQdhEYEFENDLTVFD-WMSQWKQEGDDEQAVRSILGRLLFSQDDIK----KPAKVLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:PRK10895 84 PQ--EASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEhlrdSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170
....*....|..
gi 695729787 463 DEPTNHLDMESI 474
Cdd:PRK10895 162 DEPFAGVDPISV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
333-493 |
8.01e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.57 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYaqDHEY--------EFENDL---TV 401
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQY--DHHYlhrqvalvGQEPVLfsgSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 FDWMSQWKQEGDDEQaVRSIlGRLLFSQDDIKKPAK-----------VLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD 470
Cdd:TIGR00958 572 RENIAYGLTDTPDEE-IMAA-AKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|...
gi 695729787 471 MESIESLNMALEMYQGTLIFVSH 493
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
8.29e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNV------SLDPN--ERIGKL-- 69
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidTGDFSklQGIRKLvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 70 ---RQDQFAFEEFTVLDTVIMGHAELW----EVKQERDRiyALAEmseedgykvaeletqygemdgysaearagelllgV 142
Cdd:PRK13644 81 ivfQNPETQFVGRTVEEDLAFGPENLClppiEIRKRVDR--ALAE----------------------------------I 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 143 GIPVEQHYGPMSeVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-IRWLE--QTLNDRDSTMIIISHdrhflNMVC 219
Cdd:PRK13644 125 GLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLEriKKLHEKGKTIVYITH-----NLEE 198
|
250
....*....|....*..
gi 695729787 220 THMAD----LDYGELRV 232
Cdd:PRK13644 199 LHDADriivMDRGKIVL 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-506 |
8.44e-06 |
|
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: 46.27 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGfdegPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW------------SENAQI 384
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 GYYAQDHeyefendltvfdwmsqwKQEG-DDEQAVRS--ILGRLLfsqddikkpakvlSGGEKGRMLFGKLMMEKPNILV 461
Cdd:cd03215 78 AYVPEDR-----------------KREGlVLDLSVAEniALSSLL-------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695729787 462 MDEPTNHLDMESIESL-NMALEMYQ--GTLIFVSHDREFVSSLATRVI 506
Cdd:cd03215 128 LDEPTRGVDVGAKAEIyRLIRELADagKAVLLISSELDELLGLCDRIL 175
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
1.12e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.95 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTL---GNVSL----------DPNE-- 64
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLdgediydpdvDVVElr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 65 -RIGKLRQDQFAFEeFTVLDTVIMGHaelwEVKQERDRiyalaemseedgykvaeletqyGEMDgysaeARAGELLLGVG 143
Cdd:COG1117 92 rRVGMVFQKPNPFP-KSIYDNVAYGL----RLHGIKSK----------------------SELD-----EIVEESLRKAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 144 IPveqhygpmSEV-----APGWKL------RVLLAQALFSNPDILLLDEPTNNLD-IDTIRwLEQTLND--RDSTMIIIS 209
Cdd:COG1117 140 LW--------DEVkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElkKDYTIVIVT 210
|
....*...
gi 695729787 210 HdrhflNM 217
Cdd:COG1117 211 H-----NM 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
339-506 |
1.23e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 339 NLLLEVGEKI------AILGANGVGKSTMLKTLVGELQPDNGTVKWS---------------ENAQIGYYAQDHE----Y 393
Cdd:PRK11144 12 DLCLTVNLTLpaqgitAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiclppEKRRIGYVFQDARlfphY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 394 EFENDLTVfdWMSqwkqEGDDEQ--------AVRSILGRLLFSqddikkpakvLSGGEKGRMLFGKLMMEKPNILVMDEP 465
Cdd:PRK11144 92 KVRGNLRY--GMA----KSMVAQfdkivallGIEPLLDRYPGS----------LSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 466 TNHLDMESIESLNMALEMYQGTL----IFVSHDREFVSSLATRVI 506
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREInipiLYVSHSLDEILRLADRVV 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
331-526 |
1.29e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 331 EGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGT-------------VKWSENAQIGyyaqdheyefEN 397
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsvvirgsvayvpqVSWIFNATVR----------EN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 398 DLTVFDWMSQWKQEGDDEQAVRSILGrLLFSQD--DIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIE 475
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLD-LLPGRDltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 476 SL---NMALEMYQGTLIFVSHDREFVsSLATRVIEITpERVVDFTGNYEDYLRS 526
Cdd:PLN03232 778 QVfdsCMKDELKGKTRVLVTNQLHFL-PLMDRIILVS-EGMIKEEGTFAELSKS 829
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-245 |
1.57e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.37 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGdLEPTLGNVSLDpneriGK----------------LRQDQ---FAFEEFT 80
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-----GRplsdwsaaelarhrayLSQQQsppFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 81 VLDTVIMGHAELWEVKQErdrIYALAEmseedgykvaeletQYGEMDGYSaeaRagelllgvgiPVEQHYGpmsevapG- 159
Cdd:COG4138 89 YLALHQPAGASSEAVEQL---LAQLAE--------------ALGLEDKLS---R----------PLTQLSG-------Ge 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 160 WKlRVLLAQALF-----SNPD--ILLLDEPTNNLDI------DtiRWLEQtLNDRDSTMIIISHDrhfLNMVCTHmAD-- 224
Cdd:COG4138 132 WQ-RVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVaqqaalD--RLLRE-LCQQGITVVMSSHD---LNHTLRH-ADrv 203
|
250 260
....*....|....*....|...
gi 695729787 225 --LDYGELrVYPGNYDEYMTAAT 245
Cdd:COG4138 204 wlLKQGKL-VASGETAEVMTPEN 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-72 |
1.72e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 46.62 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGS-----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD-------PNER--- 65
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklPEYKrak 80
|
....*...
gi 695729787 66 -IGKLRQD 72
Cdd:COG1101 81 yIGRVFQD 88
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
32-190 |
1.90e-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: 45.72 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 32 LIGANGSGKSTFMKILGGDLEptlGNVSLDpneriGKLRQDQFAFEEFtvldtvimghaelwEVKQERDRIYAlaemSEE 111
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTE---GNVSVE-----GDIHYNGIPYKEF--------------AEKYPGEIIYV----SEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 112 DgYKVAEL---ETqygeMDgYSAEARAGELLLGvgipveqhygpmseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:cd03233 92 D-VHFPTLtvrET----LD-FALRCKGNEFVRG--------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
..
gi 695729787 189 DT 190
Cdd:cd03233 152 ST 153
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-211 |
2.40e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.30 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDPN--------------ERIGKLRQ 71
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsrlytvrKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTV---IMGHAELWEVkqerdRIYALAEMSEEdgykvaeletqygemdgysaearagelllGVGIPVEQ 148
Cdd:PRK11831 92 SGALFTDMNVFDNVaypLREHTQLPAP-----LLHSTVMMKLE-----------------------------AVGLRGAA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695729787 149 HYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS----TMIIISHD 211
Cdd:PRK11831 138 KLMP-SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
317-526 |
2.41e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 317 RNALEVEALTKGFDEG----PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE------NAQI-- 384
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 385 ----------GYYAQDHEYEFENDLT----VFDWMSQ------WKQEGDDEQAVRSI-----LGRLLFSQDDIKKPAKVL 439
Cdd:PRK10261 90 lseqsaaqmrHVRGADMAMIFQEPMTslnpVFTVGEQiaesirLHQGASREEAMVEAkrmldQVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 440 SGGEKGRMLFGKLMMEKPNILVMDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVIEITPER 512
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqaqiLQLIKVLQKEMSM---GVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|....
gi 695729787 513 VVDfTGNYEDYLRS 526
Cdd:PRK10261 247 AVE-TGSVEQIFHA 259
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-508 |
2.56e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGeLQPD---NGTVKWSENAQIGYYAQDHEYE-- 394
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERAgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 --FENDLTVFDWMS-------------QWKQEGDDEQAVR--SILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKP 457
Cdd:TIGR02633 81 viIHQELTLVPELSvaeniflgneitlPGGRMAYNAMYLRakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695729787 458 NILVMDEPTNHLDMESIES-LNMALEMYQGTL--IFVSHDREFVSSLATRVIEI 508
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEIlLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVI 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
335-494 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 335 FKNFNL-LLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV----KWSEnaQIGYYAQDHEYEFENDLTVFDWMSQWK 409
Cdd:cd03236 15 FKLHRLpVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE--ILDEFRGSELQNYFTKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 410 QEGDDE--QAVRSILGRLLFSQDDIKKPAKV----------------LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM 471
Cdd:cd03236 93 PQYVDLipKAVKGKVGELLKKKDERGKLDELvdqlelrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 695729787 472 EsiESLNMA-----LEMYQGTLIFVSHD 494
Cdd:cd03236 173 K--QRLNAArlireLAEDDNYVLVVEHD 198
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
3.29e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKfgGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLD--------PNER-IGKLRQ 71
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 72 DQFAFEEFTVLDTVIMG-HAELWEVKQERDRIYALAE-MSEEDgykvaELETQYGEMDGysaearagelllgvgipveqh 149
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlNPGLKLNAAQREKLHAIARqMGIED-----LLARLPGQLSG--------------------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 150 ygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK10771 133 ---------GQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-245 |
3.89e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.09 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQFAFEEFTVLD-----TVIMGHAELWEVkqerdriyal 105
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDllssiTKDFYTHPYFKT---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 106 aemseeDGYKVAELEtqyGEMDGYSAEARAGELllgvgipveQhygpmsevapgwklRVLLAQALFSNPDILLLDEPTNN 185
Cdd:cd03237 98 ------EIAKPLQIE---QILDREVPELSGGEL---------Q--------------RVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695729787 186 LDID----TIRWLEQTLNDRDSTMIIISHDrhFLnmvcthMADLDYGELRVYPGNYDEYMTAAT 245
Cdd:cd03237 146 LDVEqrlmASKVIRRFAENNEKTAFVVEHD--II------MIDYLADRLIVFEGEPSVNGVANP 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-211 |
4.31e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDL-EPTL-------GNVSLD-------PNER 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtGGGAprgarvtGDVTLNgeplaaiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 66 IGKLR-----QDQFAFeEFTVLDTVIMG---HAElwevkqerdriyALAEMSEEDGyKVAeletqygemdgYSAEARAGE 137
Cdd:PRK13547 81 LARLRavlpqAAQPAF-AFSAREIVLLGrypHAR------------RAGALTHRDG-EIA-----------WQALALAGA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 138 LLLgVGIPVEQHYGpmSEVApgwklRVLLAQAL---------FSNPDILLLDEPTNNLD-------IDTIRWLEqtlndR 201
Cdd:PRK13547 136 TAL-VGRDVTTLSG--GELA-----RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTVRRLA-----R 202
|
250
....*....|..
gi 695729787 202 DSTM--IIISHD 211
Cdd:PRK13547 203 DWNLgvLAIVHD 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-493 |
4.41e-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: 44.79 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGT-----VKWSE------NAQIGYYAQDHeyefendlTV 401
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgVDISKiglhdlRSRISIIPQDP--------VL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 402 F--------DWMSQWkqeGDDE--QAVRSILGRLLFSQDDIKKPAKVLSGGEK---G-RMLF--GKLMMEKPNILVMDEP 465
Cdd:cd03244 90 FsgtirsnlDPFGEY---SDEElwQALERVGLKEFVESLPGGLDTVVEEGGENlsvGqRQLLclARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|
gi 695729787 466 TNHLDMESIESLNMAL--EMYQGTLIFVSH 493
Cdd:cd03244 167 TASVDPETDALIQKTIreAFKDCTVLTIAH 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-190 |
4.63e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSldPNERIGKLRQDQFAFEEfTVLDTVIMGHAelwe 94
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPG-TIKDNIIFGLS---- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 95 VKQERDRIYALAEMSEEDGYKVAELE-TQYGEmdgysaearAGELLLGvgipveqhygpmsevapGWKLRVLLAQALFSN 173
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDIALFPEKDkTVLGE---------GGITLSG-----------------GQRARISLARAVYKD 566
|
170
....*....|....*..
gi 695729787 174 PDILLLDEPTNNLDIDT 190
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVT 583
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-230 |
5.23e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLE-----PTLGNVSL----------DPNE---R 65
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLfgrniyspdvDPIEvrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 66 IGKLRQDQFAFEEFTVLDTVIMG--HAELWEVKQERDRI--YALAemseedgyKVAELETQYGEMDGYSAEARAGElllg 141
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAIGvkLNGLVKSKKELDERveWALK--------KAALWDEVKDRLNDYPSNLSGGQ---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 142 vgipveqhygpmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVC 219
Cdd:PRK14267 155 -------------------RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFElkKEYTIVLVTHSPAQAARVS 215
|
250
....*....|.
gi 695729787 220 THMADLDYGEL 230
Cdd:PRK14267 216 DYVAFLYLGKL 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
320-513 |
5.25e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFdeGPLF--KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYyaQDHEYE--- 394
Cdd:PRK11300 6 LSVSGLMMRF--GGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 ----FEN-----DLTVFD--WMSQWKQEGDD-----------EQAVRSILGRLLFSQDDI------KKPAKVLSGGEKGR 446
Cdd:PRK11300 82 vvrtFQHvrlfrEMTVIEnlLVAQHQQLKTGlfsgllktpafRRAESEALDRAATWLERVgllehaNRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 447 MLFGKLMMEKPNILVMDEPTNHLDMESIESLNMAL----EMYQGTLIFVSHDREFVSSLATRVIEI---------TPERV 513
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVnqgtplangTPEEI 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
140-215 |
5.44e-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: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 140 LGVG-IPVEQhygPMSEVAPGWKLRVLLAQALFSNPD--ILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRH 213
Cdd:cd03238 74 VGLGyLTLGQ---KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLD 150
|
..
gi 695729787 214 FL 215
Cdd:cd03238 151 VL 152
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
439-515 |
6.34e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 439 LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDM-----------ESIESLNMAlemyqgtLIFVSHDREFVSSLATRVIE 507
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMG-------LLFITHNLSIVRKLADRVAV 229
|
....*...
gi 695729787 508 ITPERVVD 515
Cdd:PRK15134 230 MQNGRCVE 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-212 |
7.14e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 32 LIGANGSGKSTFMKILGGDLEPTLGNVSLDPNE--------------RIGKLRQDQFAFEEFTVLDTVIMGhaelwevkq 97
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrevpflrrQIGMIFQDHHLLMDRTVYDNVAIP--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 98 erdriYALAEMSEEDgykvaeletqygemdgysAEARAGELLLGVGIPVEQHYGPMsEVAPGWKLRVLLAQALFSNPDIL 177
Cdd:PRK10908 104 -----LIIAGASGDD------------------IRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 695729787 178 LLDEPTNNLD----IDTIRWLEQtLNDRDSTMIIISHDR 212
Cdd:PRK10908 160 LADEPTGNLDdalsEGILRLFEE-FNRVGVTVLMATHDI 197
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-76 |
7.88e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 7.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLR---QDQFAF 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-RQSIKKDLctyQKQLCF 78
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
440-506 |
8.16e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 8.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 440 SGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMeSIES--LN--MALEMYQGT-LIFVSHDREFVSSLATRVI 506
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqvLNlmMDLQQELGLsYVFISHDLSVVEHIADEVM 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-526 |
8.31e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 334 LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAqIGYYAQD---HEYEFENDLTVFDwmsqWKQ 410
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERS-IAYVPQQawiMNATVRGNILFFD----EED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 411 EGDDEQAVR--------SILGRLLfsQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIEslNMALE 482
Cdd:PTZ00243 749 AARLADAVRvsqleadlAQLGGGL--ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE--RVVEE 824
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695729787 483 MYQGTL-----IFVSHDREFVsSLATRVIEITPERVVdFTGNYEDYLRS 526
Cdd:PTZ00243 825 CFLGALagktrVLATHQVHVV-PRADYVVALGDGRVE-FSGSSADFMRT 871
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
320-521 |
1.16e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFDEGP-----LFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV---------KWSENAQIG 385
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 386 YYAQDH------------------EYEFENDLTVFDWM------SQWKQEGddEQAVRSILGRLLFSQDDIKKPAKVLSG 441
Cdd:PRK13631 102 NPYSKKiknfkelrrrvsmvfqfpEYQLFKDTIEKDIMfgpvalGVKKSEA--KKLAKFYLNKMGLDDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 442 GEKGRMLFGKLMMEKPNILVMDEPTNHLDMESiESLNMAL----EMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFT 517
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKG-EHEMMQLildaKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
....
gi 695729787 518 GNYE 521
Cdd:PRK13631 259 TPYE 262
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-530 |
1.19e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV---------------KWSENAQIGYYAQdhEYEFENDLT 400
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQ--SFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 401 VFD------WMSQWKQEGDDEQAVRSIlgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD---- 470
Cdd:PRK10070 123 VLDntafgmELAGINAEERREKALDAL--RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplir 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695729787 471 MESIESLNMALEMYQGTLIFVSHDREFVSSLATR--------VIEI-TPERVVDFTGNyeDYLRS--KGID 530
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRiaimqngeVVQVgTPDEILNNPAN--DYVRTffRGVD 269
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
320-483 |
1.41e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGFD-EGPLF--------KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----AQIGY 386
Cdd:PRK15112 5 LEVRNLSKTFRyRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 387 YAQDHEYEFENDLTVFDWMSQWKQEGD-------------DEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLM 453
Cdd:PRK15112 85 RSQRIRMIFQDPSTSLNPRQRISQILDfplrlntdlepeqREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190
....*....|....*....|....*....|..
gi 695729787 454 MEKPNILVMDEPTNHLDMeSIES--LNMALEM 483
Cdd:PRK15112 165 ILRPKVIIADEALASLDM-SMRSqlINLMLEL 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-211 |
1.76e-04 |
|
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: 44.29 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMK-ILGgdLEPTLGNVSLDpNERIGKLRQDQFafeeftvldtvimghaelwevKQERDRI------- 102
Cdd:COG4172 316 GLVGESGSGKSTLGLaLLR--LIPSEGEIRFD-GQDLDGLSRRAL---------------------RPLRRRMqvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 103 YA-LA-EMSEEDgyKVAE-LETQYGEMDGYSAEARAGELLLGVGIPVE--QHYgPmSEVAPGWKLRVLLAQALFSNPDIL 177
Cdd:COG4172 372 FGsLSpRMTVGQ--IIAEgLRVHGPGLSAAERRARVAEALEEVGLDPAarHRY-P-HEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695729787 178 LLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHD 211
Cdd:COG4172 448 VLDEPTSALDvsvqaqiLDLLRDLQR---EHGLAYLFISHD 485
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
160-248 |
1.91e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.00 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 160 WKlRVLLAQALF-----SNPD--ILLLDEPTNNLDIDTIRWLEQTLNDRDS---TMIIISHDrhfLNMVCTHmAD----L 225
Cdd:PRK03695 132 WQ-RVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LNHTLRH-ADrvwlL 206
|
90 100
....*....|....*....|...
gi 695729787 226 DYGELRVYpGNYDEYMTAATQAR 248
Cdd:PRK03695 207 KQGKLLAS-GRRDEVLTPENLAQ 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-61 |
1.95e-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: 1.95e-04
10 20 30
....*....|....*....|....*....|.
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLD 61
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWD 59
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-470 |
1.99e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 31 GLIGANGSGKSTFMKILGGDLEPTLGNVSLDPNER------------IGKLRQDQFAFEEFTVLDTVIMGHaelwEVKQE 98
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeagIGIIHQELNLIPQLTIAENIFLGR----EFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 99 RDRIyALAEMSEEDGYKVAELETQYgemdgySAEARAGELLLGvgipvEQHygpMSEVApgwklrvllaQALFSNPDILL 178
Cdd:PRK10762 110 FGRI-DWKKMYAEADKLLARLNLRF------SSDKLVGELSIG-----EQQ---MVEIA----------KVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 179 LDEPTNNL-DIDT------IRwleqTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrvypgnYDEYMTAATQaRERL 251
Cdd:PRK10762 165 MDEPTDALtDTETeslfrvIR----ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF------IAEREVADLT-EDSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 252 LadnakkkaqiadlQSFVSRfsanasksrqatsrarqidkiKLEEvkassrQNPfiRFEQDKKLFRnaLEVEALTkgfde 331
Cdd:PRK10762 234 I-------------EMMVGR---------------------KLED------QYP--RLDKAPGEVR--LKVDNLS----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 332 GPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTVKWSE------------NAQIGYYAQDHEYE----- 394
Cdd:PRK10762 265 GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGIVYISEDRKRDglvlg 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 395 ---FEN-DLTVFDWMSQWK---QEGDDEQAVRSILGrlLFsqdDIKKPAK-----VLSGGEKGRMLFGKLMMEKPNILVM 462
Cdd:PRK10762 345 msvKENmSLTALRYFSRAGgslKHADEQQAVSDFIR--LF---NIKTPSMeqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
|
....*...
gi 695729787 463 DEPTNHLD 470
Cdd:PRK10762 420 DEPTRGVD 427
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
155-243 |
2.05e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RD--STMIIISHDRHFLNMVCTHMadldygeL 230
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREfnTAIIMITHDLGVVAGICDKV-------L 233
|
90
....*....|...
gi 695729787 231 RVYPGNYDEYMTA 243
Cdd:PRK09473 234 VMYAGRTMEYGNA 246
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
434-511 |
2.14e-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: 42.31 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 434 KPAKVLSGGEKGRMLFGKLMME--KPNILVMDEPTNHLDMESIESLnmaLEMYQG------TLIFVSHDREFVSSlATRV 505
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQL---LEVIKGlidlgnTVILIEHNLDVLSS-ADWI 158
|
....*.
gi 695729787 506 IEITPE 511
Cdd:cd03238 159 IDFGPG 164
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-473 |
3.01e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENAQIGYYAQDHEYEFENDLTVFD-----------WM 405
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQSEEVDWSFPVLVEDvvmmgryghmgWL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695729787 406 SQWKQEgdDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES 473
Cdd:PRK15056 113 RRAKKR--DRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-74 |
3.15e-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: 3.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 695729787 32 LIGANGSGKSTFMKILGGDLEPTLGNVSLDpNERIGKLRQDQF 74
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTADNREAY 404
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
411-509 |
3.99e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 411 EGD-DEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES---IESLNMALEMy 484
Cdd:PRK14243 121 KGDmDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKE- 199
|
90 100
....*....|....*....|....*
gi 695729787 485 QGTLIFVSHDREfvssLATRVIEIT 509
Cdd:PRK14243 200 QYTIIIVTHNMQ----QAARVSDMT 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
434-524 |
4.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 434 KPAKVLSGGEKGRMlfgKLMME------KPNILVMDEPTNHLDMESIESLNMALE--MYQG-TLIFVSHDREFVsSLATR 504
Cdd:PRK00635 805 RPLSSLSGGEIQRL---KLAYEllapskKPTLYVLDEPTTGLHTHDIKALIYVLQslTHQGhTVVIIEHNMHVV-KVADY 880
|
90 100
....*....|....*....|
gi 695729787 505 VIEITPErvvdfTGNYEDYL 524
Cdd:PRK00635 881 VLELGPE-----GGNLGGYL 895
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-231 |
4.22e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 27 GNRYGLIGANGSGKSTFMKILGGDLEPTLGNVSldpnerigklrqdqfafeeftvldtvimghaelwevkqerdriyala 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 107 emseedgykvaeletqYGEMDGYSAEARAGELLLGVGIPVEQHYGPMsevapgwKLRVLLAQALFSNPDILLLDEPTNNL 186
Cdd:smart00382 35 ----------------YIDGEDILEEVLDQLLLIIVGGKKASGSGEL-------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 187 DIDTIRWLEQTLNDRDSTMIIISHDRHFLnMVCTHMADLDYGELR 231
Cdd:smart00382 92 DAEQEALLLLLEELRLLLLLKSEKNLTVI-LTTNDEKDLGPALLR 135
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
345-528 |
5.07e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.64 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 345 GEKIAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDHEYeFenDLTVFDWMSQWKQEGD 413
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtraSLRRNIAVVFQDAGL-F--NRSIEDNIRVGRPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 414 DE---------QAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMESIESLNMAL-EM 483
Cdd:PRK13657 438 DEemraaaeraQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdEL 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 695729787 484 YQGTLIFVSHDREFVSSLATRVIEITPERVVDfTGNYEDYLRSKG 528
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVE-SGSFDELVARGG 561
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-218 |
5.08e-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: 43.11 E-value: 5.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695729787 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--------RDSTMIIISHDRHFLNMV 218
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiiksrsqqRNFQLLVITHDEDFVELL 1276
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
159-236 |
5.44e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD--------IDTIRwLEQTLNdrdSTMIIISHDRhflnMVCTHMAD----LD 226
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISR-LHKRLG---RTMIYVTHDQ----VEAMTLADkivvLD 208
|
90
....*....|....*....
gi 695729787 227 YG---------ELRVYPGN 236
Cdd:PRK11000 209 AGrvaqvgkplELYHYPAN 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
133-224 |
8.61e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.49 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 133 ARAGELLLGVGIPVEqHYG--P-MseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIdTIRwlEQTLN---DRDSTM- 205
Cdd:PRK11308 132 EKALAMMAKVGLRPE-HYDryPhM--FSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQ--AQVLNlmmDLQQELg 205
|
90 100
....*....|....*....|..
gi 695729787 206 ---IIISHDrhfLNMVcTHMAD 224
Cdd:PRK11308 206 lsyVFISHD---LSVV-EHIAD 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
439-526 |
9.48e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 439 LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMeSIES--LNMALEMYQG---TLIFVSHDREFVSSLATRVIEITPERV 513
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqiIELLLELQQKenmALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|...
gi 695729787 514 VDfTGNYEDYLRS 526
Cdd:PRK11022 233 VE-TGKAHDIFRA 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
159-210 |
1.02e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIR----WLEQTLNDRDSTMIIISH 210
Cdd:PRK11144 132 GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSH 187
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-271 |
1.54e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 152 PMSEVAPGWKLRVLLAQALFS---NPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISHDRHFLNmVCTHMAdl 225
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL-- 882
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 695729787 226 dygELRVYPGNYDEYMTAATQARERLLADNAKKKAqiadLQSFVSR 271
Cdd:PRK00635 883 ---ELGPEGGNLGGYLLASCSPEELIHLHTPTAKA----LRPYLSS 921
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
163-200 |
1.55e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 39.72 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 695729787 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND 200
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
336-530 |
1.87e-03 |
|
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: 40.32 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 336 KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA-------QIGYYAQD-----HEYEF 395
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaAMSRKElrelrrkKISMVFQSfallpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 ENdlTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD----- 470
Cdd:cd03294 121 EN--VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirr 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 471 -MESiESLNMALEMyQGTLIFVSHDREFVSSLATR--------VIEI-TPERVVdfTGNYEDYLRS--KGID 530
Cdd:cd03294 198 eMQD-ELLRLQAEL-QKTIVFITHDLDEALRLGDRiaimkdgrLVQVgTPEEIL--TNPANDYVREffRGVD 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-367 |
2.69e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 2.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG 367
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-187 |
2.69e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 32 LIGANGSGKSTFMKILGGDLepTLGNVS----------LDPN--ERIGKLRQDQFAFEEFTVLDTVIMGhAELwevkqer 99
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERV--TTGVITggdrlvngrpLDSSfqRSIGYVQQQDLHLPTSTVRESLRFS-AYL------- 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 100 dRIYALAEMSEEDGY--KVAELEtqygEMDGYsAEARAGelLLGVGIPVEQhygpmsevapgwKLRVLLAQALFSNPDIL 177
Cdd:TIGR00956 864 -RQPKSVSKSEKMEYveEVIKLL----EMESY-ADAVVG--VPGEGLNVEQ------------RKRLTIGVELVAKPKLL 923
|
170
....*....|.
gi 695729787 178 L-LDEPTNNLD 187
Cdd:TIGR00956 924 LfLDEPTSGLD 934
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-506 |
2.71e-03 |
|
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: 40.04 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 320 LEVEALTKGF--DEGPLF--KNFNLLLEVGEKIAILGANGVGKSTMLKTLVGeLQPDNGTVKwsenaqiGyyaqdhEYEF 395
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITS-------G------EILF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 396 EN-DLT-----------------VF-DWMS----------Q-----WKQEGDDEQAVRSILGRLLfSQDDIKKPAKV--- 438
Cdd:COG0444 68 DGeDLLklsekelrkirgreiqmIFqDPMTslnpvmtvgdQiaeplRIHGGLSKAEARERAIELL-ERVGLPDPERRldr 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 439 ----LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLD-------MESIESLNMALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNLLKDLQRELGL---AILFITHDLGVVAEIADRVA 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
328-376 |
2.73e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.34 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 695729787 328 GFDEGPLfknfNLLLEVGEKIAILGANGVGKSTMLKTLVGELQPDNGTV 376
Cdd:PRK10522 336 GFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
3.64e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLEPTL---GNV----------SLDPNE-- 64
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGFrveGKVtfhgknlyapDVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 65 -RIGKLRQDQFAFEEfTVLDTVIMGhaelwevkqerDRIyalaemseeDGYKvaeletqyGEMDGYSAEA-RAGELLLGV 142
Cdd:PRK14243 91 rRIGMVFQKPNPFPK-SIYDNIAYG-----------ARI---------NGYK--------GDMDELVERSlRQAALWDEV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695729787 143 GIPVEQHYGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD-IDTIRwLEQTLND--RDSTMIIISHD 211
Cdd:PRK14243 142 KDKLKQSGLSLSG---GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHElkEQYTIIIVTHN 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-188 |
3.96e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 39.62 E-value: 3.96e-03
10 20
....*....|....*....|....*
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-61 |
4.14e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 4.14e-03
10 20 30
....*....|....*....|....*....|
gi 695729787 32 LIGANGSGKSTFMKILGGDLEPTLGNVSLD 61
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
290-473 |
4.37e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 290 DKIKLEEVKASSRQNpfIRFEQDKklfRNALEVealtkgfdegplFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVGEL 369
Cdd:PTZ00265 373 DGKKLKDIKKIQFKN--VRFHYDT---RKDVEI------------YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 370 QPDNGTV-------------KWSEnAQIGYYAQDhEYEFEND-----------LTVFDWMSQWKQEG-----DDEQAVRS 420
Cdd:PTZ00265 436 DPTEGDIiindshnlkdinlKWWR-SKIGVVSQD-PLLFSNSiknnikyslysLKDLEALSNYYNEDgndsqENKNKRNS 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 421 ILGRLLFSQDDIKKP------------------------------------------------AKVLSGGEKGRMLFGKL 452
Cdd:PTZ00265 514 CRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARA 593
|
250 260
....*....|....*....|.
gi 695729787 453 MMEKPNILVMDEPTNHLDMES 473
Cdd:PTZ00265 594 IIRNPKILILDEATSSLDNKS 614
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
320-376 |
4.41e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 4.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 695729787 320 LEVEALTKGFDEGPLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG--ELQPDNGTV 376
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTV 60
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
333-473 |
5.75e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 333 PLFKNFNLLLEVGEKIAILGANGVGKSTMLKTLVG--ELQPDNGTVKWSENAQIGYYAQDHEYEFENDLTV--FDWMSQW 408
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMknVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 409 KQEGD-DEQAVRSILGRLLF------------------------------------------SQDDIKKPAKV------- 438
Cdd:PTZ00265 1262 KEGGSgEDSTVFKNSGKILLdgvdicdynlkdlrnlfsivsqepmlfnmsiyenikfgkedaTREDVKRACKFaaidefi 1341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695729787 439 -----------------LSGGEKGRMLFGKLMMEKPNILVMDEPTNHLDMES 473
Cdd:PTZ00265 1342 eslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
7.32e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLEPTLGNV--------SLDPNER--IGK 68
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIlfkgesilDLEPEERahLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695729787 69 LRQDQFAFEeftvldtvIMG--HAELWEVK-QERDRIYALAEMSEEDGYKVAELETQYGEMDGYSAEARAGELLLGvgip 145
Cdd:CHL00131 87 FLAFQYPIE--------IPGvsNADFLRLAyNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSG---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695729787 146 veqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:CHL00131 155 -------------GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINklmTSENSIILITHYQRLLDYI 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
7.37e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 7.37e-03
10 20
....*....|....*....|....*
gi 695729787 164 VLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| |
