|
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: 1233.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQYT 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLDTVIMGHSELWEVKQERDRIYSLPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQHYGPMSEVAPGW 160
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIYALPEMSEEDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEY 240
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 241 MTAATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRQNPFIRFEQDKKLFRNAL 320
Cdd:PRK15064 241 MTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQDKKLHRNAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 321 EVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFDNDLT 400
Cdd:PRK15064 321 EVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENDLT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAA 480
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 490523037 481 LEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLRSKGIE 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: 759.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQYTVLD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TVIMGHSELWEVKQERDRIYSLPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQHYGPMSEVAPGWKLR 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMTA 243
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 244 ATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEEVKASSRqNPFIRFEQDKKLFRNALEVE 323
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDK-TVEIRFPPPERLGKKVLELE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 324 AMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyEFDNDLTVFD 403
Cdd:COG0488 320 GLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-ELDPDKTVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 404 WMSQWKqEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEM 483
Cdd:COG0488 399 ELRDGA-PGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD 477
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490523037 484 YQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLR 525
Cdd:COG0488 478 FPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-523 |
7.73e-98 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 309.41 E-value: 7.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQyT 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQ-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLDTVIMGHSELWEVKQErdriysLPEMSEE-DGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQHYGPMSEVAPG 159
Cdd:PRK10636 80 ALEYVIDGDREYRQLEAQ------LHDANERnDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 160 WKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYD- 238
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 239 -EYMTAATQARERLLADNAKKKaqIADLQSFVSRFSANASKSRQATSRARQIDKIKLeeVKASSRQNPF-IRFEQDKKLF 316
Cdd:PRK10636 234 fEVQRATRLAQQQAMYESQQER--VAHLQSYIDRFRAKATKAKQAQSRIKMLERMEL--IAPAHVDNPFhFSFRAPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 317 RNALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdHEYEF- 395
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ-HQLEFl 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 DNDLTVFDWMSQWKQEgDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIE 475
Cdd:PRK10636 389 RADESPLQHLARLAPQ-ELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 490523037 476 SLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDY 523
Cdd:PRK10636 468 ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-522 |
1.22e-94 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 301.10 E-value: 1.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQYTVLDT 84
Cdd:PRK11147 7 HGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VIMGHSELWEVKQERDRIYSL--PEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQhygPMSEVAPGWKL 162
Cdd:PRK11147 87 VAEGIEEQAEYLKRYHDISHLveTDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMT 242
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 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 490523037 306 fIRFeqdkklfrnalEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIG 385
Cdd:PRK11147 318 -IVF-----------EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 386 YYAQdHEYEFDNDLTVFDWMSQWKQE----GDDeqavRSILGRL---LFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPN 458
Cdd:PRK11147 386 YFDQ-HRAELDPEKTVMDNLAEGKQEvmvnGRP----RHVLGYLqdfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 459 ILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVD-FSGGYED 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 |
2.23e-88 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 282.21 E-value: 2.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQYTVLDTVIMGHSE 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 92 LWEVKQERDRIYSLpeMSEED------GYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQhyGPMSEVAPGWKLRVL 165
Cdd:TIGR03719 96 IKDALDRFNEISAK--YAEPDadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWD--ADVTKLSGGERRRVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 166 LAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDEYMtaaT 245
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL---E 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 246 QARERLL----ADNAKKKAQIADLQsfvsrFSANASKSRQATSRARQidkIKLEEV--KASSRQNPF--IRFEQDKKLFR 317
Cdd:TIGR03719 249 QKQKRLEqeekEESARQKTLKRELE-----WVRQSPKGRQAKSKARL---ARYEELlsQEFQKRNETaeIYIPPGPRLGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyEFDN 397
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD-ALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTVFDWMSqwkqEGDDEQAV-------RSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD 470
Cdd:TIGR03719 400 NKTVWEEIS----GGLDIIKLgkreipsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 471 MESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPE-RVVDFSGGYEDY 523
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEY 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-523 |
2.41e-84 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 271.61 E-value: 2.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQYTVLDTVIMGHSE 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 92 LWEVKQERDRIYSlpEMSEEDGY------KVADLEVKYGEMDGYSAESRagelllgvgipLEQHY---------GPMSEV 156
Cdd:PRK11819 98 VKAALDRFNEIYA--AYAEPDADfdalaaEQGELQEIIDAADAWDLDSQ-----------LEIAMdalrcppwdAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGN 236
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 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 490523037 308 RFEQDKKLFRNALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYY 387
Cdd:PRK11819 313 FIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEyEFDNDLTVFDWMSqwkqEGDD-------EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK11819 393 DQSRD-ALDPNKTVWEEIS----GGLDiikvgnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 461 VMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPE-RVVDFSGGYEDY 523
Cdd:PRK11819 468 LLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDsQVEWFEGNFQEY 531
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-525 |
1.94e-81 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 268.27 E-value: 1.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGgdLQPSAGnvsLDPNERIGKLRQDQFAfEQYTVLDTV 85
Cdd:PLN03073 182 NFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG---IPKNCQILHVEQEVVG-DDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHSELWEVKQERDRIYSLPEMSEEDGYKVAD----------------LEVKYGEM---DGYSAESRAGELLLGVGIPL 146
Cdd:PLN03073 256 LNTDIERTQLLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavsqrLEEIYKRLeliDAYTAEARAASILAGLSFTP 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 227 YGELRVYPGNYDEY-MTAATQARERLLADNAKKKAQiADLQSFVSRFSANASKSRQATSRARQIDKIK-LEEVKassrQN 304
Cdd:PLN03073 416 GQKLVTYKGDYDTFeRTREEQLKNQQKAFESNERSR-SHMQAFIDKFRYNAKRASLVQSRIKALDRLGhVDAVV----ND 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 305 PFIRFE---QDKKLFRNALEVEAMTKGFDNGP-LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE 380
Cdd:PLN03073 491 PDYKFEfptPDDRPGPPIISFSDASFGYPGGPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 381 NAQIGYYAQDHEYEFDNDLTVFDWMSQWkQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PLN03073 571 KVRMAVFSQHHVDGLDLSSNPLLYMMRC-FPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 461 VMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLR 525
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-527 |
1.29e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 200.29 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 322 VEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEyeFDNDLTV 401
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP--LDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FDW---------------------MSQWKQEGDD----------------EQAVRSILGRLLFSQDDIKKPAKVLSGGEK 444
Cdd:COG0488 79 LDTvldgdaelraleaeleeleakLAEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 445 GRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYL 524
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
...
gi 490523037 525 RSK 527
Cdd:COG0488 239 EQR 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-512 |
1.99e-56 |
|
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: 185.34 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdheyefdndl 399
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 tvfdwmsqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNA 479
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 490523037 480 ALEMYQGTLIFVSHDREFVSSLATRVIEITPER 512
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-241 |
3.57e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 171.79 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAF-EQY 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELdPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 TVLDtvimghsELWEVKQERDRIyslpemseedgykvadlevkygemdgySAESRAGELLLGvGiplEQHYGPMSEVAPG 159
Cdd:COG0488 395 TVLD-------ELRDGAPGGTEQ---------------------------EVRGYLGRFLFS-G---DDAFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 160 WKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYPGNYDE 239
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDD 516
|
..
gi 490523037 240 YM 241
Cdd:COG0488 517 YL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-229 |
7.76e-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: 154.53 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQdqfafeqytvldt 84
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 vimghselwevkqerdriyslpemseedgykvadlevkygemdgysaesragelllgvgipleqhygpMSevaPGWKLRV 164
Cdd:cd03221 71 --------------------------------------------------------------------LS---GGEKMRL 79
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03221 80 ALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-530 |
1.39e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.29 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENAQIGYYAQDHE 392
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 393 yeFDND--LTVFDW--MSQWKQEG-------DDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:COG1121 86 --VDWDfpITVRDVvlMGRYGRRGlfrrpsrADREAVDEALERVgL--EDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 461 VMDEPTNHLDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVvdFSGGYEDYLRSKGIE 530
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTPENLS 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-506 |
3.90e-35 |
|
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: 132.09 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA---QIGYY 387
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYEFDndLTVFD--------WMSQWKQEG-DDEQAVRSILGRLlfsqdDIK----KPAKVLSGGEKGRMLFGKLMM 454
Cdd:COG1120 81 PQEPPAPFG--LTVRElvalgrypHLGLFGRPSaEDREAVEEALERT-----GLEhladRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 455 QKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqlevLELLRRLARERGR---TVVMVLHDLNLAARYADRLV 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-506 |
4.90e-35 |
|
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: 137.73 E-value: 4.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSAGNVSldpneriGKLRqdqFAFEQ 78
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIS-------GEVL---LDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 79 YTVLDTVIMGhSELWEVKQErdriyslpEMSEEDGYKVAD-----LEVkyGEMDGYSAESRAGELLLGVGIPLEQHYGPm 153
Cdd:COG1123 73 LLELSEALRG-RRIGMVFQD--------PMTQLNPVTVGDqiaeaLEN--LGLSRAEARARVLELLEAVGLERRLDRYP- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:COG1123 141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqaeiLDLLRELQR---ERGTTVLLITHDLGVVAEIADRVVVMD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 227 YGELrvypgnydeymtAATQARERLLADNAKKKAqiadlqsfVSRFSANASKSRQATSRARQIdkIKLEEVKassrqnpf 306
Cdd:COG1123 218 DGRI------------VEDGPPEEILAAPQALAA--------VPRLGAARGRAAPAAAAAEPL--LEVRNLS-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 307 IRFEQDKKLFRNALeveamtkgfdngplfKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KW 378
Cdd:COG1123 268 KRYPVRGKGGVRAV---------------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltKL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 379 SENA------QIGYYAQDHEYEFDNDLTVFDWMSQ------WKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGR 446
Cdd:COG1123 333 SRRSlrelrrRVQMVFQDPYSSLNPRMTVGDIIAEplrlhgLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQR 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 447 MLFGKLMMQKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQRELGL---TYLFISHDLAVVRYIADRVA 476
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
321-518 |
6.55e-33 |
|
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: 124.95 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 321 EVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQIGYYAQDHEYE 394
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 FDNDLTVFDW--MSQWKQEG-------DDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDE 464
Cdd:cd03235 81 RDFPISVRDVvlMGLYGHKGlfrrlskADKAKVDEALERVgLS--ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 465 PTNHLDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVIEItpERVVDFSG 518
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL--NRTVVASG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-230 |
7.08e-33 |
|
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: 123.28 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnerigklrqdqfafeqytv 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 ldtvimGHSELWEVKQERDRIYSLPEmseEDGYkvadlevkYGEMDGYsaesragELLLgvgipleqhygpMSEvapGWK 161
Cdd:cd03230 61 ------GKDIKKEPEEVKRRIGYLPE---EPSL--------YENLTVR-------ENLK------------LSG---GMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
9.23e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.84 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE---RIGKL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsRRElarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTVLDTVIMG---HSELWEVKQERDR--IYSLPEMSEedgykVADL-EVKYGEMDGysaesraGELllgvg 143
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGrypHLGLFGRPSAEDReaVEEALERTG-----LEHLaDRPVDELSG-------GER----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 144 ipleQhygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNM-- 217
Cdd:COG1120 144 ----Q--------------RVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNLaa 202
|
250 260
....*....|....*....|....*....
gi 490523037 218 -VCTHMADLDYGELRVYpGNYDEYMTAAT 245
Cdd:COG1120 203 rYADRLVLLKDGRIVAQ-GPPEEVLTPEL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-513 |
2.23e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDheyefdNDL---TVFDWMS---QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:COG4619 81 QE------PALwggTVRDNLPfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 463 DEPTNHLDMESIESLNAALEMY----QGTLIFVSHDREFVSSLATRVIEITPERV 513
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-512 |
4.46e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.51 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW----SENAQIGYYAQ----DH 391
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepIRDAREDYRRRlaylGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 392 EYEFDNDLTVFD----WMSQWKQEGDDEQAVRSI----LGRLLfsqddiKKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:COG4133 83 ADGLKPELTVREnlrfWAALYGLRADREAIDEALeavgLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 464 EPTNHLDMESIESLNAALEMY---QGTLIFVSHDREFVssLATRVIEITPER 512
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
4.56e-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: 116.86 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDP------NERIGKLRQdQFAFEQ 78
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQ-RRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 79 Y---TVLDTVIMGhseLWevkqerdriyslPEMSEEDGYKVADlevkygemdgysaESRAGELLLGVGIpLEQHYGPMSE 155
Cdd:cd03235 82 DfpiSVRDVVLMG---LY------------GHKGLFRRLSKAD-------------KAKVDEALERVGL-SELADRQIGE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLNDRDSTMIIISHDrhfLNMVCTH 221
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHD---LGLVLEY 198
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-239 |
7.00e-30 |
|
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: 117.27 E-value: 7.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD----------PNERIGKLR 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 QDQFAFEQYTVLDtVIMGHSELWEVKqerdriyslpemSEEDGYKVADLEVKYGeMDGYsAESRAGELllgvgipleqhy 150
Cdd:COG4555 81 DERGLYDRLTVRE-NIRYFAELYGLF------------DEELKKRIEELIELLG-LEEF-LDRRVGEL------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 151 gpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:COG4555 134 ------STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
250
....*....|..
gi 490523037 228 GELrVYPGNYDE 239
Cdd:COG4555 208 GKV-VAQGSLDE 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.09e-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: 115.65 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAfeqyt 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vlDTVIMGHselwevkqeRDRIYslPEMSeedgykVAD-LEVkYGEMDGYSA-ESRAGELLLGVGIpleQHYG--PMSEV 156
Cdd:COG4133 76 --RLAYLGH---------ADGLK--PELT------VREnLRF-WAALYGLRAdREAIDEALEAVGL---AGLAdlPVRQL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFL 215
Cdd:COG4133 133 SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhlaRGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
2.71e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGKLRQdQF 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 AFEQY---TVLDTVIMG---HSELWEVKQERDRiyslpemseedgykvadlevkygemdgysaeSRAGELLLGVGIpleQ 148
Cdd:COG1121 85 EVDWDfpiTVRDVVLMGrygRRGLFRRPSRADR-------------------------------EAVDEALERVGL---E 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 149 HYG--PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDrhfLNMV---CT 220
Cdd:COG1121 131 DLAdrPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELlreLRREGKTILVVTHD---LGAVreyFD 207
|
250 260
....*....|....*....|....*...
gi 490523037 221 HMADLDYGelRVYPGNYDEYMTAATQAR 248
Cdd:COG1121 208 RVLLLNRG--LVAHGPPEEVLTPENLSR 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
4.63e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 112.34 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRqdqfafeqytvldt 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 vimghselweVKQERDRIYSLPEMSeedgykvadlevkygemdgysaesragelllgvgipleqhygpmsevaPGWKLRV 164
Cdd:cd00267 68 ----------LEELRRRIGYVPQLS------------------------------------------------GGQRQRV 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd00267 90 ALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
3.42e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.46 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD----------PNERIGKLRQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVIMghselwevkqerdriyslpemseedgykVADLevkYGeMDGYSAESRAGELL--LGVGIPLEQH 149
Cdd:COG1131 81 EPALYPDLTVRENLRF----------------------------FARL---YG-LPRKEARERIDELLelFGLTDAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 150 YGPMSevaPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLD 226
Cdd:COG1131 129 VGTLS---GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEllrELAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
....
gi 490523037 227 YGEL 230
Cdd:COG1131 206 KGRI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-505 |
3.68e-28 |
|
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: 117.98 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSAGNV--SLDPNERIGKLRQDQFAFEQYTV 81
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGYVERPSKVGEPCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 L-DTVIMGHSELW-----EVKQERDRIYSLPE----MSEEDgyKVADLEVKYGEMDGYSAES---RAGELLLGVGipLEQ 148
Cdd:TIGR03269 85 CgGTLEPEEVDFWnlsdkLRRRIRKRIAIMLQrtfaLYGDD--TVLDNVLEALEEIGYEGKEavgRAVDLIEMVQ--LSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 149 HYGPMS-EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRW----LEQTLNDRDSTMIIISHDRHFLNMVCTHMA 223
Cdd:TIGR03269 161 RITHIArDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 224 DLDYGELrVYPGNYDEymtaatqarerlladnakkkaqiadlqsFVSRFSANASKSRQATSRARQIDKIKLEEVKASsrq 303
Cdd:TIGR03269 241 WLENGEI-KEEGTPDE----------------------------VVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKR--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 304 npFIRFEQdkklfrnaleveAMTKGFDNgplfknVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------K 377
Cdd:TIGR03269 289 --YISVDR------------GVVKAVDN------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 378 WSENAQIG---------YYAQDH-EY------------------EFDNDLTVFDWMSQWKQEGDDEQAVRSILGRLlfsq 429
Cdd:TIGR03269 349 WVDMTKPGpdgrgrakrYIGILHqEYdlyphrtvldnlteaiglELPDELARMKAVITLKMVGFDEEKAEEILDKY---- 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 430 ddikkPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD-------MESIesLNAALEMYQgTLIFVSHDREFVSSLA 502
Cdd:TIGR03269 425 -----PDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSI--LKAREEMEQ-TFIIVSHDMDFVLDVC 495
|
...
gi 490523037 503 TRV 505
Cdd:TIGR03269 496 DRA 498
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
325-527 |
4.69e-28 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 117.73 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 325 MTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdhEYEFDNDLTV-- 401
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ--EPQLDPTKTVre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 ---------------FDWMS-QWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLSG 441
Cdd:TIGR03719 88 nveegvaeikdaldrFNEISaKYAEPDADFDKLAAEQAEL---QEIIDaadawdldsqleiamdalrcppwdADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 442 GEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYE 521
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
....*.
gi 490523037 522 DYLRSK 527
Cdd:TIGR03719 245 SWLEQK 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-240 |
4.82e-28 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 117.73 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpneRIGklrqdqfafeqytvlDTV 85
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------EIG---------------ETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHselweVKQERDRIyslpemseeDGYKVADLEVKYG----EMDGYSAESRAGELLLGVGIPLEQHYgpMSEVAPGWK 161
Cdd:TIGR03719 386 KLAY-----VDQSRDAL---------DPNKTVWEEISGGldiiKLGKREIPSRAYVGRFNFKGSDQQKK--VGQLSGGER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMadLDY-GELRV--YPGNYD 238
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI--LAFeGDSHVewFEGNFS 527
|
..
gi 490523037 239 EY 240
Cdd:TIGR03719 528 EY 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
328-527 |
1.05e-27 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 117.36 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 328 GFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQD---HEYEfdndlTVFDW 404
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDpprNVEG-----TVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 405 MSqwkqEGDDEQA-----------------VRSILGRLLFSQDDIK-----------------------KPAKVLSGGEK 444
Cdd:PRK11147 87 VA----EGIEEQAeylkryhdishlvetdpSEKNLNELAKLQEQLDhhnlwqlenrinevlaqlgldpdAALSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 445 GRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYL 524
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
...
gi 490523037 525 RSK 527
Cdd:PRK11147 243 LEK 245
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
335-467 |
1.50e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 107.73 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 335 FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDHeyEFDNDLTVFD 403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 404 ------WMSQWKQEGDDEQA--VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTN 467
Cdd:pfam00005 79 nlrlglLLKGLSKREKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-508 |
3.64e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 107.48 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ----IGYYAQ 389
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdiKKEPEEvkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 dhEYEFDNDLTVFDWMSqwkqegddeqavrsilgrllfsqddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHL 469
Cdd:cd03230 81 --EPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490523037 470 DMESIESLNAALEMY---QGTLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03230 127 DPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAIL 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-527 |
6.81e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 111.36 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQdhEYEFDNDLTV----------- 401
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ--EPQLDPEKTVrenveegvaev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 ------FDWMS-QWKQEGDDEQAVRSILGRLlfsQDDIK------------------------KPAKVLSGGEKGRMLFG 450
Cdd:PRK11819 99 kaaldrFNEIYaAYAEPDADFDALAAEQGEL---QEIIDaadawdldsqleiamdalrcppwdAKVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 451 KLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLRSK 527
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQK 252
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
9.01e-26 |
|
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: 105.49 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD----PNERIGKLRQ----- 71
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 -----DQFAFEqyTVLDTVIMGhselwevkqerdriyslPE---MSEEDgykvadlevkygemdgysAESRAGELLLGVG 143
Cdd:COG1122 81 fqnpdDQLFAP--TVEEDVAFG-----------------PEnlgLPREE------------------IRERVEEALELVG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 144 IpleQHYGpmsEVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFL 215
Cdd:COG1122 124 L---EHLA---DRPPhelsgGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELlkrLNKEGKTVIIVTHDLDLV 197
|
250
....*....|....*
gi 490523037 216 NMVCTHMADLDYGEL 230
Cdd:COG1122 198 AELADRVIVLDDGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-506 |
1.26e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 105.15 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ----IGYYAQ 389
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEvrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHEyeFDNDLTVFDWMSQWKQ-----EGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:COG1131 81 EPA--LYPDLTVRENLRFFARlyglpRKEARERIDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 464 EPTNHLDMESIESLNAALEMY--QGTLIFVS-HDREFVSSLATRVI 506
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-506 |
1.79e-25 |
|
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: 104.94 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE----------NAQIGYYAQ 389
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkepreaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHE-YEFdndLTVFDWM----SQWKQEGDD-EQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:COG4555 82 ERGlYDR---LTVRENIryfaELYGLFDEElKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 464 EPTNHLDMESIESLNAALEMY--QG-TLIFVSHDREFVSSLATRVI 506
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALkkEGkTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
2.63e-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: 103.70 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAFEQYTVL---DTVIMG 88
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELRRKVGLVFqnpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 HSelwevkqerdriyslpemseedgykVADlEVKYG-EMDGYSAE---SRAGELLLGVGI-PLEQHygPMSEVAPGWKLR 163
Cdd:cd03225 91 PT-------------------------VEE-EVAFGlENLGLPEEeieERVEEALELVGLeGLRDR--SPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
333-508 |
3.71e-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: 102.93 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYAQDHEYEFDNDlTV 401
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLVFQNPDDQFFGP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FD----WMSQWKQEGDD-EQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRM-LFGKLMMQkPNILVMDEPTNHLDMESIE 475
Cdd:cd03225 94 EEevafGLENLGLPEEEiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVaIAGVLAMD-PDILLLDEPTAGLDPAGRR 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 490523037 476 SLNAALEMYQG---TLIFVSHDREFVSSLATRVIEI 508
Cdd:cd03225 172 ELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
223-309 |
6.37e-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: 98.41 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 223 ADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDkiKLEEVKASSR 302
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALE--KMERIEKPER 78
|
....*..
gi 490523037 303 QNPFIRF 309
Cdd:pfam12848 79 DKPKLRF 85
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
334-528 |
7.44e-25 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 108.72 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 334 LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDH--------EYEFDNDLTVFDWM 405
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpalpqpalEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 406 SQWKQ--EGDDEQAVRSILGRLL-------------------FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDE 464
Cdd:PRK10636 96 AQLHDanERNDGHAIATIHGKLDaidawtirsraasllhglgFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 465 PTNHLDMESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLRSKG 528
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA 239
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-508 |
1.13e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 100.01 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 321 EVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSenaqigyyaqdheyefDNDLT 400
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID----------------GKDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VFDWmsqwkqegddeQAVRSILGRLlfSQddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAA 480
Cdd:cd00267 65 KLPL-----------EELRRRIGYV--PQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 481 L-EMYQG--TLIFVSHDREFVSSLATRVIEI 508
Cdd:cd00267 123 LrELAEEgrTVIIVTHDPELAELAADRVIVL 153
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-241 |
1.25e-24 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 108.00 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV--------SLDPNE---RIGKLRQ 71
Cdd:COG2274 477 ENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQyTVLDTVIMGH-----SELWEVKQE---RDRIYSLPemseeDGYkvaDLEVkyGEMdgysaesraGELLLGvg 143
Cdd:COG2274 557 DVFLFSG-TIRENITLGDpdatdEEIIEAARLaglHDFIEALP-----MGY---DTVV--GEG---------GSNLSG-- 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 144 ipleqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNmvcth 221
Cdd:COG2274 615 ---------------GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIR----- 674
|
250 260
....*....|....*....|....
gi 490523037 222 MAD----LDYGELrVYPGNYDEYM 241
Cdd:COG2274 675 LADriivLDKGRI-VEDGTHEELL 697
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-230 |
2.64e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 101.36 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFA------ 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEIArlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 -------FEQYTVLDTVIMGHSElwevkQERDRIYSLPEMSEEDgykvadlevkygemdgySAESRAGELLLGVGIpleQ 148
Cdd:cd03219 80 tfqiprlFPELTVLENVMVAAQA-----RTGSGLLLARARREER-----------------EARERAEELLERVGL---A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 149 HYG--PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQtLNDRDSTMIIISHDRHFLNMVCTHM 222
Cdd:cd03219 135 DLAdrPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPeeteELAELIRE-LRERGITVLLVEHDMDVVMSLADRV 213
|
....*...
gi 490523037 223 ADLDYGEL 230
Cdd:cd03219 214 TVLDQGRV 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-259 |
3.61e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 105.97 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpneRIGklrqdqfafeqytvlDTV 85
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI------KIG---------------ETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHselweVKQERDRIysLPEMS--EE--DGY---KVADLEVKygemdgysaeSRAgelllgvgipleqhY-------G 151
Cdd:PRK11819 388 KLAY-----VDQSRDAL--DPNKTvwEEisGGLdiiKVGNREIP----------SRA--------------YvgrfnfkG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 P-----MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMadLD 226
Cdd:PRK11819 437 GdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LA 514
|
250 260 270
....*....|....*....|....*....|....*.
gi 490523037 227 Y-GELRV--YPGNYDEYmtaATQARERLLADNAKKK 259
Cdd:PRK11819 515 FeGDSQVewFEGNFQEY---EEDKKRRLGADAARPH 547
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
3.78e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 328 GFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFDNDLTVFDW--M 405
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLvaM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 406 SQWKQEG-------DDEQAVRSILGRLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLN 478
Cdd:NF040873 81 GRWARRGlwrrltrDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 479 AAL--EMYQG-TLIFVSHDREFVSSlATRVI 506
Cdd:NF040873 160 ALLaeEHARGaTVVVVTHDLELVRR-ADPCV 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
321-506 |
4.95e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.05 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 321 EVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWS--ENAQ-IGYYAQ 389
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSpkELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 dheyefdndltvfdWMSQWKqegddeqaVRSILGRLLFSqddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHL 469
Cdd:cd03214 81 --------------ALELLG--------LAHLADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490523037 470 D-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:cd03214 129 DiahqielLELLRRLARERGK---TVVMVLHDLNLAARYADRVI 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-210 |
6.74e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNvsldpnerigklrqdqfafeQYTVLDTV 85
Cdd:COG1119 8 NVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN--------------------DVRLFGER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 iMGHSELWEVKQerdRI-YSLPEMSE--------ED-----GYKVADLEVKYGEMDgysaESRAGELL--LGVGIPLEQH 149
Cdd:COG1119 68 -RGGEDVWELRK---RIgLVSPALQLrfprdetvLDvvlsgFFDSIGLYREPTDEQ----RERARELLelLGLAHLADRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 150 YGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISH 210
Cdd:COG1119 140 FGTLSQ---GEQRRVLIARALVKDPELLILDEPTAGLDLgareLLLALLDKLAAEGAPTLVLVTH 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-230 |
7.52e-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: 100.50 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGS-KPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFA---- 75
Cdd:COG0411 4 LLEVRGLTKRFGGlVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD-GRDITGLPPHRIArlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 ---------FEQYTVLDTVIMGHselwevkQERDRIYSLPEMSEEDGYKVADLEvkygemdgysAESRAGELLLGVGIpL 146
Cdd:COG0411 82 artfqnprlFPELTVLENVLVAA-------HARLGRGLLAALLRLPRARREERE----------ARERAEELLERVGL-A 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEP--------TNNLdIDTIRWLEQtlnDRDSTMIIISHDRHFLNMV 218
Cdd:COG0411 144 DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPaaglnpeeTEEL-AELIRRLRD---ERGITILLIEHDMDLVMGL 219
|
250
....*....|..
gi 490523037 219 CTHMADLDYGEL 230
Cdd:COG0411 220 ADRIVVLDFGRV 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-506 |
7.61e-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: 7.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--------AQIGYYAQDHEYEFDNDlTV 401
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDVDYQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FDWMS-QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAA 480
Cdd:cd03226 90 REELLlGLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180
....*....|....*....|....*....
gi 490523037 481 LE--MYQGTLIFV-SHDREFVSSLATRVI 506
Cdd:cd03226 169 IRelAAQGKAVIViTHDYEFLAKVCDRVL 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-506 |
2.23e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA---QIGY 386
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 YAQDHEyefdndltvfdwmsqwkqegddeqavrsilgrlLFS---QDDIkkpakvLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:cd03246 81 LPQDDE---------------------------------LFSgsiAENI------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 464 EPTNHLDMESIESLNAA---LEMYQGTLIFVSHDREFVSSlATRVI 506
Cdd:cd03246 122 EPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLAS-ADRIL 166
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-213 |
3.09e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 11 FGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQ-----DQFAFeqyTVLDTV 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPL---TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMG---HSELWEVKQERDRIySLPEMSEEDGykVADLEVKygemdgysaesragelllgvgipleqhygPMSEVAPGWKL 162
Cdd:NF040873 79 AMGrwaRRGLWRRLTRDDRA-AVDDALERVG--LADLAGR-----------------------------QLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRH 213
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAeehARGATVVVVTHDLE 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
3.84e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 97.56 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGS----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNERIGKLR 70
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 QDQ--FAFEQY------TVLDTVimghselwevkqerdriySLPEMseedgykvadlevkYGEMDGYSAESRAGELLLGV 142
Cdd:cd03255 81 RRHigFVFQSFnllpdlTALENV------------------ELPLL--------------LAGVPKKERRERAEELLERV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 143 GIPLEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDR 212
Cdd:cd03255 129 GLGDRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-231 |
3.84e-23 |
|
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: 97.29 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD---------PNERIGKLRQD 72
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksyqknieALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 QFAFEQYTVLDTVIMGHSELWEVKQERDRIYSLPEMSEEDGYKVAdlevkygemdGYSaesragellLGvgipleqhygp 152
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVK----------GFS---------LG----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 153 MsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDRHFLNMVCTHMADLDYGE 229
Cdd:cd03268 131 M-------KQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
..
gi 490523037 230 LR 231
Cdd:cd03268 204 LI 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-506 |
3.89e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 102.96 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN--ERIGKLR----QDQFAfeqytvldtvimghselwEVKQERDRIYS 104
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdEVLKRFRgtelQNYFK------------------KLYNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 105 LPEMSEE-----DGyKVADLEVKYGEmdgysaESRAGELL--LGVGIPLEQHYGPMSevapGWKL-RVLLAQALFSNPDI 176
Cdd:PRK13409 165 KPQYVDLipkvfKG-KVRELLKKVDE------RGKLDEVVerLGLENILDRDISELS----GGELqRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 177 LLLDEPTNNLDI-------DTIRWLEQtlndrDSTMIIISHDRHFLNMvcthMADL---DYGElrvyPGNY--------- 237
Cdd:PRK13409 234 YFFDEPTSYLDIrqrlnvaRLIRELAE-----GKYVLVVEHDLAVLDY----LADNvhiAYGE----PGAYgvvskpkgv 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 238 ----DEYMtaatqaRERLLADNAkkkaqiadlqsfvsRFsanasksrqatsrarqidkikleevkassRQNPfIRFE--- 310
Cdd:PRK13409 301 rvgiNEYL------KGYLPEENM--------------RI-----------------------------RPEP-IEFEerp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 311 -QDKKLFRNALEVEAMTKGFDNgplFKnvgllLEV-------GEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENa 382
Cdd:PRK13409 331 pRDESERETLVEYPDLTKKLGD---FS-----LEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 383 qIGYYAQdheY-EFDNDLTVFDWMSQWKQEGDD-----EQAVRSILGRLLfsqddiKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK13409 402 -ISYKPQ---YiKPDYDGTVEDLLRSITDDLGSsyyksEIIKPLQLERLL------DKNVKDLSGGELQRVAIAACLSRD 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 457 PNILVMDEPTNHLDMEsiESLNAA------LEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:PRK13409 472 ADLYLLDEPSAHLDVE--QRLAVAkairriAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-526 |
9.12e-23 |
|
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: 96.80 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQIGYYAQDHEYE 394
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 --------FDnDLTVFD----WMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:cd03261 81 mlfqsgalFD-SLTVFEnvafPLREHTRLSEEEirEIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 461 VMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVVdFSGGYEDYLRS 526
Cdd:cd03261 159 LYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEELRAS 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
316-529 |
3.33e-22 |
|
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: 100.68 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 316 FRNALEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN-----------A 382
Cdd:COG2274 470 LKGDIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 383 QIGYYAQdheyefDNDL---TVFDWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGRML 448
Cdd:COG2274 550 QIGVVLQ------DVFLfsgTIRENITLGDPDATDEEIIEAA--RLAGLHDFIEAlPmgydtvvgegGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 449 FGKLMMQKPNILVMDEPTNHLDMESIESLNAAL-EMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfSGGYEDYLRS 526
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLrRLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEELLAR 699
|
...
gi 490523037 527 KGI 529
Cdd:COG2274 700 KGL 702
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-508 |
3.90e-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: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSE------- 380
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 381 NAQIGYYAQDHEYEfdNDLTVFD-----WMSQWKQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMM 454
Cdd:cd03255 81 RRHIGFVFQSFNLL--PDLTALEnvelpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 455 QKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVsSLATRVIEI 508
Cdd:cd03255 157 NDPKIILADEPTGNLDsetgkevMELLRELNKEAGT---TIVVVTHDPELA-EYADRIIEL 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-230 |
1.05e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 93.34 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE---RIGKLRQDQF 74
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsampPPEwrrQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 AFEQyTVLDtvimgHseLWEVKQERDRIYSlpemseedgykvadlevkygemdgysaESRAGELLLGVGIP---LEQhyg 151
Cdd:COG4619 85 LWGG-TVRD-----N--LPFPFQLRERKFD---------------------------RERALELLERLGLPpdiLDK--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:COG4619 127 PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
...
gi 490523037 228 GEL 230
Cdd:COG4619 207 GRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-239 |
1.27e-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: 93.72 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQ---------FA 75
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAElyrlrrrmgML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQ------YTVLDTVIMG---HSELwevkqerdriySLPEMSEedgykvadlevkygemdgysaesRAGELLLGVGIPL 146
Cdd:cd03261 83 FQSgalfdsLTVFENVAFPlreHTRL-----------SEEEIRE-----------------------IVLEKLEAVGLRG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMIIISHDRHFLNMVC 219
Cdd:cd03261 129 AEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIA 204
|
250 260
....*....|....*....|
gi 490523037 220 THMADLDYGELrVYPGNYDE 239
Cdd:cd03261 205 DRIAVLYDGKI-VAEGTPEE 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-506 |
1.44e-21 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 91.86 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------------ENAQIGY 386
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 YAQDHeyefdndlTVFDWMSqwkqegddeqaVRSILgrllfsqddikkpAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:cd03229 81 VFQDF--------ALFPHLT-----------VLENI-------------ALGLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490523037 467 NHLDMES-------IESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:cd03229 129 SALDPITrrevralLKSLQAQLGI---TVVLVTHDLDEAARLADRVV 172
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-184 |
1.85e-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: 90.78 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-----------PNERIGKLRQDQFAFEQYTVLDTV 85
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHselwevkqerdRIYSLpeMSEEDGYKVADLEVKYGEMDGysAESRAGElllgvgipleqhygPMSEVAPGWKLRVL 165
Cdd:pfam00005 81 RLGL-----------LLKGL--SKREKDARAEEALEKLGLGDL--ADRPVGE--------------RPGTLSGGQRQRVA 131
|
170
....*....|....*....
gi 490523037 166 LAQALFSNPDILLLDEPTN 184
Cdd:pfam00005 132 IARALLTKPKLLLLDEPTA 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-506 |
2.93e-21 |
|
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: 97.16 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN-ERI-----GKLRQDQFafeqYTVLDTVImghselwEVKQERDRIYS 104
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPSwDEVlkrfrGTELQDYF----KKLANGEI-------KVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 105 LPEMSeeDGyKVADLEVKYGEmdgysaESRAGEL--LLGVGIPLEQHYGPMSevapGWKL-RVLLAQALFSNPDILLLDE 181
Cdd:COG1245 172 IPKVF--KG-TVRELLEKVDE------RGKLDELaeKLGLENILDRDISELS----GGELqRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 182 PTNNLDI-------DTIRwleqTLNDRDSTMIIISHDRHFLNMvcthMAD---LDYGElrvyPGNYDeymtAATQARERL 251
Cdd:COG1245 239 PSSYLDIyqrlnvaRLIR----ELAEEGKYVLVVEHDLAILDY----LADyvhILYGE----PGVYG----VVSKPKSVR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 252 LADNAkkkaqiadlqsFVSRFsanasksrqatsrarqidkIKLEEVKAssRQNPfIRFE----QDKKLFRNALEVEAMTK 327
Cdd:COG1245 303 VGINQ-----------YLDGY-------------------LPEENVRI--RDEP-IEFEvhapRREKEEETLVEYPDLTK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 328 GFDNgplFKnvgllLEV-------GEKLAILGANGVGKSTMLKTLVGELQPDNGTVkwSENAQIGYYAQdheY-EFDNDL 399
Cdd:COG1245 350 SYGG---FS-----LEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQ---YiSPDYDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMEsiESLNA 479
Cdd:COG1245 417 TVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAV 494
|
490 500 510
....*....|....*....|....*....|...
gi 490523037 480 A------LEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:COG1245 495 AkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
2.98e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 92.94 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD----PNERIGKLRQD 72
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 -QFAFEQ-YTVLD---TVimghselwevkqerDRIYSLPemseedgykvadLEVkYGEMDgysAESRAGELLLGVGIPLE 147
Cdd:COG1124 81 vQMVFQDpYASLHprhTV--------------DRILAEP------------LRI-HGLPD---REERIAELLEQVGLPPS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 148 QHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHflnmVCTHMA 223
Cdd:COG1124 131 FLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHDLA----VVAHLC 206
|
250
....*....|.
gi 490523037 224 D----LDYGEL 230
Cdd:COG1124 207 DrvavMQNGRI 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-230 |
4.85e-21 |
|
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: 90.57 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAfEQYTVLDT 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-GKDLASLSPKELA-RKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VImghsELWEVKQERDRIYSlpEMSeedgykvadlevkygemdgysaesrAGELllgvgipleQhygpmsevapgwklRV 164
Cdd:cd03214 81 AL----ELLGLAHLADRPFN--ELS-------------------------GGER---------Q--------------RV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNMV---CTHMADLDYGEL 230
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNLAaryADRVILLKDGRI 176
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
319-528 |
5.10e-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: 96.37 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIG 385
Cdd:COG4987 333 SLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdLDEDDlrrRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 386 YYAQDHeYEFD----NDLTVFdwmsqwKQEGDDEQAVRSI----LGRLLFSQddikkPAKV----------LSGGEKGRM 447
Cdd:COG4987 413 VVPQRP-HLFDttlrENLRLA------RPDATDEELWAALervgLGDWLAAL-----PDGLdtwlgeggrrLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 448 LFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL-EMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfSGGYEDYLR 525
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLlEALAGrTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEELLA 558
|
...
gi 490523037 526 SKG 528
Cdd:COG4987 559 QNG 561
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-514 |
9.53e-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: 91.48 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--------------AQI 384
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 385 GYYAQDHE-----YEFDNDLT-VFDWMSQWKQ-----EGDDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLM 453
Cdd:cd03256 81 GMIFQQFNlierlSVLENVLSgRLGRRSTWRSlfglfPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 454 MQKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03256 160 MQQPKLILADEPVASLDpassrqvMDLLKRINREEGI---TVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-506 |
1.19e-20 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 90.85 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENA-----QIGYY 387
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYEFDNDlTVFDWMS----QWKQEGDD-EQAVRSILGRLlfsqdDI----KKPAKVLSGGEKGRM-LFGKLMMQkP 457
Cdd:COG1122 81 FQNPDDQLFAP-TVEEDVAfgpeNLGLPREEiRERVEEALELV-----GLehlaDRPPHELSGGQKQRVaIAGVLAME-P 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 458 NILVMDEPTNHLDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVI 506
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-212 |
1.43e-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: 90.27 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQDQFAF 76
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvpPERRnIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 EQYTVLDTVIMGHSELWEVKQERDRiyslpemseedgykvadlevkygemdgysaesRAGELLLGVGIPLEQHYGPmSEV 156
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPKAEIRA--------------------------------RVRELLELVGLEGLLNRYP-HEL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDtIRW-----LEQTLNDRDSTMIIISHDR 212
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAK-LREelreeLKELQRELGITTIYVTHDQ 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
274-494 |
1.93e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.35 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 274 ANASKSRQATSRARqidkikLEEVKASSRQNPFIRFEQDKKLFRNA--LEVEAMTKGFDNGP-LFKNVGLLLEVGEKLAI 350
Cdd:TIGR02868 293 AAQQLTRVRAAAER------IVEVLDAAGPVAEGSAPAAGAVGLGKptLELRDLSAGYPGAPpVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 351 LGANGVGKSTMLKTLVGELQPDNGTV--------KWSEN---AQIGYYAQD-HEYefdnDLTVFDWMSQWKQEGDDEQAV 418
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVCAQDaHLF----DTTVRENLRLARPDATDEELW 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 419 RSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES----IESLNAALEMYq 485
Cdd:TIGR02868 443 AALervgLADWLRALPDgldtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSGR- 521
|
....*....
gi 490523037 486 gTLIFVSHD 494
Cdd:TIGR02868 522 -TVVLITHH 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-235 |
4.20e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.31 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVS---LDPNER-IGKLRQdqfafeqytvlDTVIMG 88
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvagLVPWKRrKKFLRR-----------IGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 H-SELWevkqerdriYSLPEMseeDGYKVadLEVKYGeMDGYSAESRAGEL--LLGVGIPLEQhygPMSEVAPGWKLRVL 165
Cdd:cd03267 102 QkTQLW---------WDLPVI---DSFYL--LAAIYD-LPPARFKKRLDELseLLDLEELLDT---PVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 166 LAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLN-DRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPG 235
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
4.95e-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: 88.73 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQ----------IGYYAQ 389
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDvtgvpperrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHeyefdndlTVFDWMS-----------QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:cd03259 80 DY--------ALFPHLTvaeniafglklRGVPKAEIRARVRELLELVGLEGLLNRYPHE-LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 459 ILVMDEPTNHLDMESIESLNAALEMYQG----TLIFVSHDREFVSSLATRVI 506
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIA 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
7.61e-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: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAF--- 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQDLSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 ------------EQYTVLDTV-----IMGHSElwevKQERDRIyslPEMSEedgyKVaDLEVKygemdgysAESRAGELL 139
Cdd:COG2884 80 rigvvfqdfrllPDRTVYENValplrVTGKSR----KEIRRRV---REVLD----LV-GLSDK--------AKALPHELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 140 LGvgiplEQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLNDRDSTMIIISHDRHFL 215
Cdd:COG2884 140 GG-----EQQ-------------RVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELV 200
|
.
gi 490523037 216 N 216
Cdd:COG2884 201 D 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
320-516 |
1.59e-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: 87.78 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLfKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYAQD 390
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 HeYEFDNdLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEP 465
Cdd:cd03299 80 Y-ALFPH-MTVYKNIAyglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 466 TNHLDMESIESLNAAL----EMYQGTLIFVSHDREFVSSLATRVIEITPERVVDF 516
Cdd:cd03299 157 FSALDVRTKEKLREELkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.66e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.41 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDISSLSERElar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 74 -------FAFEQY------TVLDTVIMGHselwevkqerdriyslpemseedgykvadlevKYGEMDGYSAESRAGELLL 140
Cdd:COG1136 83 lrrrhigFVFQFFnllpelTALENVALPL--------------------------------LLAGVSRKERRERARELLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 141 GVGIP-LEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFL 215
Cdd:COG1136 131 RVGLGdRLDHR-P-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELA 208
|
..
gi 490523037 216 NM 217
Cdd:COG1136 209 AR 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-514 |
1.96e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.83 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQP-DNGTVKW------SEN-----AQIGYYAQDHEYEFDNDLT 400
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLfgerrgGEDvwelrKRIGLVSPALQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 V--------FDWMSQWKQEGD-DEQAVRSILGRL-LfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD 470
Cdd:COG1119 97 VldvvlsgfFDSIGLYREPTDeQRERARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490523037 471 MESIESLNAALE--MYQG--TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:COG1119 175 LGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
2.23e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.87 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE---RIGKLRQDQFAFeqY-TVLDTV 85
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldPADlrrNIGYVPQDVTLF--YgTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHselwevkqerdriyslPEMSEEDGYKVADLevkyGEMDGYSAESRAG-ELLLGvgiplEQHYGpmseVAPGWKLRV 164
Cdd:cd03245 99 TLGA----------------PLADDERILRAAEL----AGVTDFVNKHPNGlDLQIG-----ERGRG----LSGGQRQAV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMV 218
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLLDLV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
319-508 |
2.50e-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: 87.55 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQ 383
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrrkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 IGYYAQDHEYEFDNDLTVFDWMSqwkqE-------GDDEQAVRSIL------GRLLFsqddiKKPAKvLSGGEKGRMLFG 450
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILA----EplrihglPDREERIAELLeqvglpPSFLD-----RYPHQ-LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 451 KLMMQKPNILVMDEPTNHLDM----ESIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
2.85e-19 |
|
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: 86.53 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNERIGKLRQD 72
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgedvnrlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 -QFAFEQYTVLdtvimghselwevkqerdriyslPEMSEEDGYKVAdLEVKYGEMDGYsaESRAGELLLGVGIPLEQHYG 151
Cdd:TIGR02673 81 iGVVFQDFRLL-----------------------PDRTVYENVALP-LEVRGKKEREI--QRRVGAALRQVGLEHKADAF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 152 PMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHDRH 213
Cdd:TIGR02673 135 PE-QLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLserILDLLKRLNKRGTTVIVATHDLS 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-231 |
2.89e-19 |
|
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: 86.40 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGS--KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL---DPNERIGKLRQD---- 72
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngySIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 -QF--AFEQYTVLDtvimgHSELWEvkqerdRIYSLPemsEEDGYKVADLEVKYGEMDGYsAESRAGELllgvgipleqh 149
Cdd:cd03263 81 pQFdaLFDELTVRE-----HLRFYA------RLKGLP---KSEIKEEVELLLRVLGLTDK-ANKRARTL----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 150 ygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03263 135 -------SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEvrKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
....
gi 490523037 228 GELR 231
Cdd:cd03263 208 GKLR 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-231 |
2.97e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 86.09 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGnRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNE---RIGKLRQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqPQKlrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVimghselwevkqerDRIYSLPEMSEEDgykvadlevkygemdgysAESRAGELLLGVGipLEQHYG 151
Cdd:cd03264 80 EFGVYPNFTVREFL--------------DYIAWLKGIPSKE------------------VKARVDEVLELVN--LGDRAK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 -PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-DTIRW---LEQTLNDRdsTMIIISHDRHFLNMVCTHMADLD 226
Cdd:cd03264 126 kKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeERIRFrnlLSELGEDR--IVILSTHIVEDVESLCNQVAVLN 203
|
....*
gi 490523037 227 YGELR 231
Cdd:cd03264 204 KGKLV 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-514 |
4.24e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.10 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE-----------NAQIGYYAQDHEYEF----DNdLT 400
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRNIGYVPQDVTLFYgtlrDN-IT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VFDwmsqwkQEGDDEQAVRS--ILGRLLFSQDD-------IKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM 471
Cdd:cd03245 100 LGA------PLADDERILRAaeLAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490523037 472 ESIESLNAALEMYQG--TLIFVSHdREFVSSLATRVIEITPERVV 514
Cdd:cd03245 174 NSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRIV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
4.37e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE---RIGKL 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgrpladwsPAElarRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQD---QFAFeqyTVLDTVIMGHSELWEVKQERDRiysLPE--MSEEDgykVADLEVKYgemdgYSAESrAGElllgvgi 144
Cdd:PRK13548 82 PQHsslSFPF---TVEEVVAMGRAPHGLSRAEDDA---LVAaaLAQVD---LAHLAGRD-----YPQLS-GGE------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 145 pleqhygpmsevapgwKLRVLLAQAL--FSNPD----ILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhf 214
Cdd:PRK13548 140 ----------------QQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD--- 200
|
..
gi 490523037 215 LN 216
Cdd:PRK13548 201 LN 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-518 |
4.58e-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: 85.71 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGeKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----SENAQ-----IGYYAQ 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvLKQPQklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DheYEFDNDLTVFD------WMSQWKQeGDDEQAVRSILGRL-LFsqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:cd03264 80 E--FGVYPNFTVREfldyiaWLKGIPS-KEVKARVDEVLELVnLG--DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 463 DEPTNHLDMES-IESLNAALEMYQGTLIFVS-HDREFVSSLATRVIEITPERVVdFSG 518
Cdd:cd03264 155 DEPTAGLDPEErIRFRNLLSELGEDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
345-514 |
4.72e-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: 85.81 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQ----------IGYYAQdhEYEFDNDLTVFD---WMS 406
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvLFDSRKkinlppqqrkIGLVFQ--QYALFPHLNVREnlaFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 407 QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES----IESLNAALE 482
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 483 MYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-508 |
5.14e-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: 84.36 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaqdheyefdN 397
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTVFDWmsqwkqegdDEQAVRSILGRL-----LFSqDDIKKpaKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDME 472
Cdd:cd03228 63 GVDLRDL---------DLESLRKNIAYVpqdpfLFS-GTIRE--NILSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 490523037 473 SIESLNAALEMYQG--TLIFVSHDREFVsSLATRVIEI 508
Cdd:cd03228 131 TEALILEALRALAKgkTVIVIAHRLSTI-RDADRIIVL 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-250 |
6.81e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMK-------ILGGDLQPSAGNVsLDPNERIGKLRQD- 72
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKV-NDPKVDERLIRQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 -----QF-AFEQYTVLDTVIMGHselwevKQERDriyslpeMSEEDgykvadlevkygemdgysAESRAGELLLGVGIPL 146
Cdd:PRK09493 80 gmvfqQFyLFPHLTALENVMFGP------LRVRG-------ASKEE------------------AEKQARELLAKVGLAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID---TIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMA 223
Cdd:PRK09493 129 RAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
250 260
....*....|....*....|....*..
gi 490523037 224 DLDYGELRVyPGNYDEYMTAATQARER 250
Cdd:PRK09493 208 FIDKGRIAE-DGDPQVLIKNPPSQRLQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
7.51e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 85.80 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQD-------- 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKelyelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 -----QFA--FEQYTVLDTVIMGhseLWEvkqerdriysLPEMSEEDgykvadlevkygemdgysAESRAGELLLGVGIP 145
Cdd:COG1127 84 igmlfQGGalFDSLTVFENVAFP---LRE----------HTDLSEAE------------------IRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 146 -LEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-------IRwleqTLNDR-DSTMIIISHDRHFLN 216
Cdd:COG1127 133 gAADKM-P-SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITsavidelIR----ELRDElGLTSVVVTHDLDSAF 206
|
250 260
....*....|....*....|...
gi 490523037 217 MVCTHMADLDYGELRVYpGNYDE 239
Cdd:COG1127 207 AIADRVAVLADGKIIAE-GTPEE 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-229 |
8.65e-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: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGKLRQD-QFAFE 77
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdLEDELPPLRRRiGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 78 QY------TVLDTVIMGHSelwevkqerdriyslpemseedgykvadlevkygemdgysaesragelllgvgipleqhyG 151
Cdd:cd03229 84 DFalfphlTVLENIALGLS------------------------------------------------------------G 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 pmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDS-TMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03229 104 -------GQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
..
gi 490523037 228 GE 229
Cdd:cd03229 177 GK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-506 |
1.10e-18 |
|
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: 83.25 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYEFDNDL 399
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----------DGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 tvfdwmsqwkqegddeQAVRsiLGRLLFSQddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNA 479
Cdd:cd03216 71 ----------------DARR--AGIAMVYQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|
gi 490523037 480 ALEMY--QG-TLIFVSHDREFVSSLATRVI 506
Cdd:cd03216 124 VIRRLraQGvAVIFISHRLDEVFEIADRVT 153
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-514 |
1.13e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 88.81 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGeLQPDNGTV------------KWSEN--- 381
Cdd:COG1123 4 LLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllELSEAlrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 382 AQIGYYAQDHEYEFdNDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKV----LSGGEKGRMLFGKLMMQKP 457
Cdd:COG1123 83 RRIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRyphqLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 458 NILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 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 |
1.16e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 84.94 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE------------ 64
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 65 --RIGKLRQdQFA-FEQYTVLDTVimghselwevkqerdriySLPemseedgykvadLEVkyGEMDGYSAESRAGELLLG 141
Cdd:cd03258 81 rrRIGMIFQ-HFNlLSSRTVFENV------------------ALP------------LEI--AGVPKAEIEERVLELLEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 VGIPLEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDR-DSTMIIISHDRHFLNM 217
Cdd:cd03258 128 VGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRElGLTIVLITHEMEVVKR 206
|
250
....*....|...
gi 490523037 218 VCTHMADLDYGEL 230
Cdd:cd03258 207 ICDRVAVMEKGEV 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
1.24e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 83.42 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFafeqy 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNEL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 tvldtvimghselwevkqeRDRIYSLPEmseedgykvaDLEVkygeMDGysaeSRAGELLLGvgipleqhygpmsevapG 159
Cdd:cd03246 75 -------------------GDHVGYLPQ----------DDEL----FSG----SIAENILSG-----------------G 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 160 WKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMV 218
Cdd:cd03246 101 QRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAHRPETLASA 162
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-214 |
1.29e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 84.50 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGKLRQD-QFAFEQ 78
Cdd:cd03262 5 NLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltdDKKNINELRQKvGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 79 Y------TVLDTVIMGhseLWEVKQerdriyslpeMSEEDgykvadlevkygemdgysAESRAGELLLGVGIPLEQHYGP 152
Cdd:cd03262 85 FnlfphlTVLENITLA---PIKVKG----------MSKAE------------------AEERALELLEKVGLADKADAYP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 153 mSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHF 214
Cdd:cd03262 134 -AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaeEGMTMVVVTHEMGF 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
1.41e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 84.45 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSK----PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGklrq 71
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 dqFAFEQY------TVLDTVIMGhselwevkqerdriyslpemseedgykvadLEVKygEMDGYSAESRAGELLLGVGIP 145
Cdd:cd03293 77 --YVFQQDallpwlTVLDNVALG------------------------------LELQ--GVPKAEARERAEELLELVGLS 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 146 -LEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03293 123 gFENAY-P-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTreqlQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-514 |
5.06e-18 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 83.26 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFdnGPL--FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWS---------- 379
Cdd:cd03219 1 LEVRGLTKRF--GGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPpheiarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 380 ---------------ENAQIGYYAQDHEYefdndltvFDWMSQWKQEGDDEQAVRSILGRL-LfsQDDIKKPAKVLSGGE 443
Cdd:cd03219 79 rtfqiprlfpeltvlENVMVAAQARTGSG--------LLLARARREEREARERAEELLERVgL--ADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 444 KGRMLFGKLMMQKPNILVMDEPT---NHLD----MESIESLNAalemyQG-TLIFVSHDREFVSSLATRVI--------- 506
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAaglNPEEteelAELIRELRE-----RGiTVLLVEHDMDVVMSLADRVTvldqgrvia 223
|
....*...
gi 490523037 507 EITPERVV 514
Cdd:cd03219 224 EGTPDEVR 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
335-506 |
7.18e-18 |
|
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: 82.58 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 335 FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQIGyyaqdheyeFDNDLTVFD----- 403
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvsSLLGLGGG---------FNPELTGREniyln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 404 --WMSQWKQEGDdeQAVRSILGrllFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD---ME-SIE 475
Cdd:cd03220 109 grLLGLSRKEID--EKIDEIIE---FSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafQEkCQR 183
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 476 SLNAALEMyQGTLIFVSHDREFVSSLATRVI 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 |
9.21e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 82.13 E-value: 9.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------KWSENAQIGYYAQ 389
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHeyefdndlTVFDWMS-----------QWKQEGDDEQAVRSILGRL-L--FSQddiKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:cd03293 81 QD--------ALLPWLTvldnvalglelQGVPKAEARERAEELLELVgLsgFEN---AYPHQ-LSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 456 KPNILVMDEPTNHLDMESIESLNAAL-EMYQG---TLIFVSHDREFVSSLATRVIEIT--PERVVD 515
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELlDIWREtgkTVLLVTHDIDEAVFLADRVVVLSarPGRIVA 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
1.01e-17 |
|
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: 80.50 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD----PNERIGKLRQdQFAF-EQYTVL--DT 84
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvdlRDLDLESLRK-NIAYvPQDPFLfsGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VimghselwevkqeRDRIYSlpemseedgykvadlevkygemdgysaesrAGElllgvgipleqhygpmsevapgwKLRV 164
Cdd:cd03228 92 I-------------RENILS------------------------------GGQ-----------------------RQRI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRH 213
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAHRLS 156
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-249 |
1.11e-17 |
|
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: 85.97 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL--------DPNE---RIGK 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdlDEDDlrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 LRQDQFAFEQyTVLDTVIMG-----HSELWEVKQE---RDRIYSLPemseeDGYkvaDLEVkyGEmdgysaesrAGELLL 140
Cdd:COG4987 414 VPQRPHLFDT-TLRENLRLArpdatDEELWAALERvglGDWLAALP-----DGL---DTWL--GE---------GGRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 141 GvGiplEQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMV 218
Cdd:COG4987 474 G-G---ERR-------------RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGRTVLLITHRLAGLERM 536
|
250 260 270
....*....|....*....|....*....|.
gi 490523037 219 cTHMADLDYGELRVyPGNYDEYMTAATQARE 249
Cdd:COG4987 537 -DRILVLEDGRIVE-QGTHEELLAQNGRYRQ 565
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-466 |
2.88e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKLRqdQFAfeqyT 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GEPV--RFR----S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLDT----VIMGHSELwevkqerdriySL-PEMSeedgykVAD------LEVKYGEMDGYSAESRAGELL--LGVGIPLE 147
Cdd:COG1129 73 PRDAqaagIAIIHQEL-----------NLvPNLS------VAEniflgrEPRRGGLIDWRAMRRRARELLarLGLDIDPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 148 QhygPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIIShdrHFLN---- 216
Cdd:COG1129 136 T---PVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTereverlFRIIR----RLKAQGVAIIYIS---HRLDevfe 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 217 ------------MVCTH-MADLDYGELrVypgnydEYMTaatqARErlLADNAKKKAQIADlqsfvsrfsanasksrqat 283
Cdd:COG1129 206 iadrvtvlrdgrLVGTGpVAELTEDEL-V------RLMV----GRE--LEDLFPKRAAAPG------------------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 284 srarqidkiklEEVkassrqnpfirfeqdkklfrnaLEVEamtkGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLK 363
Cdd:COG1129 254 -----------EVV----------------------LEVE----GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELAR 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 364 TLVGELQPDNGTVKWSE------------NAQIGYYAQDHEYE--------FDN-DLTVFDWMSQWK--QEGDDEQAVRS 420
Cdd:COG1129 297 ALFGADPADSGEIRLDGkpvrirsprdaiRAGIAYVPEDRKGEglvldlsiRENiTLASLDRLSRGGllDRRRERALAEE 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 490523037 421 ILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:COG1129 377 YIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
3.08e-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: 80.69 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSA---GNVSLD----------PNE---R 65
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGApdeGEVLLDgkdiydldvdVLElrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 66 IGKLRQDQFAFEQyTVLDTVIMG---HSELWevKQERDRIyslpemsEEDGYKVADL--EVKygemdgysaeSRAGELLL 140
Cdd:cd03260 83 VGMVFQKPNPFPG-SIYDNVAYGlrlHGIKL--KEELDER-------VEEALRKAALwdEVK----------DRLHALGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 141 GVGiplEQhygpmsevapgwkLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN--DRDSTMIIISHD 211
Cdd:cd03260 143 SGG---QQ-------------QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-511 |
3.66e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 294 LEEVKASSRQNPFIRFEQDkklfrNALEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGeLQPD 372
Cdd:COG4178 342 LEAADALPEAASRIETSED-----GALALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPY 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 373 -NGTVKWSENAQI-----------G------YYAQDHEyEFDndltvfdwmsqwkqegDDE-----QAVRsiLGRLLFSQ 429
Cdd:COG4178 416 gSGRIARPAGARVlflpqrpylplGtlrealLYPATAE-AFS----------------DAElrealEAVG--LGHLAERL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 430 DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL--EMYQGTLIFVSHdREFVSSLATRVIE 507
Cdd:COG4178 477 DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLreELPGTTVISVGH-RSTLAAFHDRVLE 555
|
....
gi 490523037 508 ITPE 511
Cdd:COG4178 556 LTGD 559
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-514 |
3.79e-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: 80.84 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSEN----AQIGY-YAQDHEYEFDndLTV 401
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRkkflRRIGVvFGQKTQLWWD--LPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FDWMSQWKQ--EGDDEQAVRSI--LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL 477
Cdd:cd03267 113 IDSFYLLAAiyDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 478 NAALEMY----QGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03267 193 RNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
320-514 |
3.84e-17 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 81.40 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENAQIGYYAQ-D 390
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhgLSRRARARRVALvE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 HEYEFDNDLTVFD--------WMSQWKQE-GDDEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILV 461
Cdd:TIGR03873 82 QDSDTAVPLTVRDvvalgripHRSLWAGDsPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 462 MDEPTNHLDMES-IESLNAALEMY--QGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:TIGR03873 161 LDEPTNHLDVRAqLETLALVRELAatGVTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
6.16e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKlrqdQFAFEqytvldtv 85
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-----GK----PLDIA-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 imghselwevkqERDRIYSLPemsEEDG----YKVADLEVKYGEMDGYS---AESRAGELLLGVGIPlEQHYGPMSEVAP 158
Cdd:cd03269 68 ------------ARNRIGYLP---EERGlypkMKVIDQLVYLAQLKGLKkeeARRRIDEWLERLELS-EYANKRVEELSK 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-514 |
6.46e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQDH------EY 393
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNRigylpeER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 394 EFDNDLTVFD---WMSQWKQEGDDEQA--VRSILGRLLFSqDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNH 468
Cdd:cd03269 80 GLYPKMKVIDqlvYLAQLKGLKKEEARrrIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490523037 469 LDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
6.68e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-----------PNERIGKL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQD-QFAFEqYTVLDTVIMGHSelwevkqerdriyslPEMSEEDGYKVADLEVKYGEMDGYSAESRAGElllgvgipleq 148
Cdd:PRK09536 83 PQDtSLSFE-FDVRQVVEMGRT---------------PHRSRFDTWTETDRAAVERAMERTGVAQFADR----------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 149 hygPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID-TIRWLE--QTLNDRDSTMIIISHDrhfLNM 217
Cdd:PRK09536 136 ---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHD---LDL 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
1.49e-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: 78.70 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 17 FENISVKFGGGNRY-----------------GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFEQY 79
Cdd:cd03257 4 VKNLSVSFPTGGGSvkalddvsfsikkgetlGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 tvldtVIMghselweVKQerDRIYSL-PEMSEEDgyKVADLEVKYGEMDGYSAESRAGELLLgVGIPL-EQHYG--PmSE 155
Cdd:cd03257 84 -----IQM-------VFQ--DPMSSLnPRMTIGE--QIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLpEEVLNryP-HE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-493 |
1.58e-16 |
|
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: 77.35 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSenaqiGYYAQDHEYEFDNDLTVFDwmsqwkqeg 412
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-----GVPVSDLEKALSSLISVLN--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 413 ddeQAVRsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES-IESLNAALEMYQG-TLIF 490
Cdd:cd03247 82 ---QRPY------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTLIW 152
|
...
gi 490523037 491 VSH 493
Cdd:cd03247 153 ITH 155
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-213 |
2.07e-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: 78.63 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGS--KPL--FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQ--- 73
Cdd:COG4181 8 IIELRGLTKTVGTgaGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDArar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 74 -------FAFEQY------TVLDTVimghselwevkqerdriySLPemseedgykvadLEVKyGEMDgysAESRAGELLL 140
Cdd:COG4181 87 lrarhvgFVFQSFqllptlTALENV------------------MLP------------LELA-GRRD---ARARARALLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 141 GVGI-PLEQHY-GPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQtLN-DRDSTMIIISHDRH 213
Cdd:COG4181 133 RVGLgHRLDHYpAQLSG---GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFE-LNrERGTTLVLVTHDPA 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
333-515 |
2.15e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS-ENAQIGYYAQD-----HEYEFDNDLTVFDWMS 406
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 407 QWKQ--EGDDEQAVRSI----LGRLLfsqdDIkkPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAA 480
Cdd:PRK13539 96 FWAAflGGEELDIAAALeavgLAPLA----HL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 481 LEMYQ---GTLIFVSHdrefvSSLAT---RVIEITPERVVD 515
Cdd:PRK13539 170 IRAHLaqgGIVIAATH-----IPLGLpgaRELDLGPFAAED 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-506 |
2.28e-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: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLF----KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN-------------- 381
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 382 AQIGYYAQDHEYEFDNDLTVFD--WMSQWKQEGDDEQAVRSILGRLLFSQddIKKPAKV-------LSGGEKGRMLFGKL 452
Cdd:cd03257 82 KEIQMVFQDPMSSLNPRMTIGEqiAEPLRIHGKLSKKEARKEAVLLLLVG--VGLPEEVlnrypheLSGGQRQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 453 MMQKPNILVMDEPTNHLDMES----IESLNAALEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
330-528 |
2.34e-16 |
|
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: 81.73 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN-----------AQIGYYAQdHEYEFDnd 398
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAWVPQ-NPYLFA-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 LTVFDWMSQWKQEGDDEQAVRSI----LGRLLFSQDD-----IKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHL 469
Cdd:COG4988 425 GTIRENLRLGRPDASDEELEAALeaagLDEFVAALPDgldtpLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 470 DMESIESLNAAL-EMYQG-TLIFVSHDREFVsSLATRVIEITPERVVDfSGGYEDYLRSKG 528
Cdd:COG4988 505 DAETEAEILQALrRLAKGrTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKNG 563
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
318-498 |
2.44e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFDN 397
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTVFDWMSQwkQEGDDEQAVRSILGRLLfSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL 477
Cdd:PRK09544 83 PLTVNRFLRL--RPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|....*
gi 490523037 478 NAALEMYQGTL----IFVSHDREFV 498
Cdd:PRK09544 160 YDLIDQLRRELdcavLMVSHDLHLV 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
330-511 |
2.55e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.42 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLvGELQP-DNGTVKWSENAQIGYYAQdHEYefdndltvfdwMSQw 408
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPwGSGRIGMPEGEDLLFLPQ-RPY-----------LPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 409 kqegddeqavrsilGRLlfsQDDIKKP-AKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGT 487
Cdd:cd03223 78 --------------GTL---REQLIYPwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT 140
|
170 180
....*....|....*....|....
gi 490523037 488 LIFVSHdREFVSSLATRVIEITPE 511
Cdd:cd03223 141 VISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
326-515 |
3.40e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 326 TKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW--------SENA------QIGYYAQD 390
Cdd:COG2884 8 SKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlKRREipylrrRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 HEyeFDNDLTVFDWMS-----QWKQEGDDEQAVRSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDE 464
Cdd:COG2884 88 FR--LLPDRTVYENVAlplrvTGKSRKEIRRRVREVLDLVgLSDKAK-ALPHE-LSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 465 PTNHLD-------MESIESLNAalemyQG-TLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:COG2884 164 PTGNLDpetsweiMELLEEINR-----RGtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-505 |
7.67e-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: 76.52 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE--FDN 397
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAmvFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 -----DLTVFDWMS---QWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGKLMMQKPNILVMDEPTN 467
Cdd:cd03301 81 yalypHMTVYDNIAfglKLRKVPKDEidERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490523037 468 HLD------MES-IESLNAALEMyqgTLIFVSHDREFVSSLATRV 505
Cdd:cd03301 160 NLDaklrvqMRAeLKRLQQRLGT---TTIYVTHDQVEAMTMADRI 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
302-514 |
8.06e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 302 RQNPFIRFEQDKKLFRNAL----EVEAMTKGF------DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGEL-- 369
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLdlseRVAIVLEAFgvelrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 370 QPDNGTVKWSENaqigyyaqdheyEFDNDLTVFDwmsQWKQEGDDEQAVRsILGRL-LFSQDDIKKPAKVLSGGEKGRML 448
Cdd:COG2401 83 TPVAGCVDVPDN------------QFGREASLID---AIGRKGDFKDAVE-LLNAVgLSDAVLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 449 FGKLMMQKPNILVMDEPTNHLDMESIESLNAAL-EMYQ---GTLIFVSHDREFVSSLAtrvieitPERVV 514
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLqKLARragITLVVATHHYDVIDDLQ-------PDLLI 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-210 |
8.72e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 76.89 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQF-----AFEQ 78
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLrraigVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 79 YTVL--DTVimghselwevkqeRDRI-YSLPEMSEEDGY---KVADLEVKYGEM-DGYsaESRAGELllgvGIPLeqhyg 151
Cdd:cd03253 83 DTVLfnDTI-------------GYNIrYGRPDATDEEVIeaaKAAQIHDKIMRFpDGY--DTIVGER----GLKL----- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 152 pmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03253 139 -----SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAH 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-231 |
1.53e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.87 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAG-------NVSLDPNE---RIGKLRQ 71
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREvrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVIMgHSelwevkqerdRIYSLPemseedgykvadlevkygemdGYSAESRAGELLLGVGIpLEQHYG 151
Cdd:cd03265 81 DLSVDDELTGWENLYI-HA----------RLYGVP---------------------GAERRERIDELLDFVGL-LEAADR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 PMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDY 227
Cdd:cd03265 128 LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTrahvWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH 207
|
....
gi 490523037 228 GELR 231
Cdd:cd03265 208 GRII 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-509 |
1.57e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---QIGYYAQD-----H 391
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfQRDSIARGllylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 392 EYEFDNDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIkkPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM 471
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 472 ESIESLNAALEMYQ---GTLIFVSHDREFVSSLATRVIEIT 509
Cdd:cd03231 159 AGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-505 |
1.66e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKLRqdqfafeqytvldt 84
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-----GNPC-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 vimghSELWEVKQERDRIYSLPemseEDGYKVADLEVK----YGEMDGYSAESRAGELL--LGVGIPLEQHYGPMsEVAP 158
Cdd:PRK15439 76 -----ARLTPAKAHQLGIYLVP----QEPLLFPNLSVKenilFGLPKRQASMQKMKQLLaaLGCQLDLDSSAGSL-EVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 159 GWKLRVLlaQALFSNPDILLLDEPTNNLD-IDTIRWLEQ--TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPG 235
Cdd:PRK15439 146 RQIVEIL--RGLMRDSRILILDEPTASLTpAETERLFSRirELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI-ALSG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 236 NYDEYMTAATqarerlladnakkkaqiadlqsfvsrFSANASKSRQATSRARQidKIKLeEVKASSRQNPfirfeQDKKL 315
Cdd:PRK15439 223 KTADLSTDDI--------------------------IQAITPAAREKSLSASQ--KLWL-ELPGNRRQQA-----AGAPV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 316 frnaLEVEAMTkgfdnGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGeLQPDNGTVKWSENAQIGYYA------- 388
Cdd:PRK15439 269 ----LTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPARGGRIMLNGKEINALStaqrlar 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 ---------QDHEYEFDNDLT------VFDWMSQWKQEGdDEQAV----RSILGrLLFSQDDikKPAKVLSGGEKGRMLF 449
Cdd:PRK15439 339 glvylpedrQSSGLYLDAPLAwnvcalTHNRRGFWIKPA-RENAVleryRRALN-IKFNHAE--QAARTLSGGNQQKVLI 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 450 GKLMMQKPNILVMDEPTNHLDMES-------IESLNAalemyQGT-LIFVSHDREFVSSLATRV 505
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDVSArndiyqlIRSIAA-----QNVaVLFISSDLEEIEQMADRV 473
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-211 |
1.68e-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: 76.22 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKL----RQDQFAFE 77
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATDVpvqeRNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 78 QY------TVLDTVIMGhselwevkqerdriyslpemseedgykvadLEVKYGEMDGYSAE--SRAGELLLGVGIP-LEQ 148
Cdd:cd03296 82 HYalfrhmTVFDNVAFG------------------------------LRVKPRSERPPEAEirAKVHELLKLVQLDwLAD 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 149 HYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03296 132 RY-P-AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHD 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-506 |
1.72e-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: 75.84 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV---------KWSENAQIGYYAQ 389
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 dhEYEFDNDLTVFDWMS-----QWKQEGDDEQAVRSILGRLL-FSQDDI---KKPAKvLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:cd03296 82 --HYALFRHMTVFDNVAfglrvKPRSERPPEAEIRAKVHELLkLVQLDWladRYPAQ-LSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490523037 461 VMDEPTNHLDMESIESLNAAL-----EMYQgTLIFVSHDREFVSSLATRVI 506
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLrrlhdELHV-TTVFVTHDQEEALEVADRVV 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-211 |
1.82e-15 |
|
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: 76.07 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE----RIGKLRQ--DQFA--FEQY---- 79
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklKGKALRQlrRQIGmiFQQFnlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 --TVLDTVIMG----HSELWevkqerdriySLPEMseedgYKVADLEvkygemdgysaesRAGELLLGVGIpLEQHYGPM 153
Cdd:cd03256 92 rlSVLENVLSGrlgrRSTWR----------SLFGL-----FPKEEKQ-------------RALAALERVGL-LDKAYQRA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQ 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-506 |
2.18e-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: 78.87 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGF-DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIGY 386
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladADADSwrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 YAQdHEYEFDNdlTVFDWMSQWKQEGDDEQAVRSI-----------LGRLLFSQddIKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:TIGR02857 401 VPQ-HPFLFAG--TIAENIRLARPDASDAEIREALeragldefvaaLPQGLDTP--IGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 456 KPNILVMDEPTNHLDMESIESLNAALEMY-QG-TLIFVSHDREfVSSLATRVI 506
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALaQGrTVLLVTHRLA-LAALADRIV 527
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-212 |
2.71e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.11 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD---------PNER-IGklrqdqFA 75
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlpPRERrVG------FV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQY------TVLDTVIMGHSELWEVKQERDRiyslpemseedgykvadlevkygemdgysaesRAGELLLGVGIP-LEQ 148
Cdd:COG1118 81 FQHYalfphmTVAENIAFGLRVRPPSKAEIRA--------------------------------RVEELLELVQLEgLAD 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 149 HYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI---DTIR-WLEQTLNDRDSTMIIISHDR 212
Cdd:COG1118 129 RY-P-SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-262 |
2.73e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE---RIGKL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpismlsSRQlarRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTVLDTVIMGHS---ELWEvkqerdriyslpEMSEEDGYKVAdlevkygemdgySAESRAGELLLGVGipl 146
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSpwlSLWG------------RLSAEDNARVN------------QAMEQTRINHLADR--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 eqhygPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDID---TIRWLEQTLNDRDSTMIIISHDrhfLNMV---CT 220
Cdd:PRK11231 135 -----RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD---LNQAsryCD 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490523037 221 HMADLDYGELrVYPGNYDEYMTaatqarERLLADNAKKKAQI 262
Cdd:PRK11231 207 HLVVLANGHV-MAQGTPEEVMT------PGLLRTVFDVEAEI 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
415-527 |
2.80e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 78.75 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 415 EQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQGTLIFVSHD 494
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHA 400
|
90 100 110
....*....|....*....|....*....|...
gi 490523037 495 REFVSSLATRVIEITPERVVDFSGGYEDYLRSK 527
Cdd:PLN03073 401 REFLNTVVTDILHLHGQKLVTYKGDYDTFERTR 433
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-227 |
3.45e-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: 78.10 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN-----------ERIGKL 69
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQyTVLDTVIMGHSElwevkqerdriyslpemseedgykVADLEVKygemdgySAESRAG--ELLLGVGIPLE 147
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPD------------------------ASDAEIR-------EALERAGldEFVAALPQGLD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 148 QHYGPM-SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTirwlEQTLND------RDSTMIIISHDRHflnmvct 220
Cdd:TIGR02857 450 TPIGEGgAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEalralaQGRTVLLVTHRLA------- 518
|
....*..
gi 490523037 221 HMADLDY 227
Cdd:TIGR02857 519 LAALADR 525
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-512 |
3.69e-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: 74.78 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFD----NG---PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------KWSENAQ--- 383
Cdd:COG4778 5 LEVENLSKTFTlhlqGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdgGWVDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 ----------IGYYAQdheyeFdndLTV------FDWMSQ--WKQEGDDEQA---VRSILGRLlfsqdDIKK------PA 436
Cdd:COG4778 85 reilalrrrtIGYVSQ-----F---LRViprvsaLDVVAEplLERGVDREEArarARELLARL-----NLPErlwdlpPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 437 kVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES----IESLNAALEmyQGT-LIFVSHDREFVSSLATRVIEITPE 511
Cdd:COG4778 152 -TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGTaIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 490523037 512 R 512
Cdd:COG4778 229 S 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-230 |
4.02e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQ-----FAF 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVN-GQTINLVRDKDgqlkvADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 EQYTVLD---TVIMGHSELWEVKQERDRIYSLPemseedgykvadleVKYGEMDGYSAESRAGELLLGVGIPLEQHYGPM 153
Cdd:PRK10619 85 NQLRLLRtrlTMVFQHFNLWSHMTVLENVMEAP--------------IQVLGLSKQEARERAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-230 |
4.38e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV------------SLDPNER------IGKLRQDQFAFEQY 79
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtKPGPDGRgrakryIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 TVLDTVIMGHS-ELWEVKQERDRIYSLpemseedgyKVADLEVKYGE--MDGYSAESRAGelllgvgiplEQHygpmsev 156
Cdd:TIGR03269 381 TVLDNLTEAIGlELPDELARMKAVITL---------KMVGFDEEKAEeiLDKYPDELSEG----------ERH------- 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 157 apgwklRVLLAQALFSNPDILLLDEPTNNLD-IDTIRWLEQTLNDR---DSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:TIGR03269 435 ------RVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-527 |
4.68e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.73 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 335 FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN--AQIGYYAQdheyeFDNDLTVfdwmsqwkqeg 412
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLELGAG-----FHPELTG----------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 413 ddEQAVRSIlGRLL-FSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESI 474
Cdd:COG1134 106 --RENIYLN-GRLLgLSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 475 ESLNAALEMYQ---GTLIFVSHDREFVSSLATRVIEI---------TPERVVDFsggYEDYLRSK 527
Cdd:COG1134 183 KKCLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLekgrlvmdgDPEEVIAA---YEALLAGR 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-233 |
4.78e-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: 74.49 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 17 FENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKLR---------QDQFAFEQYTVLDTVIM 87
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-----GRVSsllglgggfNPELTGRENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 88 GHSELwEVKQERDRIYSLPEMSEedgykVADLEVKYgemdgYSAesragelllgvgipleqhygpmsevapGWKLRVLLA 167
Cdd:cd03220 113 GLSRK-EIDEKIDEIIEFSELGD-----FIDLPVKT-----YSS---------------------------GMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 168 QALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDaafqekcQRRLR----ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
5.05e-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: 74.39 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF-----GSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnerigklrqdq 73
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 74 fafEQYTVLDTVIMGHSELWEVKqeRDRI-Y------SLPEMSEEDgyKVADLEVKYGEMDGySAESRAGELLLGVGIPL 146
Cdd:COG4778 72 ---HDGGWVDLAQASPREILALR--RRTIgYvsqflrVIPRVSALD--VVAEPLLERGVDRE-EARARARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHygpmsEVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIISHDRHF 214
Cdd:COG4778 144 RLW-----DLPPatfsgGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIE----EAKARGTAIIGIFHDEEV 214
|
250
....*....|..
gi 490523037 215 LNMVCTHMADLD 226
Cdd:COG4778 215 REAVADRVVDVT 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-239 |
5.24e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVS---LDPNErigklRQDQFAFEQytvldTVIMGH-SELW 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgYVPFK-----RRKEFARRI-----GVVFGQrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 94 ---------EVKQErdrIYSLPEmseedgykvADLEVKYGEMDGysaesragelLLGVGIPLEQhygPMSEVAPGWKLRV 164
Cdd:COG4586 109 wdlpaidsfRLLKA---IYRIPD---------AEYKKRLDELVE----------LLDLGELLDT---PVRQLSLGQRMRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLN-DRDSTMIIISHDrhflnmvcthMAD----------LDYGEL 230
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNrERGTTILLTSHD----------MDDiealcdrvivIDHGRI 233
|
....*....
gi 490523037 231 rVYPGNYDE 239
Cdd:COG4586 234 -IYDGSLEE 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-514 |
5.74e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 73.94 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGT--------VKWSEN--AQIGYYAQ 389
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DheYEFDNDLTVFD---WMSQ---WKQEGDDEQAVRSILGRLLFSQDDikKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:cd03265 81 D--LSVDDELTGWEnlyIHARlygVPGAERRERIDELLDFVGLLEAAD--RLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 464 EPTNHLDMES-------IESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03265 157 EPTIGLDPQTrahvweyIEKLKEEFGM---TILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-506 |
7.86e-15 |
|
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: 74.37 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQdhEYEFDNDLTVFDWMSQwkqegddeqaVRSILGR 424
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQ--YIKADYEGTVRDLLSS----------ITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 425 LLFSQDDIKKPAKV----------LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMEsiESLNAA------LEMYQGTL 488
Cdd:cd03237 92 HPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMASkvirrfAENNEKTA 169
|
170
....*....|....*...
gi 490523037 489 IFVSHDREFVSSLATRVI 506
Cdd:cd03237 170 FVVEHDIIMIDYLADRLI 187
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-506 |
8.11e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.36 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------SENAQIGYYA 388
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDHeyefdndlTVFDWMS-----------QWKQEGDDEQAVRSILGR--LLFSQDdiKKPaKVLSGGEK-----GRMLfg 450
Cdd:COG1116 87 QEP--------ALLPWLTvldnvalglelRGVPKAERRERARELLELvgLAGFED--AYP-HQLSGGMRqrvaiARAL-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 451 klmMQKPNILVMDEPTNHLDMESIESLNA-ALEMYQG---TLIFVSHD-REFVsSLATRVI 506
Cdd:COG1116 154 ---ANDPEVLLMDEPFGALDALTRERLQDeLLRLWQEtgkTVLFVTHDvDEAV-FLADRVV 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-505 |
9.07e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 313 KKLFRNALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS--ENAQIGYYAQD 390
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 HEYEFDNdLTVFDWMS-------QWKQE----GDDEQAVRSILGrLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNI 459
Cdd:PRK11607 93 INMMFQS-YALFPHMTveqniafGLKQDklpkAEIASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 460 LVMDEPTNHLDMESIESLNAA----LEMYQGTLIFVSHDREFVSSLATRV 505
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
9.85e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV-----SLDP----------NERIGKLRQDQFAFEQYTVLD 83
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKlssaakaelrNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TVIMghselwevkqerdriyslpemseedgykvadlEVKYGEMDGYSAESRAGELLLGVGIPLEQHYGPmSEVAPGWKLR 163
Cdd:PRK11629 107 NVAM--------------------------------PLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDRDST-MIIISHD 211
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
1.26e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFafeqyt 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vLDTvimghselwevkqerdriySLPE-----MSEEDGYKVADLevkygemdgYSAESR--AGELllgvgipLEQhygPM 153
Cdd:PRK09544 78 -LDT-------------------TLPLtvnrfLRLRPGTKKEDI---------LPALKRvqAGHL-------IDA---PM 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDRHFLnmvcthMADLD 226
Cdd:PRK09544 119 QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLRRELD---CAVLMVSHDLHLV------MAKTD 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-211 |
1.28e-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: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-----------PNERIGKLRQDQFAFEQyT 80
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLDTVIMGH-----SELWEVkQERDRIYSLPEmSEEDGykvadLEVKYGEMdgysaesraGELLLGvgipleqhygpmse 155
Cdd:TIGR02868 425 VRENLRLARpdatdEELWAA-LERVGLADWLR-ALPDG-----LDTVLGEG---------GARLSG-------------- 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 156 vapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS--TMIIISHD 211
Cdd:TIGR02868 475 ---GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
1.50e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNERIGK----L 69
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvattPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTVLDTVIMG---HSelwevkQERdriyslpeMSEEDGYKVadlevkygemdgysaeSRAGELL-LGvgiP 145
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpYS------KGR--------LTAEDREII----------------DEAIAYLdLE---D 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 146 LEQHYgpMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG4604 128 LADRY--LDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-211 |
1.59e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAG-------NVSLDPNERIGKLRQDQFAFeqytvldtvimghs 90
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLRREHFGF-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 91 elweVKQerdRIYSLPEMSEEDGYKVADLevkYGEMDGYSAESRAGELLLGVGIPLEQHYGPmSEVAPGWKLRVLLAQAL 170
Cdd:PRK10535 91 ----IFQ---RYHLLSHLTAAQNVEVPAV---YAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490523037 171 FSNPDILLLDEPTNNLD----IDTIRWLEQtLNDRDSTMIIISHD 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-496 |
1.66e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.82 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 27 GNRYGLIGANGSGKSTFMKILGGDLQPSAGNvsldpnerigklRQDQF------AFEQytvLDTVImghSELWEvkqeRD 100
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGE------------RQSQFshitrlSFEQ---LQKLV---SDEWQ----RN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 101 RIYSLPEMSEEDGYKVADLEvkygeMDGYSAESRAGEL--LLGVGIPLEQHYGPMSEvapGWKLRVLLAQALFSNPDILL 178
Cdd:PRK10938 87 NTDMLSPGEDDTGRTTAEII-----QDEVKDPARCEQLaqQFGITALLDRRFKYLST---GETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 179 LDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrvypgnydeymtAATQARERLLADn 255
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAEllaSLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTL------------AETGEREEILQQ- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 256 akkkAQIADLqsfvsrfsanasksrqatSRARQIDKIKLEEvKASSRQNPFIRFEQDKKLFRNAleveamTKGFDNGPLF 335
Cdd:PRK10938 226 ----ALVAQL------------------AHSEQLEGVQLPE-PDEPSARHALPANEPRIVLNNG------VVSYNDRPIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLK--------------TLVGElQPDNGTVKWSENAQIGYYAQDHEYEFDNDLTV 401
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndlTLFGR-RRGSGETIWDIKKHIGYVSSSLHLDYRVSTSV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 --------FDWMSQWKQEGDDEQA-VRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDme 472
Cdd:PRK10938 356 rnvilsgfFDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD-- 433
|
490 500 510
....*....|....*....|....*....|...
gi 490523037 473 sieSLNAALEMY---------QGTLIFVSHDRE 496
Cdd:PRK10938 434 ---PLNRQLVRRfvdvlisegETQLLFVSHHAE 463
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
320-466 |
1.70e-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: 72.85 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW----------SENAQ--IGYY 387
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglppHERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYeFDNdLTVFD--WMSQWKQEGDDEQAvrsILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMQKPNIL 460
Cdd:cd03224 81 PEGRRI-FPE-LTVEEnlLLGAYARRRAKRKA---RLERVyeLFPrlKERRKQLAGTLSGGEQ-QMLaIARALMSRPKLL 154
|
....*.
gi 490523037 461 VMDEPT 466
Cdd:cd03224 155 LLDEPS 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-515 |
1.76e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.79 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPL----FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGtvkwseNAQIGYYAQDHE--- 392
Cdd:cd03266 2 ITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG------FATVDGFDVVKEpae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 393 ------YEFDNDlTVFDWMSQWKQ----------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:cd03266 76 arrrlgFVSDST-GLYDRLTARENleyfaglyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 457 PNILVMDEPTNHLDMESIESLNAALEMY---QGTLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
2.01e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.75 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DqfafeqytvldtvimghselwevkqerdriYSL-PEMSeedgykVADlEVKYG-EMDGYSAE---SRAGELLLGVGIP- 145
Cdd:COG3842 85 D------------------------------YALfPHLT------VAE-NVAFGlRMRGVPKAeirARVAELLELVGLEg 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 146 LEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDR 212
Cdd:COG3842 128 LADRY-P-HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
2.20e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 72.06 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNErIGKLRQDQFAFEQYTVldT 84
Cdd:cd03292 5 NVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGRAIPYLRRKI--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VIMGHSELwevkqerdriysLPEMSEEDGYKVAdLEVKYgeMDGYSAESRAGELLLGVGIPLEQHYGPMsEVAPGWKLRV 164
Cdd:cd03292 82 VVFQDFRL------------LPDRNVYENVAFA-LEVTG--VPPREIRKRVPAALELVGLSHKHRALPA-ELSGGEQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 165 LLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHDRHFLN 216
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVD 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
2.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAfeqy 79
Cdd:PRK13651 6 KNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 TVLDTVIMGHS---ELWEVKQERDRI--------YSLPEMS-EEDgykVADLEVKYGeMDGYSAESRAGELLLGVGIPLE 147
Cdd:PRK13651 82 KVLEKLVIQKTrfkKIKKIKEIRRRVgvvfqfaeYQLFEQTiEKD---IIFGPVSMG-VSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 148 qhYGPMS--EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-IDTIRWLE--QTLNDRDSTMIIISHD 211
Cdd:PRK13651 158 --YLQRSpfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-210 |
2.66e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 75.93 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFG-SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDP----NERIGKLR------ 70
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkDIDRHTLRqfinyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 -QDQFAFEQyTVLDTVIMGHSElwevKQERDRIYSLPEMSEEDgykvADLEvkygemdgysaesragELLLGVGIPLEQH 149
Cdd:TIGR01193 554 pQEPYIFSG-SILENLLLGAKE----NVSQDEIWAACEIAEIK----DDIE----------------NMPLGYQTELSEE 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 150 YGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-IRWLEQTLNDRDSTMIIISH 210
Cdd:TIGR01193 609 GSSISG---GQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH 667
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-506 |
3.08e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.03 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA----------QIGYYAQ 389
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 D-----HeyefdndLTVFDwms-qwKQEGDDEQAVRSILGRLL--FSQDDIKK--PAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:COG1118 83 HyalfpH-------MTVAEniafglRVRPPSKAEIRARVEELLelVQLEGLADryPSQ-LSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 460 LVMDEPTNHLD------MESieSLNAALEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:COG1118 155 LLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-245 |
3.91e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAfeqytvldtv 85
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-AQPLESWSSKAFA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 imghselwevkqeRDRIYSLPEMSEEDGYKVADLEV--KY---GEMDGYSAESRAG--ELLLGVGI-PLEQHYgpMSEVA 157
Cdd:PRK10575 85 -------------RKVAYLPQQLPAAEGMTVRELVAigRYpwhGALGRFGAADREKveEAISLVGLkPLAHRL--VDSLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDrhfLNMV---CTHMADLDYGEL 230
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD---INMAaryCDYLVALRGGEM 226
|
250
....*....|....*
gi 490523037 231 rVYPGNYDEYMTAAT 245
Cdd:PRK10575 227 -IAQGTPAELMRGET 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
333-510 |
4.49e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE---NAQIGYYAQD-----HEYEFDNDLTVF-- 402
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHQDllylgHQPGIKTELTALen 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 403 -DWMSQWKQEGDDEqAVRSILGRL-LFSQDDIkkPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAA 480
Cdd:PRK13538 95 lRFYQRLHGPGDDE-ALWEALAQVgLAGFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170 180 190
....*....|....*....|....*....|...
gi 490523037 481 LEMYQ---GTLIFVSHDREFVSSLATRVIEITP 510
Cdd:PRK13538 172 LAQHAeqgGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
336-505 |
5.30e-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: 71.38 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----------AQIGYYAQdheyeFDN---DLTVF 402
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYCPQ-----FDAlfdELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 403 D---WMSQWK-QEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL- 477
Cdd:cd03263 94 EhlrFYARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIw 173
|
170 180
....*....|....*....|....*....
gi 490523037 478 NAALEMYQG-TLIFVSHDREFVSSLATRV 505
Cdd:cd03263 174 DLILEVRKGrSIILTTHSMDEAEALCDRI 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-527 |
5.65e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.22 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 338 VGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPD------NGTVkWSENAQ----------IGYYAQDheyefdndLTV 401
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDegeivlNGRT-LFDSRKgiflppekrrIGYVFQE--------ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FDWMS--------QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES 473
Cdd:TIGR02142 87 FPHLSvrgnlrygMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 474 -------IESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVVDFsGGYEDYLRSK 527
Cdd:TIGR02142 167 kyeilpyLERLHAEFGI---PILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAEVWASP 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-231 |
7.53e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.86 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPnerigklrqdqfafeqytvLDTvimgHSELWEVKQ 97
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-------------------FDV----VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 98 ------ERDRIYslPEMS--EEDGYkVADLevkYGeMDGYSAESRAGEL--LLGVGIPLEQHYGPMSEvapGWKLRVLLA 167
Cdd:cd03266 79 rlgfvsDSTGLY--DRLTarENLEY-FAGL---YG-LKGDELTARLEELadRLGMEELLDRRVGGFST---GMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 168 QALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-505 |
7.89e-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: 71.11 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---------QIGYYAQD 390
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 heYEFDNDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEP 465
Cdd:cd03300 81 --YALFPHLTVFENIAfglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490523037 466 TNHLDMESIESLNAALEMYQG----TLIFVSHDREFVSSLATRV 505
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRI 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-516 |
8.37e-14 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 70.67 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTL-----VGELQPDNGTV--------KWSEN----- 381
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVlldgkdiyDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 382 AQIGYYAQdHEYEFDndLTVFDWMS--------QWKQEGDDEqaVRSILGR-LLFSQDDIKKPAKVLSGGEKGRMLFGKL 452
Cdd:cd03260 81 RRVGMVFQ-KPNPFP--GSIYDNVAyglrlhgiKLKEELDER--VEEALRKaALWDEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 453 MMQKPNILVMDEPTNHLDMES---IESLNAALEMyQGTLIFVSHDREFVSSLATRVIEITPERVVDF 516
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-254 |
8.82e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAG-----NVSLDPNERIGK------- 68
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 LRQD-QFAFEQY------TVLDTVIMGHSElweVKQE-RDriyslpemseedgykvadlevkygemdgySAESRAGELLL 140
Cdd:PRK11264 83 LRQHvGFVFQNFnlfphrTVLENIIEGPVI---VKGEpKE-----------------------------EATARARELLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 141 GVGIPLEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlndRDSTMIIISHDRH 213
Cdd:PRK11264 131 KVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQ----EKRTMVIVTHEMS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490523037 214 FLNMVCTHMADLDYGELrVYPGNYDEYMTAATQARERLLAD 254
Cdd:PRK11264 206 FARDVADRAIFMDQGRI-VEQGPAKALFADPQQPRTRQFLE 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
318-515 |
9.15e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE----------------- 380
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 381 --NAQIGYYAQD-----HEYEFDNdltVFDWMSQWKQEGDDE--QAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGK 451
Cdd:PRK11264 82 qlRQHVGFVFQNfnlfpHRTVLEN---IIEGPVIVKGEPKEEatARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 452 LMMQKPNILVMDEPTNHLDMESI-ESLNA--ALEMYQGTLIFVSHDREFVSSLATRVIEITPERVVD 515
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
320-514 |
1.20e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQD--------- 390
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKevarrigll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 -HEYEFDNDLTVFDWMS-----------QWKQEgdDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPN 458
Cdd:PRK10253 87 aQNATTPGDITVQELVArgryphqplftRWRKE--DEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 459 ILVMDEPTNHLDME---SIESLNAALEMYQG-TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10253 164 IMLLDEPTTWLDIShqiDLLELLSELNREKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-510 |
1.73e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.74 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYAQD----HEYEFDN 397
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqQVSYCAQTptlfGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 dlTVFDWmsQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL 477
Cdd:PRK10247 101 --LIFPW--QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 490523037 478 NAALEMY----QGTLIFVSHDREFVSSlATRVIEITP 510
Cdd:PRK10247 177 NEIIHRYvreqNIAVLWVTHDKDEINH-ADKVITLQP 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-506 |
1.82e-13 |
|
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: 69.48 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSE-NAQIGY 386
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 YAQDheYEFDNDLTVFDWMS---QWKQEGDDEQAV---RSILGRL-LFSQDDiKKPAKvLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03262 81 VFQQ--FNLFPHLTVLENITlapIKVKGMSKAEAEeraLELLEKVgLADKAD-AYPAQ-LSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 460 LVMDEPTNHLDMESI-ESLNAALEMYQG--TLIFVSHDREFVSSLATRVI 506
Cdd:cd03262 157 MLFDEPTSALDPELVgEVLDVMKDLAEEgmTMVVVTHEMGFAREVADRVI 206
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-210 |
1.83e-13 |
|
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: 69.81 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKP---LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKLRQdQFAFEQYtvl 82
Cdd:cd03248 16 NVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD-----GKPIS-QYEHKYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 83 dtvimgHSELWEVKQE--------RDRI-YSLPEMSEEdgyKVADLEVKYG------EM-DGYSAES-RAGELLLGvgip 145
Cdd:cd03248 87 ------HSKVSLVGQEpvlfarslQDNIaYGLQSCSFE---CVKEAAQKAHahsfisELaSGYDTEVgEKGSQLSG---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 146 leqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03248 154 -------------GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAH 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-230 |
2.06e-13 |
|
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: 70.60 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVS--------LDPNERIGKLRQDQFAFEqytvld 83
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRKQRRAFRRDVQLVFQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 tvimghselwevkqerDRIYSL-PEMSEEdgYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLE--QHYGPmsEVAPGW 160
Cdd:TIGR02769 96 ----------------DSPSAVnPRMTVR--QIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdaDKLPR--QLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
320-508 |
2.07e-13 |
|
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: 69.36 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-------QIGYYAQD- 390
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgrAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 ----HEYEFDNDLTVFDWMS---QWKQEGDDEQAVR-SILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:cd03292 81 gvvfQDFRLLPDRNVYENVAfalEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 463 DEPTNHLD-------MESIESLNAAlemyqGTLIFVS-HDREFVSSLATRVIEI 508
Cdd:cd03292 161 DEPTGNLDpdttweiMNLLKKINKA-----GTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-507 |
2.44e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----------AQIGYYA 388
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QdheyeFDN---DLTVFDWMSQWKQE-GDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILV 461
Cdd:PRK13537 87 Q-----FDNldpDFTVRENLLVFGRYfGLSAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 462 MDEPTN-------HLDMESIESLNAALEmyqgTLIFVSHDREFVSSLATR--VIE 507
Cdd:PRK13537 162 LDEPTTgldpqarHLMWERLRSLLARGK----TILLTTHFMEEAERLCDRlcVIE 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-212 |
2.49e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.27 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL---DPNERIGKLRQDQFAFEQY-- 79
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtDVSRLHARDRKVGFVFQHYal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 ----TVLDTVIMGHSELwevkQERDRiyslPemseedgykvadlevkygemDGYSAESRAGELLLGVGIP-LEQHYgPmS 154
Cdd:PRK10851 86 frhmTVFDNIAFGLTVL----PRRER----P--------------------NAAAIKAKVTQLLEMVQLAhLADRY-P-A 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDR 212
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
2.96e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 67.45 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLdpnerigklrqdqfafeqytv 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 ldtvimghselwevkqerdriyslpemseeDGYKVADLEVKygemdgysaESRAgellLGVGIpleqhygpMSEVAPGWK 161
Cdd:cd03216 60 ------------------------------DGKEVSFASPR---------DARR----AGIAM--------VYQLSVGER 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND-RDS--TMIIISH 210
Cdd:cd03216 89 QMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRlRAQgvAVIFISH 140
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-513 |
2.99e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK-----------WSENAQIGYYAQDHEYEF----DN 397
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQVGMVFQNPDNQFvgatVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTVF---------DWMSQWKQEGDDEQAVRSILGRllfsqddikKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNH 468
Cdd:PRK13635 101 DDVAFglenigvprEEMVERVDQALRQVGMEDFLNR---------EPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 469 LD-------MESIESLNAALEMyqgTLIFVSHDREFVSSlATRVI---------EITPERV 513
Cdd:PRK13635 171 LDprgrrevLETVRQLKEQKGI---TVLSITHDLDEAAQ-ADRVIvmnkgeileEGTPEEI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
317-494 |
3.70e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 71.70 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 317 RNALEVEAMTKGF--DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---Q 383
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqWDREElgrH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 IGYYAQDHEYeFDNdlTV------FDwmsqwkqEGDDEQAVRS---------ILgRLlfsqddikkP----------AKV 438
Cdd:COG4618 408 IGYLPQDVEL-FDG--TIaeniarFG-------DADPEKVVAAaklagvhemIL-RL---------PdgydtrigegGAR 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 439 LSGGEK-----GRMLFGKlmmqkPNILVMDEPTNHLDMESIESLNAALEM--YQG-TLIFVSHD 494
Cdd:COG4618 468 LSGGQRqriglARALYGD-----PRLVVLDEPNSNLDDEGEAALAAAIRAlkARGaTVVVITHR 526
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
3.98e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.34 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLdpNERIGKLrqdqfaFE-------QYTVLDTV-----I 86
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--NGRVSAL------LElgagfhpELTGRENIylngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 87 MGHSElWEVKQERDRIYSLPEMSEedgykVADLEVKYgemdgYSAesragelllgvgipleqhygpmsevapGWKLRVLL 166
Cdd:COG1134 116 LGLSR-KEIDEKFDEIVEFAELGD-----FIDQPVKT-----YSS---------------------------GMRARLAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 167 AQALFSNPDILLLDEptnNL---DID----TIRWLEQtLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVY 233
Cdd:COG1134 158 AVATAVDPDILLVDE---VLavgDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-211 |
4.42e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 68.90 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQDQFAFEQYTVLDTVIMG 88
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlpPEKRdISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 HSELWEVKQERDRiySLPEMSEedgykvadlevkygemdgysaesragelLLGVGIPLEQHYGPMSEvapGWKLRVLLAQ 168
Cdd:cd03299 96 LKKRKVDKKEIER--KVLEIAE----------------------------MLGIDHLLNRKPETLSG---GEQQRVAIAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490523037 169 ALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHD 211
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
340-514 |
5.40e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 68.29 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 340 LLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGtvkwsenaQIGYYAQDHEYE----------F-DND----LTVFDW 404
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSG--------RVLINGVDVTAAppadrpvsmlFqENNlfahLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 405 MS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD----MESIE 475
Cdd:cd03298 91 VGlglspGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 490523037 476 SLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
320-494 |
6.28e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDH---EyefdnDLTVFD--------WMSQW-KQEGDDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK11231 83 QHHltpE-----GITVRElvaygrspWLSLWgRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 457 PNILVMDEPTNHLDM-ESIESLNAALEMYQG--TLIFVSHD 494
Cdd:PRK11231 157 TPVVLLDEPTTYLDInHQVELMRLMRELNTQgkTVVTVLHD 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-218 |
7.15e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.93 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER---IGK 68
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDgadlsqwdREELgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 LRQDQFAFEqytvlDTVimghselwevkqeRDRIYSLPEMSEEDGYKVADLEvkyG--EM-----DGYsaESRAGELllg 141
Cdd:COG4618 411 LPQDVELFD-----GTI-------------AENIARFGDADPEKVVAAAKLA---GvhEMilrlpDGY--DTRIGEG--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 vGIPLeqhygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:COG4618 465 -GARL----------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalkARGATVVVITHRPSLLAAV 533
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-231 |
7.60e-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: 67.71 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 27 GNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------------PNER-IGKLRQDQFAFEQYTVLDTVIMGhse 91
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkinlpPQQRkIGLVFQQYALFPHLNVRENLAFG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 92 LWEVKQERDRIySLPEMSEedgykvadlevkygemdgysaesragelLLGVGiPLEQHYgpMSEVAPGWKLRVLLAQALF 171
Cdd:cd03297 100 LKRKRNREDRI-SVDELLD----------------------------LLGLD-HLLNRY--PAQLSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 172 SNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:cd03297 148 AQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
8.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.48 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE-----------RIG 67
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeirkKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 68 KLRQD---QFAfeQYTVLDTVIMGHselwevkqeRDRIYSLPEMSEedgyKVADLEVKYGeMDGYsaesragelllgvgI 144
Cdd:PRK13632 87 IIFQNpdnQFI--GATVEDDIAFGL---------ENKKVPPKKMKD----IIDDLAKKVG-MEDY--------------L 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 145 PLEQHYgpmseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13632 137 DKEPQN-----LSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
318-519 |
8.92e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.72 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGP-LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV---------------KWSEN 381
Cdd:PRK13636 4 YILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 382 AQIGYYAQDHE------YEfdnDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMQ 455
Cdd:PRK13636 84 VGMVFQDPDNQlfsasvYQ---DVS-FGAVNLKLPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 456 KPNILVMDEPTNHLDMESI-ESLNAALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVVdFSGG 519
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVsEIMKLLVEMQKElglTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-212 |
9.24e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.75 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNErigklrqdqfafeqytV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED----------------V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 LDTVImghselwevkQERD-----RIYSL-PEMSEEDgykvadlEVKYG-EMDGYSAE---SRAGELLLGVGIP-LEQHY 150
Cdd:PRK11432 71 THRSI----------QQRDicmvfQSYALfPHMSLGE-------NVGYGlKMLGVPKEerkQRVKEALELVDLAgFEDRY 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 151 gpMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDR 212
Cdd:PRK11432 134 --VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFN---ITSLYVTHDQ 197
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-507 |
1.04e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK----------WSENAQIGYYA 388
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 Q----DHEYEFDNDLTVFDwmsqwKQEGDDEQAVRSILGRLL-FSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILV 461
Cdd:PRK13536 121 QfdnlDLEFTVRENLLVFG-----RYFGMSTREIEAVIPSLLeFARLESKADARVsdLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 462 MDEPTN-------HLDMESIESLNAalemyQG-TLIFVSHDREFVSSLATR--VIE 507
Cdd:PRK13536 196 LDEPTTgldpharHLIWERLRSLLA-----RGkTILLTTHFMEEAERLCDRlcVLE 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
318-514 |
1.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGP-LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSENaQI 384
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaeneKWVRS-KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 385 GYYAQDheyefdNDLTVFDwMSQWkqegDD---------------EQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLF 449
Cdd:PRK13647 82 GLVFQD------PDDQVFS-STVW----DDvafgpvnmgldkdevERRVEEAL-KAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 450 GKLMMQKPNILVMDEPTNHLDMESIESLNAALEMY--QG-TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-210 |
1.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 11 FGSKPLFEnISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpneRIGklrqdqfafeqytvlDTVIMGHS 90
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVG---------------DIVVSSTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 91 ELWEVKQERDR---IYSLPE--MSEEDGYKvadlEVKYGEMD-GYS---AESRAGELLLGVGIPLEQHYGPMSEVAPGWK 161
Cdd:PRK13643 75 KQKEIKPVRKKvgvVFQFPEsqLFEETVLK----DVAFGPQNfGIPkekAEKIAAEKLEMVGLADEFWEKSPFELSGGQM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEqTLNDRDSTMIIISH 210
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFE-SIHQSGQTVVLVTH 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-530 |
1.26e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.49 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-----------QIGYYA 388
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDHEYEFDND------------LTVFDWMSQwkqegDDEQAVRSILGRLLFSQdDIKKPAKVLSGGEKGRMLFGKLMMQK 456
Cdd:PRK09536 84 QDTSLSFEFDvrqvvemgrtphRSRFDTWTE-----TDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 457 PNILVMDEPTNHLDM-ESIESLNAALEMYQG--TLIFVSHDREFVSSLATRVIEITPERVVDfSGGYEDYLRSKGIE 530
Cdd:PRK09536 158 TPVLLLDEPTASLDInHQVRTLELVRRLVDDgkTAVAAIHDLDLAARYCDELVLLADGRVRA-AGPPADVLTADTLR 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-239 |
1.64e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.21 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGklrqdqfafeqyt 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLD------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vldtvimghselwevKQERDRI-YsLPemsEEDGY----KVADLEVKYGEMDGYS---AESRAGELL--LGVGiplEQHY 150
Cdd:COG4152 67 ---------------PEDRRRIgY-LP---EERGLypkmKVGEQLVYLARLKGLSkaeAKRRADEWLerLGLG---DRAN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 151 GPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQT---LNDRDSTMIIISHDrhfLNMV---CTHMAD 224
Cdd:COG4152 125 KKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVireLAAKGTTVIFSSHQ---MELVeelCDRIVI 201
|
250
....*....|....*
gi 490523037 225 LDYGELRVYpGNYDE 239
Cdd:COG4152 202 INKGRKVLS-GSVDE 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
319-470 |
1.71e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.49 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WS--ENAQI-GYY 387
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladWSpaELARRrAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYEFdnDLTVFD--WM--SQWKQ-EGDDEQAVRSIL---------GRLLfsqddikkPAkvLSGGEKGRMLFGKLM 453
Cdd:PRK13548 82 PQHSSLSF--PFTVEEvvAMgrAPHGLsRAEDDALVAAALaqvdlahlaGRDY--------PQ--LSGGEQQRVQLARVL 149
|
170 180
....*....|....*....|...
gi 490523037 454 MQ------KPNILVMDEPTNHLD 470
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALD 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
321-493 |
1.96e-12 |
|
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: 66.87 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 321 EVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQIGYYA 388
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDhEYEFDNdlTVFDWMSQWKQEGDDEQAVrsILGRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMQKP 457
Cdd:cd03254 84 QD-TFLFSG--TIMENIRLGRPNATDEEVI--EAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 490523037 458 NILVMDEPTNHLDMESIESLNAALE--MYQGTLIFVSH 493
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEklMKGRTSIIIAH 196
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-211 |
2.05e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 67.46 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGklrqdqfafeqytvLD 83
Cdd:TIGR04520 5 NVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----G--------------LD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TviMGHSELWEVKQERDRIYSLPE------MSEEDgykVA----DLEVKYGEMdgysaESRAGELLLGVGipleqhygpM 153
Cdd:TIGR04520 66 T--LDEENLWEIRKKVGMVFQNPDnqfvgaTVEDD---VAfgleNLGVPREEM-----RKRVDEALKLVG---------M 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 154 SE---VAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHD 211
Cdd:TIGR04520 127 EDfrdREPhllsgGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNK---EEGITVISITHD 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
2.54e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIgklrqDQFAFEQYT 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-----DPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLdtvimGHSElwEVKqerdriyslPEMSeedgykVAD-LEV---KYGemdgySAESRAGELLLGVGIPLEQH--YGPMS 154
Cdd:PRK13539 77 YL-----GHRN--AMK---------PALT------VAEnLEFwaaFLG-----GEELDIAAALEAVGLAPLAHlpFGYLS 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 490523037 155 EvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIR 192
Cdd:PRK13539 130 A---GQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-187 |
2.56e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpnerigklrqdqfafeqyTVLDT 84
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------------------TVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VIMGHSELwevkqERDRIYSLPEMSEED-GYKVADLEVKYGEMDGYSAesRAGELLlgvgIP-------LEQHY-GPMSE 155
Cdd:PRK13536 104 PVPARARL-----ARARIGVVPQFDNLDlEFTVRENLLVFGRYFGMST--REIEAV----IPsllefarLESKAdARVSD 172
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-187 |
2.60e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL--DP-NERIGKLRQDQFAFEQYTVL 82
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPvPSRARHARQRVGVVPQFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 83 D---TV-----IMGHSELWEVKQERDRIYSLPEMseedgykvADLEVKygemdgysAESRAGELllgvgipleqhygpms 154
Cdd:PRK13537 92 DpdfTVrenllVFGRYFGLSAAAARALVPPLLEF--------AKLENK--------ADAKVGEL---------------- 139
|
170 180 190
....*....|....*....|....*....|...
gi 490523037 155 evAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13537 140 --SGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-506 |
3.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGT------------VKWSE-NAQIGYYAQDHEYEF-----DN 397
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkVKLSDiRKKVGLVFQYPEYQLfeetiEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIK-KPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD------ 470
Cdd:PRK13637 104 DIA-FGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrde 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 490523037 471 -MESIESLNaalEMYQGTLIFVSHDREFVSSLATRVI 506
Cdd:PRK13637 183 iLNKIKELH---KEYNMTIILVSHSMEDVAKLADRII 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-210 |
3.19e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 17 FENISVKFGG-------------GNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERigklrqdQFAFEQYTVLD 83
Cdd:PRK11288 7 FDGIGKTFPGvkalddisfdcraGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-------RFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TVIMGHSELWEVkqerdriyslPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQHyGPMSEVAPGWKLR 163
Cdd:PRK11288 80 GVAIIYQELHLV----------PEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPD-TPLKYLSIGQRQM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-216 |
3.25e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSkplF---ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL-----DPNE-----RIGKLRQd 72
Cdd:NF033858 271 GLTMRFGD---FtavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDiatrrRVGYMSQ- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 qfAFEQYtvldtvimghSELwEVKQERD---RIYSLPEmsEEDGYKVADLEVKYGEMDgySAESRAGELLLGVgipleqh 149
Cdd:NF033858 347 --AFSLY----------GEL-TVRQNLElhaRLFHLPA--AEIAARVAEMLERFDLAD--VADALPDSLPLGI------- 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 150 ygpmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLD-----------IDtirwleqtLNDRDSTMIIIShdRHFLN 216
Cdd:NF033858 403 -----------RQRLSLAVAVIHKPELLILDEPTSGVDpvardmfwrllIE--------LSREDGVTIFIS--THFMN 459
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-211 |
3.40e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnerigklrqdqfafeqytvlDTVIMGHSELWEVKQE 98
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD---------------------DITITHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 99 RDRI---YSLPEMSE-EDGykvADLEVKYG----EMDGYSAESRAGELLLGVGIP---LEQHYGPMSevapGWKLR-VLL 166
Cdd:PRK13646 84 RKRIgmvFQFPESQLfEDT---VEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrdvMSQSPFQMS----GGQMRkIAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490523037 167 AQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-210 |
3.56e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGK---------LRQdQFAF-EQYTV 81
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-----GVdirdltlesLRR-QIGVvPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 L--DTVimghselwevkqeRDRI-YSLPEMSEEDGYKVADLevkygemdgysaeSRAGELLLGvgipLEQHYGpmSEVAP 158
Cdd:COG1132 425 LfsGTI-------------RENIrYGRPDATDEEVEEAAKA-------------AQAHEFIEA----LPDGYD--TVVGE 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 159 -GWKL------RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:COG1132 473 rGVNLsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAH 533
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-211 |
4.17e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.26 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGKLRQDQF 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 AFEQYTVLDTVIMGhSELWEV-KQERdriyslpemseedgykvadlevkygemdgysaESRAGELLLGVGIP-LEQHYgp 152
Cdd:PRK11248 81 LLPWRNVQDNVAFG-LQLAGVeKMQR--------------------------------LEIAHQMLKKVGLEgAEKRY-- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTiRWLEQTL-----NDRDSTMIIISHD 211
Cdd:PRK11248 126 IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT-REQMQTLllklwQETGKQVLLITHD 188
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-242 |
4.20e-12 |
|
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: 66.17 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV--------SLDPNE---RIGKLRQD 72
Cdd:cd03295 4 ENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedirEQDPVElrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 QFAFEQYTVLDTVIMGHSEL-WEVKQERDRIYslpemseedgykvadlevkygemdgysaesragELLLGVGIPlEQHYG 151
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLkWPKEKIRERAD---------------------------------ELLALVGLD-PAEFA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 ---PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDRHFLNMVCTH 221
Cdd:cd03295 130 dryP-HELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdqlqEEFKRLQQELG---KTIVFVTHDIDEAFRLADR 205
|
250 260
....*....|....*....|.
gi 490523037 222 MADLDYGELRVYpGNYDEYMT 242
Cdd:cd03295 206 IAIMKNGEIVQV-GTPDEILR 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
319-513 |
4.75e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW---------SENAQIGYYAQ 389
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 dhEYEFDNDLTVFDWMSQW-----KQEGDDEQAVRSILGRLL----FSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK10851 82 --HYALFRHMTVFDNIAFGltvlpRRERPNAAAIKAKVTQLLemvqLAHLADRYPAQ-LSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 461 VMDEPTNHLDMESIESLNAAL----EMYQGTLIFVSHDREFVSSLATRV-------IEI--TPERV 513
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVvvmsqgnIEQagTPDQV 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-211 |
4.80e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 32 LIGANGSGKSTFMKILGGDLQPSAGNVSL--------DPNERiGKLRQDQ--FAFEQYTVLDTVimghSELWEVKqerdr 101
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEAR-AKLRAKHvgFVFQSFMLIPTL----NALENVE----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 102 iysLPEMSEedgykvadlevkyGEMDGYSAEsRAGELLLGVGIPLEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
Cdd:PRK10584 111 ---LPALLR-------------GESSRQSRN-GAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....
gi 490523037 182 PTNNLDIDT---IRWLEQTLN-DRDSTMIIISHD 211
Cdd:PRK10584 173 PTGNLDRQTgdkIADLLFSLNrEHGTTLILVTHD 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-187 |
5.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 11 FGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnerigklrqdqfafeqytvlDTVIMGHS 90
Cdd:PRK13649 18 FEGRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD---------------------DTLITSTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 91 ELWEVKQERDR---IYSLPE--MSEEDGYKvadlEVKYGEMD-GYS---AESRAGELLLGVGIPLEQHYGPMSEVAPGWK 161
Cdd:PRK13649 76 KNKDIKQIRKKvglVFQFPEsqLFEETVLK----DVAFGPQNfGVSqeeAEALAREKLALVGISESLFEKNPFELSGGQM 151
|
170 180
....*....|....*....|....*.
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-211 |
6.41e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.16 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltalpPAERpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVIMG-HSELwevkqerdriyslpEMSEEDGYKVADLEVKYGeMDGYsaESRAGELLLGvgipleqhy 150
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlRPGL--------------KLTAEQRAQVEQALERVG-LAGL--LDRLPGQLSG--------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 151 gpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG3840 133 --------GQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-244 |
9.91e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE-----------RIGKLRQDQF 74
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 AFEQYTVLDTVIMG---HSELWEVKQERDriyslpemseEDGYKVADLEVKYGEMDGYSAESRAGelllgvgipleqhyg 151
Cdd:PRK10253 92 TPGDITVQELVARGrypHQPLFTRWRKED----------EEAVTKAMQATGITHLADQSVDTLSG--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 152 pmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDrhfLNMVC---THMAD 224
Cdd:PRK10253 147 -------GQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQACryaSHLIA 216
|
250 260
....*....|....*....|
gi 490523037 225 LDYGELrVYPGNYDEYMTAA 244
Cdd:PRK10253 217 LREGKI-VAQGAPKEIVTAE 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
1.03e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 67.37 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDP-----------NERIGKLRQDqfafeqyt 80
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfGKHIGYLPQD-------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vldtvimghSELWE--VKQERDRIYSLPEmSEE--DGYKVADL-EVKYGEMDGYSAESRAGelllgvGIPLeqhygpmse 155
Cdd:TIGR01842 401 ---------VELFPgtVAENIARFGENAD-PEKiiEAAKLAGVhELILRLPDGYDTVIGPG------GATL--------- 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 156 vAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMV 218
Cdd:TIGR01842 456 -SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlkaRGITVVVITHRPSLLGCV 520
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-210 |
1.13e-11 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 64.56 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSK--PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDP-----------NERIGKLRQD 72
Cdd:cd03251 5 NVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 QFAFEqytvlDTVimghselwevkqeRDRI-YSLPEMSEEDGYKVADL----EVKYGEMDGYsaESRAGELllgvGIPLe 147
Cdd:cd03251 85 VFLFN-----DTV-------------AENIaYGRPGATREEVEEAARAanahEFIMELPEGY--DTVIGER----GVKL- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 148 qhygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03251 140 ---------SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlmKNRTTFVIAH 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-530 |
1.32e-11 |
|
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: 66.75 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVG--ELQPDNGTVKWS------------------ 379
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 380 ---------ENAQIGYYAQDHEYEFD----------------NDLTVFD----WMSQWKQEGDDEQAVRSILGRLLFSQD 430
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRRRirkriaimlqrtfalyGDDTVLDnvleALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 431 DIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEM----YQGTLIFVSHDREFVSSLATRVI 506
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....
gi 490523037 507 ---------EITPERVVD-FSGGYEDYLRSKGIE 530
Cdd:TIGR03269 241 wlengeikeEGTPDEVVAvFMEGVSEVEKECEVE 274
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-514 |
1.77e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYEFDN- 397
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL----------DGEPVRFRSp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 -------------DLTVFDWMS-----------------QWKQEgddEQAVRSILGRLLFSqDDIKKPAKVLSGGEKGRM 447
Cdd:COG1129 74 rdaqaagiaiihqELNLVPNLSvaeniflgreprrggliDWRAM---RRRARELLARLGLD-IDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 448 LFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMY--QG-TLIFVSH---------DR-------EFVSSLATRviEI 508
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISHrldevfeiaDRvtvlrdgRLVGTGPVA--EL 227
|
....*.
gi 490523037 509 TPERVV 514
Cdd:COG1129 228 TEDELV 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
336-509 |
2.26e-11 |
|
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: 63.64 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYYAQDHEYEFDNdLTVFDWMSQWKQ----- 410
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQN-YSLLPWLTVRENialav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 411 --------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL- 481
Cdd:TIGR01184 80 drvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELm 158
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 482 ---EMYQGTLIFVSHDREFVSSLATRVIEIT 509
Cdd:TIGR01184 159 qiwEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-243 |
2.42e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPneRIGKLRQDQFAFEQYTVLDT 84
Cdd:PRK14246 14 SRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VIMghselweVKQERDriySLPEMSEEDgyKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQH---YGPMSEVAPGWK 161
Cdd:PRK14246 92 VGM-------VFQQPN---PFPHLSIYD--NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVARVADYVAFLYNGEL-VEWGSSNE 238
|
....
gi 490523037 240 YMTA 243
Cdd:PRK14246 239 IFTS 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-514 |
2.46e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLF---------KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------ENAQ 383
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 IGYYAQDHEYEFDNDLTVFdwmsqwkqegDDEQAVRSILG---RLLFSQDDIKKPAKV--------------------LS 440
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAV----------NPRKTVREIIReplRHLLSLDKAERLARAsemlravdlddsvldkrppqLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 441 GGEKGRMLFGKLMMQKPNILVMDEPTNHLDM---ESIESLNAALEMYQGT-LIFVSHDREFVSSLATRVI-----EITPE 511
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMvmdngQIVET 233
|
...
gi 490523037 512 RVV 514
Cdd:PRK10419 234 QPV 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
2.56e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNE----RIGK 68
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsPRDaialGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 LRQDqFA-FEQYTVLDTVIMGHSELWEV----KQERDRIyslPEMSEEDGYKVaDLEVKYGEmdgysaesragellLGVG 143
Cdd:COG3845 85 VHQH-FMlVPNLTVAENIVLGLEPTKGGrldrKAARARI---RELSERYGLDV-DPDAKVED--------------LSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 144 iplEQHygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDSTMIIISH 210
Cdd:COG3845 146 ---EQQ-------------RVEILKALYRGARILILDEPTAVLTpqeadelFEILR----RLAAEGKSIIFITH 199
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-211 |
3.35e-11 |
|
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: 63.82 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 10 QFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNERIGKLRQDQFA------- 75
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamSRKELRELRRKKISmvfqsfa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 -FEQYTVLDTVIMGHSELWEVKQERdriyslpemseedgykvadlevkygemdgysaESRAGELLLGVGI-PLEQHYgpM 153
Cdd:cd03294 113 lLPHRTVLENVAFGLEVQGVPRAER--------------------------------EERAAEALELVGLeGWEHKY--P 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDiDTIRWLEQTL-----NDRDSTMIIISHD 211
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRREMQDEllrlqAELQKTIVFITHD 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-211 |
3.64e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 63.02 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQDQFA 75
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlpPHKRpVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQYTVLDTVIMGhselwevkqerdriyslpemseedgykvadLEVKygEMDGYSAESRAGELLLGVGipLEQHYGPM-S 154
Cdd:cd03300 84 FPHLTVFENIAFG------------------------------LRLK--KLPKAEIKERVAEALDLVQ--LEGYANRKpS 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLE---QTLNDR-DSTMIIISHD 211
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKElGITFVFVTHD 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
4.36e-11 |
|
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: 61.95 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFG--SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--PNERIGKLRQDQFAFe 77
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDgvPVSDLEKALSSLISV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 78 qytvldtvimghselweVKQerdRIYSLpemseedgykvadlevkygemdgysaesrAGELLLGVGIPLeqhygpmsevA 157
Cdd:cd03247 80 -----------------LNQ---RPYLF-----------------------------DTTLRNNLGRRF----------S 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITH 155
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-230 |
4.84e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKL-RQDQFAFeQYTV-------LD 83
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLnRAQRKAF-RRDIqmvfqdsIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TVIMGHSELWEVkqeRDRIYSLPEMSEEDgykvadlevkygemdgysAESRAGELLLGVGIPLEQHYGPMSEVAPGWKLR 163
Cdd:PRK10419 101 AVNPRKTVREII---REPLRHLLSLDKAE------------------RLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
320-466 |
4.99e-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: 62.69 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW----------SENAQ--IGYY 387
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditglppHRIARlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYeFDNdLTVFD--WMSQWKqeGDDEQAVRSILGRL--LFS--QDDIKKPAKVLSGGEKgRML-FGKLMMQKPNIL 460
Cdd:COG0410 84 PEGRRI-FPS-LTVEEnlLLGAYA--RRDRAEVRADLERVyeLFPrlKERRRQRAGTLSGGEQ-QMLaIGRALMSRPKLL 158
|
....*.
gi 490523037 461 VMDEPT 466
Cdd:COG0410 159 LLDEPS 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
336-514 |
5.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.28 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK------WSENAQ-----IGYYAQDHEYEFDNDLTVFDW 404
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepiTKENIRevrkfVGLVFQNPDDQIFSPTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 405 MSQWKQEGDDEQAVR---SILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL---- 477
Cdd:PRK13652 101 AFGPINLGLDEETVAhrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELidfl 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 490523037 478 NAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK13652 181 NDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
336-505 |
7.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV-------KWSENA------QIGYYAQDHeyefDNDL--- 399
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepiKYDKKSllevrkTVGIVFQNP----DDQLfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TV-----FDWMSQWKQEGDDEQAVRSILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD---- 470
Cdd:PRK13639 95 TVeedvaFGPLNLGLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmga 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 490523037 471 ---MESIESLNAalemyQG-TLIFVSHDREFVSSLATRV 505
Cdd:PRK13639 174 sqiMKLLYDLNK-----EGiTIIISTHDVDLVPVYADKV 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-506 |
7.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 7.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNG---PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQ 383
Cdd:PRK13650 3 NIIEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 IGYYAQDHEYEFDNDLTVFDWMSQWKQEGDDEQAVRS-------ILGRLLFSQddiKKPAKvLSGGEKGRMLFGKLMMQK 456
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKErvnealeLVGMQDFKE---REPAR-LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 457 PNILVMDEPTNHLD----MESIESLNAALEMYQGTLIFVSHDREFVsSLATRVI 506
Cdd:PRK13650 159 PKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-508 |
1.03e-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: 64.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG-------------DLQP-SAGNVSLDPNERI 66
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 67 GKLRQDQFAFEQYTVLDTVIMGHselwevkqerdriyslpemseedgykvaDLEVKYGEMDGYSAESRAGELLLGVGIPL 146
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGN----------------------------EITLPGGRMAYNAMYLRAKNLLRELQLDA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlndRDSTMIIISHDrhfLNMVc 219
Cdd:TIGR02633 133 DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTeketeilLDIIRDLKA----HGVACVYISHK---LNEV- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 220 thmadldygelrvypgnydeymtaatqarerlladnakkkAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEEVKA 299
Cdd:TIGR02633 205 ----------------------------------------KAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREITS 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 300 SSRQNPfirfeqdKKLFRNALEVEAMTKGFDNGPLFK---NVGLLLEVGEKLAILGANGVGKSTMLKTLVGEL------- 369
Cdd:TIGR02633 245 LYPHEP-------HEIGDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpgkfegn 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 370 ------QPDNGTVKWSENAQIGYYAQDHEYE---------FDNDLTVFDWMSQWKQ--EGDDEQAVRSILGRLLFSQDDI 432
Cdd:TIGR02633 318 vfingkPVDIRNPAQAIRAGIAMVPEDRKRHgivpilgvgKNITLSVLKSFCFKMRidAAAELQIIGSAIQRLKVKTASP 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 433 KKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES---IESLNAALEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
1.04e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV-----SLDPNER-IGKLRQdqf 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRgLLALRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 afeqytvldtvimghsELWEVKQERDRIYSLPEMSEEDGYKVADLEVKYGEMdgysaESRAGELLLGVGiplEQHY--GP 152
Cdd:PRK13638 78 ----------------QVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEI-----TRRVDEALTLVD---AQHFrhQP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNDrdstMIIISHDRHFLNMVCTHMADL 225
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVL 209
|
250
....*....|..
gi 490523037 226 DYGELRVY--PG 235
Cdd:PRK13638 210 RQGQILTHgaPG 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-508 |
1.08e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSenaqiGYYAQDHEYEFDNDLT-VFDWMSQ--Wkqeg 412
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVPFKRRKEFARRIGvVFGQRSQlwW---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 413 D----------------DEQAVRSILGRL--LFSQDDI-KKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES 473
Cdd:COG4586 110 DlpaidsfrllkaiyriPDAEYKKRLDELveLLDLGELlDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 490523037 474 IESLNAAL----EMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:COG4586 190 KEAIREFLkeynRERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-230 |
1.09e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 17 FENISVKFGGGNR-----------------YGLIGANGSGKSTFMKILGGdLQ-PSAGNV--------SLDPNERIgKLR 70
Cdd:COG1135 4 LENLSKTFPTKGGpvtalddvsltiekgeiFGIIGYSGAGKSTLIRCINL-LErPTSGSVlvdgvdltALSERELR-AAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 QD------QFA-FEQYTVLDTV-----IMGHSelwevKQERDRiyslpemseedgykvadlevkygemdgysaesRAGEL 138
Cdd:COG1135 82 RKigmifqHFNlLSSRTVAENValpleIAGVP-----KAEIRK--------------------------------RVAEL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 139 LLGVGIP-LEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IrwLE--QTLNDR-DSTMIIISHD 211
Cdd:COG1135 125 LELVGLSdKADAY-P-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsI--LDllKDINRElGLTIVLITHE 200
|
250
....*....|....*....
gi 490523037 212 RHFLNMVCTHMADLDYGEL 230
Cdd:COG1135 201 MDVVRRICDRVAVLENGRI 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-473 |
1.24e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNG----------TVKWS---------E 380
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREgrlardirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 381 NAQIGYYAQdhEYEFDNDLTVFD------------WMS--QWKQEGDDEQAVRSI--LGRLLFSQDDIkkpaKVLSGGEK 444
Cdd:PRK09984 85 RANTGYIFQ--QFNLVNRLSVLEnvligalgstpfWRTcfSWFTREQKQRALQALtrVGMVHFAHQRV----STLSGGQQ 158
|
170 180
....*....|....*....|....*....
gi 490523037 445 GRMLFGKLMMQKPNILVMDEPTNHLDMES 473
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPES 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-529 |
1.25e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 61.48 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDheyefdnd 398
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldSLRRAIGVVPQD-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 lTV-FDwmsqwkqegddeqavRSIL-----GRLLFSQDDIKKPAKV------------------------LSGGEKGRML 448
Cdd:cd03253 84 -TVlFN---------------DTIGyniryGRPDATDEEVIEAAKAaqihdkimrfpdgydtivgerglkLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 449 FGKLMMQKPNILVMDEPTNHLDMESIESLNAALE-MYQG-TLIFVSHDREFVSSlATRVIEITPERVVDfSGGYEDYLRS 526
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRdVSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE-RGTHEELLAK 225
|
...
gi 490523037 527 KGI 529
Cdd:cd03253 226 GGL 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-505 |
1.35e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFD----NgplfKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsenaqigyyaQDHEYE 394
Cdd:COG3845 5 ALELRGITKRFGgvvaN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI----------DGKPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 FDN--------------------DLTVFD-----------WMSQWKQEgddEQAVRSILGRLLFSQDdikkP-AKV--LS 440
Cdd:COG3845 71 IRSprdaialgigmvhqhfmlvpNLTVAEnivlgleptkgGRLDRKAA---RARIRELSERYGLDVD----PdAKVedLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 441 GGEKGR--MLfgKLMMQKPNILVMDEPTNHLDMESIESLNAALEMY--QG-TLIFVSHD-REfVSSLATRV 505
Cdd:COG3845 144 VGEQQRveIL--KALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHKlRE-VMAIADRV 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-242 |
1.42e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.97 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIgklrqdqfafEQYtvlDTVIMgHSEL 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPL----------VQY---DHHYL-HRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 93 WEVKQE--------RDRI-YSLPEMSEEDGYKVADLEvkygemdgySAESRAGELLLGVGIPLEQHYGPMSevaPGWKLR 163
Cdd:TIGR00958 558 ALVGQEpvlfsgsvRENIaYGLTDTPDEEIMAAAKAA---------NAHDFIMEFPNGYDTEVGEKGSQLS---GGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHDRHFLNMvCTHMADLDYGELrVYPGNYDEYMT 242
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGTHKQLME 702
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
334-505 |
1.62e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 334 LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------------ENAQIGYYAQDHEyeFDND 398
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelRNQKLGFIYQFHH--LLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 LTVFDWMSQ-----WKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM-- 471
Cdd:PRK11629 102 FTALENVAMplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDArn 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 490523037 472 -ESIESLNAALEMYQGT-LIFVSHDREFVSSLATRV 505
Cdd:PRK11629 181 aDSIFQLLGELNRLQGTaFLVVTHDLQLAKRMSRQL 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-514 |
2.19e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.66 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 307 IRFEQDKKLF---RNALEveamtkgfdngplfkNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------- 376
Cdd:PRK10908 2 IRFEHVSKAYlggRQALQ---------------GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 377 ---KWSE----NAQIGYYAQDHEYEFDNdlTVFDWMS-----QWKQEGDDEQAVRSILGR--LLfsqDDIKKPAKVLSGG 442
Cdd:PRK10908 67 trlKNREvpflRRQIGMIFQDHHLLMDR--TVYDNVAipliiAGASGDDIRRRVSAALDKvgLL---DKAKNFPIQLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 443 EKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
320-508 |
2.23e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQDHEYEFdNDL 399
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMF-QDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TVFDWMS-----------QWKQEGddEQAVRSIlGRLLFSQDdikKPAkVLSGGEKGRMLFGKLMMQKPNILVMDEPTNH 468
Cdd:PRK11247 91 RLLPWKKvidnvglglkgQWRDAA--LQALAAV-GLADRANE---WPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490523037 469 LD------MES-IESLnaaLEMYQGTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK11247 164 LDaltrieMQDlIESL---WQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
349-511 |
2.32e-10 |
|
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: 60.31 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 349 AILGANGVGKSTMLK----TLVGELQPDNGTVKWS-----ENAQIGYYaqdhEYEFDNDltvfdwmsqwkqEGDDEQAVR 419
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDpklirEGEVRAQV----KLAFENA------------NGKKYTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 420 S--ILGRLLF-SQDDIKKPA----KVLSGGEKgrMLFG--------KLMMQKPNILVMDEPTNHLDMESIE-SLNAALEM 483
Cdd:cd03240 90 SlaILENVIFcHQGESNWPLldmrGRCSGGEK--VLASliirlalaETFGSNCGILALDEPTTNLDEENIEeSLAEIIEE 167
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 484 YQGTLIF----VSHDREFVsSLATRVIEITPE 511
Cdd:cd03240 168 RKSQKNFqlivITHDEELV-DAADHIYRVEKD 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
320-495 |
2.81e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW---SENAQIGYYAQD-----H 391
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqSIKKDLCTYQKQlcfvgH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 392 EYEFDNDLTV-----FDWMSQWKQEGDDEqavrsiLGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK13540 82 RSGINPYLTLrenclYDIHFSPGAVGITE------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 467 NHLDMESIESLNAALEMYQ---GTLIFVSHDR 495
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-210 |
2.88e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 9 MQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKlrqdqfafeqytvldtvimg 88
Cdd:PRK13637 16 TPFEKKAL-DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK-------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 HSELWEVKQERDRIYSLPE--MSEEDGYKvadlEVKYGEMD-GYSAE---SRAGELLLGVGIPLEQhYGPMS--EVAPGW 160
Cdd:PRK13637 75 KVKLSDIRKKVGLVFQYPEyqLFEETIEK----DIAFGPINlGLSEEeieNRVKRAMNIVGLDYED-YKDKSpfELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLDI---DTIRWLEQTLNDR-DSTMIIISH 210
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPkgrDEILNKIKELHKEyNMTIILVSH 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-187 |
2.99e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.16 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQ 71
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvpPYQRpINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVIMGhselweVKQERdriysLPEmseedgykvadlevkyGEMdgysaESRAGELLLGVGIPLEQHYG 151
Cdd:PRK11607 99 SYALFPHMTVEQNIAFG------LKQDK-----LPK----------------AEI-----ASRVNEMLGLVHMQEFAKRK 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 490523037 152 PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK11607 147 P-HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-514 |
3.09e-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: 60.29 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA----- 382
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 383 -QIGYYAQdhEYEFDNDLTVFD----WMSQWKQEGDD-EQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQK 456
Cdd:cd03258 82 rRIGMIFQ--HFNLLSSRTVFEnvalPLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQ-LSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 457 PNILVMDEPTNHLDMESIES-------LNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSilallrdINRELGL---TIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-471 |
3.30e-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: 63.01 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSenAQIGYYAQdheyefdndltvFDWMSQWKQEG 412
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--GRISFSPQ------------TSWIMPGTIKD 505
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 413 D-------DEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM 471
Cdd:TIGR01271 506 NiifglsyDEYRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-525 |
3.34e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHDrhfLNMVcthmadldygelr 231
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilQLLRELQQELN---MGLLFITHN---LSIV------------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 232 vypgnydeymtaatqareRLLADNAK--KKAQIADLQSFVSRFSANASKSRQATSRARQIDkiklEEVKASSRQNPFIRF 309
Cdd:PRK15134 221 ------------------RKLADRVAvmQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSG----DPVPLPEPASPLLDV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 310 EQDKKLF--RNALeveaMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLV------GELQPDNGTV-KWSE 380
Cdd:PRK15134 279 EQLQVAFpiRKGI----LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIWFDGQPLhNLNR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 381 NA------QIGYYAQDHEYEFDNDLTVFdwmsQWKQEG-----------DDEQAVRSILGRLLFSQDDIKKPAKVLSGGE 443
Cdd:PRK15134 355 RQllpvrhRIQVVFQDPNSSLNPRLNVL----QIIEEGlrvhqptlsaaQREQQVIAVMEEVGLDPETRHRYPAEFSGGQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 444 KGRMLFGKLMMQKPNILVMDEPTNHLD---MESIESLNAAL-EMYQGTLIFVSHDREFVSSLATRVIEITPERVVD---- 515
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEqgdc 510
|
410
....*....|...
gi 490523037 516 ---FSGGYEDYLR 525
Cdd:PRK15134 511 ervFAAPQQEYTR 523
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
319-516 |
3.40e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaQIGyyaqDHEYEFDND 398
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------NIA----GHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 LT-------------VFDWMSQW--------------------KQEGDDEQAvrSILGRLLFSQDDIKKPAKvLSGGEKG 445
Cdd:COG4161 72 PSekairllrqkvgmVFQQYNLWphltvmenlieapckvlglsKEQAREKAM--KLLARLRLTDKADRFPLH-LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 446 RMLFGKLMMQKPNILVMDEPTNHLDME-SIESLNAALEMYQG--TLIFVSHDREFVSSLATRVIEITPERVVDF 516
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-210 |
3.60e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSaGNVSldpneriGKLRQDQFAFEQYTVLDT- 84
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH-GTYE-------GEIIFEGEELQASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 ----VIMgHSELWEVkqerdriyslPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQhYGPMSEVAPGW 160
Cdd:PRK13549 81 ragiAII-HQELALV----------KELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINP-ATPVGNLGLGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-210 |
4.79e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNErigklrqdqfafeqYTVLDTV 85
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN--------------YNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 IMGHSELWEVKQERDRIyslPEMSEEDGYKVADLEVK---------YGEMdgysaESRAGELLLGVGI--PLEQHYGPMS 154
Cdd:PRK09700 76 LAAQLGIGIIYQELSVI---DELTVLENLYIGRHLTKkvcgvniidWREM-----RVRAAMMLLRVGLkvDLDEKVANLS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 155 evaPGWKLRVLLAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK09700 148 ---ISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
316-470 |
4.80e-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: 59.10 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 316 FRNaLEVEAMTK-GFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQP--DNGTV--------KWSENAQI 384
Cdd:cd03213 6 FRN-LTVTVKSSpSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVlingrpldKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 385 GYYAQD---HEYefdndLTVfdwmsqwkqegddEQAvrsilgrLLFSqddikkpAKV--LSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03213 85 GYVPQDdilHPT-----LTV-------------RET-------LMFA-------AKLrgLSGGERKRVSIALELVSNPSL 132
|
170
....*....|.
gi 490523037 460 LVMDEPTNHLD 470
Cdd:cd03213 133 LFLDEPTSGLD 143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-211 |
4.85e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 7 VTMQFGSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFAFeqytvldtvi 86
Cdd:PRK15056 14 VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 87 mghselweVKQERDRIYSLPEMSEEdgykvADLEVKYGEMdGY----SAESRA--GELLLGVGIpLEQHYGPMSEVAPGW 160
Cdd:PRK15056 83 --------VPQSEEVDWSFPVLVED-----VVMMGRYGHM-GWlrraKKRDRQivTAALARVDM-VEFRHRQIGELSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
5.09e-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: 59.08 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSAGNVSLDpNERIGKLRQDqfafeqy 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK-GEDITDLPPE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 tvldtvimghselwevkqERDR--IYSLPEMSEE-DGYKVADL--EVKYGemdgYSAesraGElllgvgipleqhygpms 154
Cdd:cd03217 73 ------------------ERARlgIFLAFQYPPEiPGVKNADFlrYVNEG----FSG----GE----------------- 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 155 evapgwKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:cd03217 110 ------KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINklrEEGKSVLIITHYQRLLDYI 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
320-519 |
5.21e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGP----LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS-------ENAQIGYYA 388
Cdd:PRK10535 5 LELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgqdvatlDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDH------EYEFDNDLT---------VFDWMSQWKQEgddeQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLM 453
Cdd:PRK10535 85 REHfgfifqRYHLLSHLTaaqnvevpaVYAGLERKQRL----LRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 454 MQKPNILVMDEPTNHLDMESIESLNAALEMY--QG-TLIFVSHDREfVSSLATRVIEITPERVVDFSGG 519
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLrdRGhTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPA 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-210 |
5.42e-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: 59.86 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKP---LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKL----RQDQFAF- 76
Cdd:cd03249 4 KNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD-GVDIRDLnlrwLRSQIGLv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 EQYTVL-DTVImghselwevkqeRDRI-YSLPEMSEEDGYKVADL----EVKYGEMDGYsaESRAGElllgvgipleqhY 150
Cdd:cd03249 83 SQEPVLfDGTI------------AENIrYGKPDATDEEVEEAAKKanihDFIMSLPDGY--DTLVGE------------R 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 151 GpmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03249 137 G--SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRamKGRTTIVIAH 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-233 |
5.56e-10 |
|
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: 59.37 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPnERIGKLRQDQFA-------------FEQYTVLDTVIMGHSELW--EV 95
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-RDITGLPPHERAragigyvpegrriFPELTVEENLLLGAYARRraKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 96 KQERDRIYSL-PEMSEEdgykvadlevkygemdgysAESRAGELLLGvgiplEQHygpMsevapgwklrVLLAQALFSNP 174
Cdd:cd03224 109 KARLERVYELfPRLKER-------------------RKQLAGTLSGG-----EQQ---M----------LAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 175 DILLLDEPTNNL------DI-DTIRwleqTLNDRDSTMIIISHDRHFlnmvCTHMADldygelRVY 233
Cdd:cd03224 152 KLLLLDEPSEGLapkiveEIfEAIR----ELRDEGVTILLVEQNARF----ALEIAD------RAY 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-211 |
5.74e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.41 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnerigklrqdQFAFEQYTVldtvimghsel 92
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----------GMVLSEETV----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 93 WEVKQERDRIYSLPEmSEEDGYKVADlEVKYG-EMDGYSAES---RAGELLLGVGIPLEQHYGPmSEVAPGWKLRVLLAQ 168
Cdd:PRK13635 77 WDVRRQVGMVFQNPD-NQFVGATVQD-DVAFGlENIGVPREEmveRVDQALRQVGMEDFLNREP-HRLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 169 ALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMIIISHD 211
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKG---ITVLSITHD 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-514 |
5.86e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQDHEYE--- 394
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 -----FDN-----DLTVFDWMSQWKQEGDD--EQAVRS-ILGRL----LFSQDDIkKPAKvLSGGEKGRMLFGKLMMQKP 457
Cdd:PRK11831 85 rmsmlFQSgalftDMNVFDNVAYPLREHTQlpAPLLHStVMMKLeavgLRGAAKL-MPSE-LSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 458 NILVMDEP-------TNHLDMESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK11831 163 DLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
6.21e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpnERIGKLRqdqfafeqyt 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR--MRDGQLR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vlDTVIMGHSelwevkqERDRIyslpeMSEEDGYkvadleVKYGEMDGY----SAESRAGELLLGVGiplEQHYGPMSEV 156
Cdd:PRK11701 74 --DLYALSEA-------ERRRL-----LRTEWGF------VHQHPRDGLrmqvSAGGNIGERLMAVG---ARHYGDIRAT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 157 APGWKLRVLLAQA----------------------LFSNPDILLLDEPTNNLDI-------DTIRWLEQTLndrDSTMII 207
Cdd:PRK11701 131 AGDWLERVEIDAAriddlpttfsggmqqrlqiarnLVTHPRLVFMDEPTGGLDVsvqarllDLLRGLVREL---GLAVVI 207
|
....
gi 490523037 208 ISHD 211
Cdd:PRK11701 208 VTHD 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-210 |
6.84e-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: 59.04 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--PNERIG--KLR-------QD 72
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvDISKIGlhDLRsrisiipQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 73 QFAFE-----------QYTvlDtvimghSELWEVKQE---RDRIYSLPEMseedgykvADLEVKYGEmDGYSAesragel 138
Cdd:cd03244 87 PVLFSgtirsnldpfgEYS--D------EELWQALERvglKEFVESLPGG--------LDTVVEEGG-ENLSV------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 139 llgvgipleqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03244 143 --------------------GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
316-493 |
6.94e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.33 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 316 FRNALEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQ 383
Cdd:COG1132 336 VRGEIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirdltleSLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 384 IGYYAQDHeyefdndlTVFDwmsqwkqegddeqavRSI-----LGRLLFSQDDIKKPAKV-------------------- 438
Cdd:COG1132 416 IGVVPQDT--------FLFS---------------GTIrenirYGRPDATDEEVEEAAKAaqahefiealpdgydtvvge 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 439 ----LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL-EMYQG-TLIFVSH 493
Cdd:COG1132 473 rgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALeRLMKGrTTIVIAH 533
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-210 |
7.96e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 59.16 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSK-PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN-----------ERIGKLRQDQ 73
Cdd:cd03254 7 NVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 74 FAFEQyTVLDTVIMGHS--------ELWEVKQERDRIYSLPemseeDGYkvadlevkygemdgYSAESRAGELLlgvgip 145
Cdd:cd03254 87 FLFSG-TIMENIRLGRPnatdeeviEAAKEAGAHDFIMKLP-----NGY--------------DTVLGENGGNL------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 146 leqhygpmSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRdsTMIIISH 210
Cdd:cd03254 141 --------SQ---GERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGR--TSIIIAH 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-496 |
9.40e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.87 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSenAQIGYYAQdheyefdndltvFDW-MSQWKQE 411
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--GRISFSSQ------------FSWiMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 412 G------DDEQAVRSILGRLLFSQDDIKKPAK----------VLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM---- 471
Cdd:cd03291 117 NiifgvsYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftek 196
|
170 180
....*....|....*....|....*
gi 490523037 472 ESIESLNAALeMYQGTLIFVSHDRE 496
Cdd:cd03291 197 EIFESCVCKL-MANKTRILVTSKME 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
326-506 |
9.76e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 326 TKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVG-------ELQPDNGTVKWSENAQ--IGYYAQdhEYEFD 396
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgDLFIGEKRMNDVPPAErgVGMVFQ--SYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 397 NDLTVFDWMS-------QWKQEGDD--EQAVRSI-LGRLLfsqddIKKPaKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK11000 88 PHLSVAENMSfglklagAKKEEINQrvNQVAEVLqLAHLL-----DRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490523037 467 NHLD------MES-IESLNAALemyQGTLIFVSHDREFVSSLATRVI 506
Cdd:PRK11000 162 SNLDaalrvqMRIeISRLHKRL---GRTMIYVTHDQVEAMTLADKIV 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
320-506 |
1.50e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.96 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYAQd 390
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaENRHVNTVFQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 hEYEFDNDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEP 465
Cdd:PRK09452 94 -SYALFPHMTVFENVAfglrmQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ-LSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490523037 466 TNHLD------MES-IESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:PRK09452 172 LSALDyklrkqMQNeLKALQRKLGI---TFVFVTHDQEEALTMSDRIV 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-210 |
1.51e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLQPS---AGNVSLD------PNERIGKL 69
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNghniysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQD-QFAFEQ-----YTVLDTVIMGhselWEVKQERDRiYSLPEMSEED--GYKVADlEVKYGEMDgySAESRAGelllg 141
Cdd:PRK14239 85 RKEiGMVFQQpnpfpMSIYENVVYG----LRLKGIKDK-QVLDEAVEKSlkGASIWD-EVKDRLHD--SALGLSG----- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 142 vgipleqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK14239 152 -----------------GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGlkDDYTMLLVTR 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-187 |
1.60e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 58.88 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSL--------DPNERIGKLRQD-----QFAFEQytvldtv 85
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagKKNKKLKPLRKKvgivfQFPEHQ------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 imghseLWEVKQERDrIYSLPE---MSEEDgykvadlevkygemdgysAESRAGELLLGVGIPLE-QHYGPMsEVAPGWK 161
Cdd:PRK13634 98 ------LFEETVEKD-ICFGPMnfgVSEED------------------AKQKAREMIELVGLPEElLARSPF-ELSGGQM 151
|
170 180
....*....|....*....|....*.
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
319-506 |
1.81e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.97 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-------SENAQIGY----- 386
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYlpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 --YAqdheyefdnDLTVFD---WMSQWK--QEGDDEQAVRSILGRLlfsqdDI----KKPAKVLSGGekgrmlfgklMMQ 455
Cdd:COG4152 81 glYP---------KMKVGEqlvYLARLKglSKAEAKRRADEWLERL-----GLgdraNKKVEELSKG----------NQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 456 K----------PNILVMDEPTNHLD-------MESIESLNAalemyQG-TLIFVSHDREFVSSLATRVI 506
Cdd:COG4152 137 KvqliaallhdPELLILDEPFSGLDpvnvellKDVIRELAA-----KGtTVIFSSHQMELVEELCDRIV 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-210 |
1.83e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.95 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF------GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPnerigklrqdqf 74
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 75 afeqytvLDTVIMGHseLWEVKQERDRIYSLPE------MSEEDgykvadleVKYG-EMDGYSAE---SRAGELLLGVGI 144
Cdd:PRK13633 72 -------LDTSDEEN--LWDIRNKAGMVFQNPDnqivatIVEED--------VAFGpENLGIPPEeirERVDESLKKVGM 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 145 PLEQHYGPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRwleqTLNDRDS-TMIIISH 210
Cdd:PRK13633 135 YEYRRHAP-HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIK----ELNKKYGiTIILITH 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-493 |
2.05e-09 |
|
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: 58.01 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW-----------SENAQIGYYAQDhEYEFDNd 398
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaSLRRQIGLVSQD-VFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 lTVFDWMSQWKQEGDDEQAVRSilGRLLFSQDDIKK-PAKV----------LSGGEKGRMLFGKLMMQKPNILVMDEPTN 467
Cdd:cd03251 91 -TVAENIAYGRPGATREEVEEA--ARAANAHEFIMElPEGYdtvigergvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180
....*....|....*....|....*...
gi 490523037 468 HLDMESIESLNAALE--MYQGTLIFVSH 493
Cdd:cd03251 168 ALDTESERLVQAALErlMKNRTTFVIAH 195
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-210 |
2.09e-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: 57.94 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER----IGKL 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpMHKRarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTVLDTVIMGHSELWEVKQERdriyslpemseedgykvadlevkygemdgysaESRAGELLLGVGI-PLEQ 148
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKER--------------------------------EEKLEELLEEFHItHLRK 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 149 HYGpmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISH 210
Cdd:cd03218 129 SKA--SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVLITDH 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-521 |
2.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 337 NVGLLLEVGEKLAILGANGVGKSTMLK------------TLVGELQPDNGTVKWSE----NAQIGYYAQDHEYEFDNDLT 400
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEvkrlRKEIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VFDWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD------ 470
Cdd:PRK13645 109 EKDIAFGPVNLGENKQEAYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeed 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 471 -MESIESLNaalEMYQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYE 521
Cdd:PRK13645 189 fINLFERLN---KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
310-470 |
2.43e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 310 EQDKKLFRNALEVEAMTKGfdngpLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVG------ELQPD---NGT-VKWS 379
Cdd:TIGR00955 21 KQLVSRLRGCFCRERPRKH-----LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspkgvKGSGSvllNGMpIDAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 380 ENAQIGYYAQDHEYeFDNDLTVFD---WMSQWK---QEGDDE--QAVRSILGRL-LFSQDD--IKKPA--KVLSGGEKGR 446
Cdd:TIGR00955 96 EMRAISAYVQQDDL-FIPTLTVREhlmFQAHLRmprRVTKKEkrERVDEVLQALgLRKCANtrIGVPGrvKGLSGGERKR 174
|
170 180
....*....|....*....|....
gi 490523037 447 MLFGKLMMQKPNILVMDEPTNHLD 470
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-211 |
2.82e-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: 57.26 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVS--------LDPNER-IGKLRQDQFAF 76
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 EQYTVLDTVIMGhseLWEVKQERDRIyslpemsEEDGYKVADlevkygemdgysaesragelLLGVGIPLEQHYGPMSEv 156
Cdd:cd03301 85 PHMTVYDNIAFG---LKLRKVPKDEI-------DERVREVAE--------------------LLQIEHLLDRKPKQLSG- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 157 apGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQTLNdrdSTMIIISHD 211
Cdd:cd03301 134 --GQRQRVALGRAIVREPKVFLMDEPLSNLDAklrvqmrAELKRLQQRLG---TTTIYVTHD 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-235 |
2.93e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 57.28 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 3 VTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSAGNVS---------LDPNE---RIGKLR 70
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilfngqpRKPDQfqkCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 QDQFAFEQYTVLDTV-IMGHSELWEVKQERDRIYSLPEMSEEDgykVADLEVkygemdgysaesrAGELLLGVGIpleqh 149
Cdd:cd03234 88 QDDILLPGLTVRETLtYTAILRLPRKSSDAIRKKRVEDVLLRD---LALTRI-------------GGNLVKGISG----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 150 ygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHD------RHFlnmvcT 220
Cdd:cd03234 147 ---------GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlarRNRIVILTIHQprsdlfRLF-----D 212
|
250
....*....|....*
gi 490523037 221 HMADLDYGELrVYPG 235
Cdd:cd03234 213 RILLLSSGEI-VYSG 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-465 |
2.97e-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: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KW--SENAQ--IGYY 387
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLpmHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEYeFdNDLTVFD-WMSQWKQEGDDEQAVRSILGRLL--FSQDDI-KKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:cd03218 81 PQEASI-F-RKLTVEEnILAVLEIRGLSKKEREEKLEELLeeFHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 490523037 464 EP 465
Cdd:cd03218 159 EP 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-210 |
3.19e-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: 57.04 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGK-----LRQDQFAFEQYTVLdtvIMGh 89
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-GIDISTipledLRSSLTIIPQDPTL---FSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 90 selwEVKQERDRiysLPEMSEEDGYKVadLEVKYGemdgysaesragelllgvGIPLEQhygpmsevapGWKLRVLLAQA 169
Cdd:cd03369 97 ----TIRSNLDP---FDEYSDEEIYGA--LRVSEG------------------GLNLSQ----------GQRQLLCLARA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490523037 170 LFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREefTNSTILTIAH 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-210 |
3.26e-09 |
|
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: 57.12 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLfeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQDQFA 75
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaapPADRpVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQYTVLDTVIMGHS---ELWEVKQERdriyslpemseedgykvadLEVKYGEMDGYSAESRAGELLLGvgipleqhygp 152
Cdd:cd03298 82 FAHLTVEQNVGLGLSpglKLTAEDRQA-------------------IEVALARVGLAGLEKRLPGELSG----------- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 153 msevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISH 210
Cdd:cd03298 132 ------GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhaeTKMTVLMVTH 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-515 |
3.44e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 334 LFkNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA----------QIGYYAQD-----HEYEFDND 398
Cdd:PRK11124 18 LF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdkAIRELRRNvgmvfQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 LTVFDWMSQ--WKQEG-DDEQAV---RSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDME 472
Cdd:PRK11124 97 LTVQQNLIEapCRVLGlSKDQALaraEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 473 SIESLNAALEMYQGTLI---FVSHDREFVSSLATRVIEITPERVVD 515
Cdd:PRK11124 176 ITAQIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-218 |
3.87e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.38 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSAGNVSLD--------PNER----IG 67
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDgedilelsPDERaragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 68 klrqdqFAFeQYTVldtvimghselwEVKqerdriyslpemseedGYKVADL------EVKYGEMDGYSAESRAGELLLG 141
Cdd:COG0396 81 ------LAF-QYPV------------EIP----------------GVSVSNFlrtalnARRGEELSAREFLKLLKEKMKE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 VGIP---LEqhygpmSEVAPGW----KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHD 211
Cdd:COG0396 126 LGLDedfLD------RYVNEGFsggeKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNklrSPDRGILIITHY 199
|
....*..
gi 490523037 212 RHFLNMV 218
Cdd:COG0396 200 QRILDYI 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
320-523 |
4.50e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA----------QIGYYAQ 389
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarltpakahQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHEYEFDNDLTVfdwmsqwkQEG---------DDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK15439 92 PQEPLLFPNLSV--------KENilfglpkrqASMQKMKQLL-AALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 461 VMDEPTNHLDMESIESLNAALEMYQGT---LIFVSHDREFVSSLATRvIEITPERVVDFSGGYEDY 523
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADR-ISVMRDGTIALSGKTADL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
318-504 |
4.62e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNG----PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENAQIG 385
Cdd:PRK10584 5 NIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 386 YYAQDHEYEFDNDLTV----------FDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQ 455
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIptlnalenveLPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 456 KPNILVMDEPTNHLDMESIE-------SLNaalEMYQGTLIFVSHDrefvSSLATR 504
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDkiadllfSLN---REHGTTLILVTHD----LQLAAR 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-211 |
5.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAgnvslDPNERIgklrqdqfafeqytVLDTVIMGHSELW 93
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKI--------------TVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 94 EVKQERDRIYSLPEmSEEDGYKVADlEVKYGemdgysAESRA----------GELLLGVGIPLEQHYGPmSEVAPGWKLR 163
Cdd:PRK13640 81 DIREKVGIVFQNPD-NQFVGATVGD-DVAFG------LENRAvprpemikivRDVLADVGMLDYIDSEP-ANLSGGQKQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEqtlNDRDSTMIIISHD 211
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDpagkeqiLKLIRKLK---KKNNLTVISITHD 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
5.76e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.78 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGklrq 71
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtdlpPKDRnIA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 dqFAFEQY------TVLDTV-----IMGHSelwevKQERDRiyslpemseedgyKVADLevkygemdgysAEsragelLL 140
Cdd:COG3839 79 --MVFQSYalyphmTVYENIafplkLRKVP-----KAEIDR-------------RVREA-----------AE------LL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 141 GVGiPLEQHYgPmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:COG3839 122 GLE-DLLDRK-P-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-514 |
5.91e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQdqfaf 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 eqytVLDTVIMGHSELWEVK-QERDRIYSLPEMSEED----GYKVADLEVKYGEMDGYSAESRAGELLLGVGIPLEQ--- 148
Cdd:PRK10261 87 ----VIELSEQSAAQMRHVRgADMAMIFQEPMTSLNPvftvGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 149 ----HygpmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------DTIRWLEQtlnDRDSTMIIISHDRHFLNM 217
Cdd:PRK10261 163 srypH-----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaqilQLIKVLQK---EMSMGVIFITHDMGVVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 218 VCTHMADLDYGElRVYPGNYDEYMTAATQARER-LLAdnAKKKAQIADLQSFVSRFSANASKSRQATSRARQIDKIKLEE 296
Cdd:PRK10261 235 IADRVLVMYQGE-AVETGSVEQIFHAPQHPYTRaLLA--AVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 297 VKASSRqNPFIRFEQDKKLF-RNALEVEAMtkgfdngplfKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGT 375
Cdd:PRK10261 312 PILQVR-NLVTRFPLRSGLLnRVTREVHAV----------EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 376 VKW--------------SENAQIGYYAQDHEYEFDNDLTV-FDWMSQWKQEG--DDEQAVRSI---LGRLLFSQDDIKKP 435
Cdd:PRK10261 381 IIFngqridtlspgklqALRRDIQFIFQDPYASLDPRQTVgDSIMEPLRVHGllPGKAAAARVawlLERVGLLPEHAWRY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 436 AKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMeSIES--LNAALEMYQG---TLIFVSHDREFVSSLATRV----- 505
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDV-SIRGqiINLLLDLQRDfgiAYLFISHDMAVVERISHRVavmyl 539
|
570
....*....|..
gi 490523037 506 ---IEITPERVV 514
Cdd:PRK10261 540 gqiVEIGPRRAV 551
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-231 |
6.08e-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: 58.87 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE---RIGKLRQDQFAFEQYTVLDTVIMGH 89
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 90 SELWEVKqerdRIYSLPEMSEEdgyKVADLEVKYgemdgysaesragellLGVGIPLEQHYGPMSEvapGWKLRVLLAQA 169
Cdd:TIGR01257 2031 EHLYLYA----RLRGVPAEEIE---KVANWSIQS----------------LGLSLYADRLAGTYSG---GNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 170 LFSNPDILLLDEPTNNLDIDTIRWLEQTLND---RDSTMIIISHDRHFLNMVCTHMADLDYGELR 231
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiirEGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-230 |
6.61e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLdpnerigklrqdqfafEQYTVldTVIMGHSELWEVKQ 97
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI----------------AGYHI--TPETGNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 98 ERDRIYSLPE--MSEEDGYKvadlEVKYGEMD-GYS---AESRAGELLLGVGIPLEQHYGPMSEVAPGWKLRVLLAQALF 171
Cdd:PRK13641 86 KVSLVFQFPEaqLFENTVLK----DVEFGPKNfGFSedeAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 172 SNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS---TMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-210 |
6.74e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 56.34 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE-----------RIGKLRQDQFAFEQyTVLDTVI 86
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlaladpawlrrQVGVVLQENVLFNR-SIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 87 MGHSELwevkqERDRIYSLPEMSEEDGYkVADLEVKYGEMDGYSaesragelllGVGIpleqhygpmsevAPGWKLRVLL 166
Cdd:cd03252 98 LADPGM-----SMERVIEAAKLAGAHDF-ISELPEGYDTIVGEQ----------GAGL------------SGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 167 AQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDicAGRTVIIIAH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
303-493 |
7.44e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.30 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 303 QNPFIRF--EQDKKLFRNALEVEAMTKGFDNG--PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK- 377
Cdd:PRK11160 320 QKPEVTFptTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 378 -------WSENA---QIGYYAQdHEYEFDNdlTVFDWMSQWKQEGDDEQAVRSI----LGRLLfsQDD------IKKPAK 437
Cdd:PRK11160 400 ngqpiadYSEAAlrqAISVVSQ-RVHLFSA--TLRDNLLLAAPNASDEALIEVLqqvgLEKLL--EDDkglnawLGEGGR 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 438 VLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESiES--LNAALEMYQG-TLIFVSH 493
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET-ERqiLELLAEHAQNkTVLMITH 532
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-506 |
8.07e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE---------------NAQIGYYAQDHEYEFDNDLT 400
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VFDWMSQWKQEGDDEQAVRSILGRLL----FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES--- 473
Cdd:PRK13646 104 EREIIFGPKNFKMNLDEVKNYAHRLLmdlgFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrq 183
|
170 180 190
....*....|....*....|....*....|....
gi 490523037 474 IESLNAALEMYQG-TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13646 184 VMRLLKSLQTDENkTIILVSHDMNEVARYADEVI 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-493 |
1.01e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.50 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE-----------NAQIGYYAQDHEYeFD----N 397
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlRSSLTIIPQDPTL-FSgtirS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 DLTVFDwmsqwkqEGDDEQavrsilgrlLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESL 477
Cdd:cd03369 101 NLDPFD-------EYSDEE---------IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170
....*....|....*...
gi 490523037 478 NAAL--EMYQGTLIFVSH 493
Cdd:cd03369 165 QKTIreEFTNSTILTIAH 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-504 |
1.03e-08 |
|
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: 54.30 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTVKwsenaqigyyaqdheyEFDNDLTVFDWMSQWKQEGDDEQavrsilgr 424
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------YIDGEDILEEVLDQLLLIIVGGK-------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 425 llfsqddikkpAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQG---------TLIFVSHDR 495
Cdd:smart00382 58 -----------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllkseknlTVILTTNDE 126
|
....*....
gi 490523037 496 EFVSSLATR 504
Cdd:smart00382 127 KDLGPALLR 135
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-183 |
1.13e-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: 55.76 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFA-------------FEQYTVLDTVIMG---HSELWE 94
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GEDITGLPPHRIArlgigyvpegrriFPSLTVEENLLLGayaRRDRAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 95 VKQERDRIYSL-PEMseedgykvadlevkyGEMdgysAESRAGELLLGvgiplEQHygpMseVApgwklrvlLAQALFSN 173
Cdd:COG0410 112 VRADLERVYELfPRL---------------KER----RRQRAGTLSGG-----EQQ---M--LA--------IGRALMSR 154
|
170
....*....|
gi 490523037 174 PDILLLDEPT 183
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-526 |
1.16e-08 |
|
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: 55.77 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK--------WSENA---QIGYY 387
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFidgedireQDPVElrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQD-----HEYEFDNDLTVFDwMSQWKQEGDDEQAVRSI----LGRLLFSQddiKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:cd03295 81 IQQiglfpHMTVEENIALVPK-LLKWPKEKIRERADELLalvgLDPAEFAD---RYPHE-LSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 459 ILVMDEPTNHLDMESIESLNAALEMYQ----GTLIFVSHDREFVSSLATRVIEITPERVVDFsGGYEDYLRS 526
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-GTPDEILRS 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
318-506 |
1.25e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 318 NALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS---------ENAQIGYYA 388
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 389 QDHEYEFDNDLT-VFDWMSQW--------------------KQEGDdEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRM 447
Cdd:PRK10619 84 KNQLRLLRTRLTmVFQHFNLWshmtvlenvmeapiqvlglsKQEAR-ERAVKYLAKVGIDERAQGKYPVH-LSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 448 LFGKLMMQKPNILVMDEPTNHLDMESI-ESLNAALEMYQ--GTLIFVSHDREFVSSLATRVI 506
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVI 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
319-515 |
1.28e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.86 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAqDHEYEFDND 398
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 -----LTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDI----KKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHL 469
Cdd:PRK11248 80 gllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLegaeKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 470 DM---ESIESLnaALEMYQGT---LIFVSHDREFVSSLATRVIEITPE--RVVD 515
Cdd:PRK11248 160 DAftrEQMQTL--LLKLWQETgkqVLLITHDIEEAVFMATELVLLSPGpgRVVE 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-211 |
1.31e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDP--------NER----IGKL 69
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTVLDTvimghseLWEVKQERDriyslpEMSEEdgykvadlevkygemdgySAESRAGELLLGVGIP-LEQ 148
Cdd:PRK10895 84 PQEASIFRRLSVYDN-------LMAVLQIRD------DLSAE------------------QREDRANELMEEFHIEhLRD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 149 HYGpmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDtIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK10895 133 SMG--QSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisvID-IKRIIEHLRDSGLGVLITDHN 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-389 |
1.35e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.17 E-value: 1.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWseNAQIGYYAQ 389
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYVSQ 73
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
320-506 |
1.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.25 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNG-PL----FKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA------------ 382
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 383 -----------------------QIGYYAQDHEYEF-----DNDLtVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKK 434
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrRVGVVFQFAEYQLfeqtiEKDI-IFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 435 PAKVLSGGEKGRM-LFGKLMMQkPNILVMDEPTNHLDME-SIESLNAALEMYQG--TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13651 162 SPFELSGGQKRRVaLAGILAME-PDFLVFDEPTAGLDPQgVKEILEIFDNLNKQgkTIILVTHDLDNVLEWTKRTI 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
340-514 |
1.40e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 340 LLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENaqigyyaQDHEYE----------F-DNDLtvFDWMSQW 408
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNG-------QDHTTTppsrrpvsmlFqENNL--FSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 409 -----------KQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGK-LMMQKPnILVMDEPTNHLD----ME 472
Cdd:PRK10771 90 qniglglnpglKLNAAQREKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARcLVREQP-ILLLDEPFSALDpalrQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490523037 473 SIESLNAALEMYQGTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-513 |
1.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.25 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaqigyYAQDHEYEFDNDLtvfdWMSQWKQ----E 411
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----------YVDGLDTSDEENL----WDIRNKAgmvfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 412 GDDEQAVRSILGR--------LLFSQDDIKK-----------------PAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK13633 93 NPDNQIVATIVEEdvafgpenLGIPPEEIRErvdeslkkvgmyeyrrhAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 467 NHLD-------MESIESLNaalEMYQGTLIFVSH--------DREFVSSLATRVIEITPERV 513
Cdd:PRK13633 173 AMLDpsgrrevVNTIKELN---KKYGITIILITHymeeaveaDRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-530 |
1.46e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 329 FDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA-------------QIGYYAQDHEYE- 394
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalrqQVATVFQDPEQQi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 ----FDNDLTvFDWMSQWKQEGDDEQAVRSILgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD 470
Cdd:PRK13638 91 fytdIDSDIA-FSLRNLGVPEAEITRRVDEAL-TLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 471 MESIESLNAALE--MYQGT-LIFVSHDREFVSSLATRVIEITPERVVDFSGGYEDYLRSKGIE 530
Cdd:PRK13638 169 PAGRTQMIAIIRriVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-506 |
1.88e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 56.26 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 349 AILGANGVGKSTMLKTLVGELQPDNGTVK-----WSENAQ----------IGYYAQD-----HeyefdndLTVFD----- 403
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARgiflpphrrrIGYVFQEarlfpH-------LSVRGnllyg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 404 -WMSQWKQEGDDEQAVRSILG--RLLfsqdDiKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES------- 473
Cdd:COG4148 102 rKRAPRAERRISFDEVVELLGigHLL----D-RRPAT-LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeilpy 175
|
170 180 190
....*....|....*....|....*....|...
gi 490523037 474 IESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG4148 176 LERLRDELDI---PILYVSHSLDEVARLADHVV 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-493 |
2.14e-08 |
|
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: 54.46 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGelqpdngtvkwsenaqigyyaqDHEYEFDNDL 399
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------------------HPKYEVTEGE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TVFDwmsqwkqeGDD----EQAVRSILGRLLFSQDDIKKPA-KV----------LSGGEKGRMLFGKLMMQKPNILVMDE 464
Cdd:cd03217 59 ILFK--------GEDitdlPPEERARLGIFLAFQYPPEIPGvKNadflryvnegFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 465 PTNHLDMESIESLNAALEMYQG---TLIFVSH 493
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-198 |
2.36e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRqDQFAfeqyt 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIRRQR-DEYH----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 vLDTVIMGHseLWEVKqerdriyslPEMSEEDGYKVadlevkYGEMDGYSAESRAGELLLGVGIpLEQHYGPMSEVAPGW 160
Cdd:PRK13538 74 -QDLLYLGH--QPGIK---------TELTALENLRF------YQRLHGPGDDEALWEALAQVGL-AGFEDVPVRQLSAGQ 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTL 198
Cdd:PRK13538 135 QRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-211 |
2.38e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpnerigklrqdqfafeqyTVLDTVIMGHSE 91
Cdd:PRK13647 17 GTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---------------------KVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 92 LWEVKQ-------ERDRIYSlpeMSEEDgykvadlEVKYG----EMDGYSAESRAGELLLGVGIPLEQHYGPMsEVAPGW 160
Cdd:PRK13647 75 KWVRSKvglvfqdPDDQVFS---STVWD-------DVAFGpvnmGLDKDEVERRVEEALKAVRMWDFRDKPPY-HLSYGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
320-514 |
2.57e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkwsenaqiGYYAQDHEYEfdnDL 399
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLR---DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TVF-----------DW-------------------------MSQ-WKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGG 442
Cdd:PRK11701 76 YALseaerrrllrtEWgfvhqhprdglrmqvsaggnigerlMAVgARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 443 EKGRMLFGKLMMQKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPERVV 514
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGLVRELGL---AVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-506 |
3.11e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENA---------------QIGYYAQDHEYE-FDNdl 399
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplrkKVGIVFQFPEHQlFEE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 400 TV-----FDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRM-LFGKLMMQkPNILVMDEPTNHLD--- 470
Cdd:PRK13634 102 TVekdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVaIAGVLAME-PEVLVLDEPTAGLDpkg 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490523037 471 ----MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:PRK13634 181 rkemMEMFYKLHKEKGL---TTVLVTHSMEDAARYADQIV 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
326-506 |
3.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 326 TKGFDNgplfknVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVK---WSENAQ------------IGYYAQD 390
Cdd:PRK13641 20 KKGLDN------ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPEtgnknlkklrkkVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 HEYEFDNDLTVFDWMSQWKQEGDDEQAVRSI----LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK13641 94 PEAQLFENTVLKDVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490523037 467 NHLDMESIESLNAALEMYQG---TLIFVSHDREFVSSLATRVI 506
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVL 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
320-465 |
3.52e-08 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 54.20 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWS----------ENAQ--IGYY 387
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmhERARlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQdhEYEFDNDLTVFD-WMSQWK-QEGDDEQAVRSILGRLL--FSQDDIKK-PAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:TIGR04406 82 PQ--EASIFRKLTVEEnIMAVLEiRKDLDRAEREERLEALLeeFQISHLRDnKAMSLSGGERRRVEIARALATNPKFILL 159
|
...
gi 490523037 463 DEP 465
Cdd:TIGR04406 160 DEP 162
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-505 |
3.91e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKwsENAQIGYYAQDhEYEFDN------------ 397
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK--VDGKVLYFGKD-IFQIDAiklrkevgmvfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 ------DLTVFDWMS-QWKQEG-DDEQAVRSILGRLLFS-------QDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:PRK14246 98 qpnpfpHLSIYDNIAyPLKSHGiKEKREIKKIVEECLRKvglwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 463 DEPTNHLDM---ESIESLNAALEMyQGTLIFVSHDREFVSSLATRV 505
Cdd:PRK14246 178 DEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYV 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-502 |
3.98e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTL--VGELQpdnGTVKwsENAQIGYYAQDhEYE-- 394
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVR--VEGRVEFFNQN-IYErr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 ------------------------FDN---DLTVFDWMSQWKQEGDDEQAVRSilGRLLfsqDDIK----KPAKVLSGGE 443
Cdd:PRK14258 81 vnlnrlrrqvsmvhpkpnlfpmsvYDNvayGVKIVGWRPKLEIDDIVESALKD--ADLW---DEIKhkihKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 444 KGRMLFGKLMMQKPNILVMDEPTNHLDMES---IESLNAALEM-YQGTLIFVSHDREFVSSLA 502
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLrSELTMVIVSHNLHQVSRLS 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
5.27e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE----------RIGKLR 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiaRMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 --QDQFAFEQYTVLDTVImghselweVKQERD-RIYSLPEMSEEDGYKVADLEvkygemdgysAESRAGELLLGVGIpLE 147
Cdd:PRK11300 85 tfQHVRLFREMTVIENLL--------VAQHQQlKTGLFSGLLKTPAFRRAESE----------ALDRAATWLERVGL-LE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490523037 148 QHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEP--------TNNLD--IDTIRwleqtlNDRDSTMIIISHD 211
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELDelIAELR------NEHNVTVLLIEHD 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
5.73e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.31 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD------PNERIGKLRQ----------DQ-FAfeqYTV 81
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikyDKKSLLEVRKtvgivfqnpdDQlFA---PTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 LDTVIMGHSELwevkqerdriySLPEmsEEDGYKVADLEVKYGeMDGYsaESRAGELLLGvgipleqhygpmsevapGWK 161
Cdd:PRK13639 97 EEDVAFGPLNL-----------GLSK--EEVEKRVKEALKAVG-MEGF--ENKPPHHLSG-----------------GQK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLD---IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHD 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-211 |
5.75e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPS-----AGNVSL-DPNERIGKLRQDQFA 75
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagellAGTAPLaEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQYTVLDTVIMGHSELWevkqeRDriyslpemseedgykvADLEVkygeMDGYSAESRAGELllgvgipleqhygPmSE 155
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQW-----RD----------------AALQA----LAAVGLADRANEW-------------P-AA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----------IDTIrWLEQTLndrdsTMIIISHD 211
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdlIESL-WQQHGF-----TVLLVTHD 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-485 |
5.81e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNER------------IGKLRQDQFAFEQYTVLDTVIMGHselwEVKQE 98
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeagIGIIHQELNLIPQLTIAENIFLGR----EFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 99 RDRIySLPEMSEEDGYKVADLEVKygemdgYSAESRAGELLLGvgiplEQHygpMSEVapgwklrvllAQALFSNPDILL 178
Cdd:PRK10762 110 FGRI-DWKKMYAEADKLLARLNLR------FSSDKLVGELSIG-----EQQ---MVEI----------AKVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 179 LDEPTNNL-DIDT------IRwleqTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrvypgnYDEYMTAATQaRERL 251
Cdd:PRK10762 165 MDEPTDALtDTETeslfrvIR----ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF------IAEREVADLT-EDSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 252 ladnakkkaqiadLQSFVSRfsanasksrqatsrarqidkiKLEEvkassrQNPfiRFEQDKKLFRnaLEVEAMTkgfdn 331
Cdd:PRK10762 234 -------------IEMMVGR---------------------KLED------QYP--RLDKAPGEVR--LKVDNLS----- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 332 GPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE------------NAQIGYYAQDHEYE----- 394
Cdd:PRK10762 265 GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGIVYISEDRKRDglvlg 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 ---FDN-DLTVFDWMSQWK---QEGDDEQAVRSILGrlLFsqdDIKKPA-----KVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:PRK10762 345 msvKENmSLTALRYFSRAGgslKHADEQQAVSDFIR--LF---NIKTPSmeqaiGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
490 500
....*....|....*....|...
gi 490523037 463 DEPTNHLDmesiesLNAALEMYQ 485
Cdd:PRK10762 420 DEPTRGVD------VGAKKEIYQ 436
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-487 |
6.74e-08 |
|
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: 53.04 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 327 KGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPD---NGTVKWSEN----------AQIGYYAQDHEy 393
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIpykefaekypGEIIYVSEEDV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 394 eFDNDLTVFDWMS-QWKQEGDdeQAVRSIlgrllfsqddikkpakvlSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDME 472
Cdd:cd03233 94 -HFPTLTVRETLDfALRCKGN--EFVRGI------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170
....*....|....*
gi 490523037 473 SieslnaALEMYQGT 487
Cdd:cd03233 153 T------ALEILKCI 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
6.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLF--ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGnvsldpnerigklrqdQFAFEQYTVLD 83
Cdd:PRK13648 12 NVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG----------------EIFYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 tvimghSELWEVKQERDRIYSLPE---MSEEDGYKVA-DLE---VKYGEMdgysaESRAGELLLGVGIPLEQHYGPMSeV 156
Cdd:PRK13648 76 ------DNFEKLRKHIGIVFQNPDnqfVGSIVKYDVAfGLEnhaVPYDEM-----HRRVSEALKQVDMLERADYEPNA-L 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQtlnDRDSTMIIISHD 211
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDpdarqnlLDLVRKVKS---EHNITIISITHD 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-211 |
7.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNErigkLRQDQfafeqytvldtvimghseLW 93
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL----LTEEN------------------VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 94 EVKQERDRIYSLPEmSEEDGYKVADlEVKYG-EMDGYSAE---SRAGELLLGVGIPLEQHYGPmSEVAPGWKLRVLLAQA 169
Cdd:PRK13650 78 DIRHKIGMVFQNPD-NQFVGATVED-DVAFGlENKGIPHEemkERVNEALELVGMQDFKEREP-ARLSGGQKQRVAIAGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490523037 170 LFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
145-217 |
9.10e-08 |
|
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: 52.61 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 145 PLEQHYGPMS---EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRW-----LEQTLNDRDSTMIIISHDRHFLN 216
Cdd:cd03240 108 PLLDMRGRCSggeKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD 187
|
.
gi 490523037 217 M 217
Cdd:cd03240 188 A 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
331-494 |
9.34e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 331 NGplFKNVGL-LLEVGEKLAILGANGVGKSTMLKTLVGELQPD----NGTVKWSEnaQIGYYA----QDHEYEF-DNDLT 400
Cdd:PRK13409 86 NG--FKLYGLpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyEEEPSWDE--VLKRFRgtelQNYFKKLyNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VfdwmSQWKQ-----------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:PRK13409 162 V----VHKPQyvdlipkvfkgkvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 490523037 464 EPTNHLDMEsiESLNAAL---EMYQG-TLIFVSHD 494
Cdd:PRK13409 238 EPTSYLDIR--QRLNVARlirELAEGkYVLVVEHD 270
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
330-528 |
9.89e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 52.87 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQIGYYAQDheyefdND 398
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGVVLQE------NV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 399 L---TVFDWMSQwkqeGDDEQAVRSIL--GRLLFSQDDIKK-----------PAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:cd03252 87 LfnrSIRDNIAL----ADPGMSMERVIeaAKLAGAHDFISElpegydtivgeQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 463 DEPTNHLDMESIESLNAAL-EMYQG-TLIFVSHDREFVSSlATRVIEITPERVVDfSGGYEDYLRSKG 528
Cdd:cd03252 163 DEATSALDYESEHAIMRNMhDICAGrTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELLAENG 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
1.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKfgGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKlrqdqfafeqytVLDTVIMGHSELWE---- 94
Cdd:PRK13636 26 NINIK--KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-----GK------------PIDYSRKGLMKLREsvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 95 VKQERDRIYSLPEMSEEDGYKVADLEVKYGEMdgysaESRAGELLLGVGIPLEQHyGPMSEVAPGWKLRVLLAQALFSNP 174
Cdd:PRK13636 87 VFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV-----RKRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 175 DILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDE 239
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV-ILQGNPKE 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-188 |
1.06e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.25 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNerigklrqdQFAFEQYTvldtvimghselweVKQ 97
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---------PLHFGDYS--------------YRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 98 ERDR-IYSLPEMSEEDGYKVA---DLEVKYG-EMDGYSAESRAGELLLGVGI-PLEQHYGPMSeVAPGWKLRVLLAQALF 171
Cdd:PRK15112 87 QRIRmIFQDPSTSLNPRQRISqilDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHM-LAPGQKQRLGLARALI 165
|
170
....*....|....*..
gi 490523037 172 SNPDILLLDEPTNNLDI 188
Cdd:PRK15112 166 LRPKVIIADEALASLDM 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-493 |
1.15e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAqigYYAQDHEYEFDN-- 397
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN---YNKLDHKLAAQLgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 -----DLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKV-----------------LSGGEKGRMLFGKLMMQ 455
Cdd:PRK09700 83 giiyqELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMmllrvglkvdldekvanLSISHKQMLEIAKTLML 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 456 KPNILVMDEPTNHLDMESIESLNAALEMYQG---TLIFVSH 493
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISH 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-493 |
1.35e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQD--------- 390
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 391 -HEYEFDNDLTVFD--WMSQWKQEG---DDEQAVRSILGRLLFSQDDIKKPAKV--LSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:PRK11288 85 yQELHLVPEMTVAEnlYLGQLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190
....*....|....*....|....*....|....
gi 490523037 463 DEPTNHLDMESIESLNAALEMY--QGT-LIFVSH 493
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELraEGRvILYVSH 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-211 |
1.44e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKIL------------GGDLQPSAGNV-----SLDPNE 64
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDVLLGGRSIfnyrdVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 65 RIGKLRQDQFAFEQyTVLDTVIMGHselwevkqerdRIYSLPEMSEEDGYkvadlevkygemdgysAESRAGELLLGVGI 144
Cdd:PRK14271 102 RVGMLFQRPNPFPM-SIMDNVLAGV-----------RAHKLVPRKEFRGV----------------AQARLTEVGLWDAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 145 PLEQHYGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRdSTMIIISHD 211
Cdd:PRK14271 154 KDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEfirSLADR-LTVIIVTHN 221
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-216 |
1.68e-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: 52.26 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGD--LQPSAGNVSLD--------PNERIgklRQ 71
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKgqdllelePDERA---RA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVldtVIMGHSE---LWEVKQERDRIYSLPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGvgipleq 148
Cdd:TIGR01978 78 GLFLAFQYPE---EIPGVSNlefLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEGFSG------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 149 hygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLN 216
Cdd:TIGR01978 148 ----------GEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINrlrEPDRSFLIITHYQRLLN 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-198 |
1.85e-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: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNerigklrqdqfafeqytv 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 ldtvimghselwEVKQERDRIY-SLPEMSEEDGYKVAdLEVKYGEMDGYSAESRAG--ELLLGVGIPLEQHYgPMSEVAP 158
Cdd:cd03231 63 ------------PLDFQRDSIArGLLYLGHAPGIKTT-LSVLENLRFWHADHSDEQveEALARVGLNGFEDR-PVAQLSA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490523037 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTL 198
Cdd:cd03231 129 GQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
330-514 |
1.88e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.68 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV-----------KWSENAQI-GYYAQDHEYEF-- 395
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsKLQGIRKLvGIVFQNPETQFvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 ---DNDLTvFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPaKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDME 472
Cdd:PRK13644 93 rtvEEDLA-FGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 473 SIES-LNAALEMYQ--GTLIFVSH--------DREFVSSLATRVIEITPERVV 514
Cdd:PRK13644 171 SGIAvLERIKKLHEkgKTIVYITHnleelhdaDRIIVMDRGKIVLEGEPENVL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-226 |
2.40e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSA-GNVSLDPNERI-----------GKLRQ--------DQ 73
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGsGRIARPAGARVlflpqrpylplGTLREallypataEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 74 FAFEQY-TVLDTVIMGH-SELWEVKQERDRIYSLpemseedgykvadlevkygemdgysaesraGElllgvgiplEQhyg 151
Cdd:COG4178 455 FSDAELrEALEAVGLGHlAERLDEEADWDQVLSL------------------------------GE---------QQ--- 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 152 pmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDR--DSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:COG4178 493 -----------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-506 |
2.63e-07 |
|
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: 53.15 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLF--ENISVKFGGGNRY-----------------GLIGANGSGKS-TFMKILG----GDLQPSaGNVSLD------- 61
Cdd:COG4172 3 SMPLLsvEDLSVAFGQGGGTveavkgvsfdiaagetlALVGESGSGKSvTALSILRllpdPAAHPS-GSILFDgqdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 62 PNERIGKLRQDQFAF---EQYTVLDTVimgHS---ELWEVkqerdriyslpemseedgykvadLEVKYGeMDGYSAESRA 135
Cdd:COG4172 82 SERELRRIRGNRIAMifqEPMTSLNPL---HTigkQIAEV-----------------------LRLHRG-LSGAAARARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 136 GELLLGVGIP-----LEQ--HygpmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIdTIRwlEQTLN-------DR 201
Cdd:COG4172 135 LELLERVGIPdperrLDAypH-----QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQ--AQILDllkdlqrEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 202 DSTMIIISHDrhfLNMVcTHMAD----LDYGELrVYPGNYDEYMTAATQARERLLADnakkkaqiadlqsfvsrfSANAS 277
Cdd:COG4172 207 GMALLLITHD---LGVV-RRFADrvavMRQGEI-VEQGPTAELFAAPQHPYTRKLLA------------------AEPRG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 278 KSRQATSRARQIdkIKLEEVKassrqnpfIRFEQDKKLF-RNALEVEAMtkgfdngplfKNVGLLLEVGEKLAILGANGV 356
Cdd:COG4172 264 DPRPVPPDAPPL--LEARDLK--------VWFPIKRGLFrRTVGHVKAV----------DGVSLTLRRGETLGLVGESGS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 357 GKSTMLKTLVGeLQPDNGTV--------KWSENA--------QIGYyaQDHEYEFDNDLTVFDWMSqwkqEG-------- 412
Cdd:COG4172 324 GKSTLGLALLR-LIPSEGEIrfdgqdldGLSRRAlrplrrrmQVVF--QDPFGSLSPRMTVGQIIA----EGlrvhgpgl 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 413 ---DDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMeSIE----SLNAAL-EMY 484
Cdd:COG4172 397 saaERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVQaqilDLLRDLqREH 475
|
570 580
....*....|....*....|..
gi 490523037 485 QGTLIFVSHDREFVSSLATRVI 506
Cdd:COG4172 476 GLAYLFISHDLAVVRALAHRVM 497
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
345-506 |
2.75e-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: 50.65 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWsENAQIGYyaqdheyefdndltvfdwmsqwkqegddeqavrsilgr 424
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY-------------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 425 llfsqddikKPAKV-LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMEsiESLNAA------LEMYQGTLIFVSHDREF 497
Cdd:cd03222 66 ---------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE--QRLNAArairrlSEEGKKTALVVEHDLAV 134
|
....*....
gi 490523037 498 VSSLATRVI 506
Cdd:cd03222 135 LDYLSDRIH 143
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-226 |
2.78e-07 |
|
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: 50.23 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSAgnvsldpNERIGKLRQDQFAFeqytvldtvimghsel 92
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWG-------SGRIGMPEGEDLLF---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 93 wevkqerdriysLPEMSeedgykvadlevkygemdgYsaesragellLGVGIPLEQHYGPMSEV-APGWKLRVLLAQALF 171
Cdd:cd03223 69 ------------LPQRP-------------------Y----------LPLGTLREQLIYPWDDVlSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 172 SNPDILLLDEPTNNLDIDTIRWLEQTLNDRDSTMIIISHdRHFLNMVCTHMADLD 226
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-514 |
3.12e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 317 RNALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTL--VGELQPD---NGTVK------WSENA--- 382
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEarvEGEVRlfgrniYSPDVdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 383 ----QIGYYAQ-----DHEYEFDNDLTVFDWMSQWKQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKGRMLFG 450
Cdd:PRK14267 82 evrrEVGMVFQypnpfPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 451 KLMMQKPNILVMDEPTNHLD---MESIESLNAALEMyQGTLIFVSHDREFVSSLATRV--------IEITPERVV 514
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVaflylgklIEVGPTRKV 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-241 |
3.21e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.73 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPnerigklrqdqfafeqytvLDTVIMGHSELWEVKQ 97
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-------------------VDIAKISDAELREVRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 98 ER-----DRIYSLPEMSEEDgykvadlEVKYG-EMDGYSAESR---AGELLLGVGIPLEQHYGPmSEVAPGWKLRVLLAQ 168
Cdd:PRK10070 106 KKiamvfQSFALMPHMTVLD-------NTAFGmELAGINAEERrekALDALRQVGLENYAHSYP-DELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 169 ALFSNPDILLLDEPTNNLDIDTIRWLEQTL----NDRDSTMIIISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYM 241
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV-VQVGTPDEIL 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-508 |
3.40e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTL-------VGELQPDNGTVKwSENAQIGYYAQDHE 392
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVN-DPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 393 YEFDNdLTVFDWMSQWKQ------------EGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNIL 460
Cdd:PRK09493 81 MVFQQ-FYLFPHLTALENvmfgplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 461 VMDEPTNHLDME-------SIESLnAALEMyqgTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK09493 159 LFDEPTSALDPElrhevlkVMQDL-AEEGM---TMVIVTHEIGFAEKVASRLIFI 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
3.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsLDPNERIGKlrqdqfafeqy 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 tvldtvimghSELWEVKQ--------ERDRIYSlPEMSEEDGYKVADLevkygEMDGYSAESRAGELLLGVGIPLEQHYG 151
Cdd:PRK13652 71 ----------ENIREVRKfvglvfqnPDDQIFS-PTVEQDIAFGPINL-----GLDEETVAHRVSSALHMLGLEELRDRV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 152 PmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDST--MIIIsHDRHFLNMVcTHMADLDY 227
Cdd:PRK13652 135 P-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVI-FSTHQLDLV-PEMADYIY 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-493 |
3.77e-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: 51.32 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYyaqDHEY------EFDNDLTVFD--- 403
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYlhskvsLVGQEPVLFArsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 404 ------WMSQWKQEGDDEQAVRS-----ILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDME 472
Cdd:cd03248 105 qdniayGLQSCSFECVKEAAQKAhahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|....*
gi 490523037 473 SIESLNAALemYQG----TLIFVSH 493
Cdd:cd03248 185 SEQQVQQAL--YDWperrTVLVIAH 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-493 |
3.81e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.39 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV------------KWSENaQIGYYAQdheyE---FDN 397
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlRWLRS-QIGLVSQ----EpvlFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 dlTVFDWMSQWKQEGDDEQAVRSIlgRLLFSQDDIKK-P----------AKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:cd03249 92 --TIAENIRYGKPDATDEEVEEAA--KKANIHDFIMSlPdgydtlvgerGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180
....*....|....*....|....*....
gi 490523037 467 NHLDMESIESLNAALE--MYQGTLIFVSH 493
Cdd:cd03249 168 SALDAESEKLVQEALDraMKGRTTIVIAH 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-210 |
3.85e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.45 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSA---GNVSLDPnerigklrQDQFAF 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDG--------QDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 EqytvldtvimghseLWEVKQERDRIYSLPE-MSEEDGYKVADLEVKYGEMdgysAESRAgELLLGVGIPLEQHY----- 150
Cdd:PRK14247 76 D--------------VIELRRRVQMVFQIPNpIPNLSIFENVALGLKLNRL----VKSKK-ELQERVRWALEKAQlwdev 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 151 -----GPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK14247 137 kdrldAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLElkKDMTIVLVTH 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
333-506 |
4.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.53 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------SEN-----AQIGYYAQDHEYEF------ 395
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitisKENlkeirKKIGIIFQNPDNQFigatve 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 -------DNDLTVFDWMSQWKQEGDDEQAVRSILgrllfsqddiKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNH 468
Cdd:PRK13632 103 ddiafglENKKVPPKKMKDIIDDLAKKVGMEDYL----------DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490523037 469 LD----MESIESLNAALEMYQGTLIFVSHDREFVsSLATRVI 506
Cdd:PRK13632 173 LDpkgkREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVI 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-269 |
4.93e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPL----FENISVKFGGGNRYGLIGANGSGKS-TFMKILGGDLQPsagnvsldpneriGKLRQDQFA 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP-------------GRVMAEKLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 76 FEQYTVLDTvimghSElwevKQERDRIYSLPEMSEED-----------GYKVAD-LEVKYGemdGYSAE--SRAGELLLG 141
Cdd:PRK11022 70 FNGQDLQRI-----SE----KERRNLVGAEVAMIFQDpmtslnpcytvGFQIMEaIKVHQG---GNKKTrrQRAIDLLNQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 VGIPleqhyGPMS--EVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTLNdrdSTMII 207
Cdd:PRK11022 138 VGIP-----DPASrlDVYPhqlsgGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQKEN---MALVL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 208 ISHDRHFLNMVCTHMADLDYGELrVYPGNYDEYMTAA----TQARERLLADNAKKKAQIADLQSFV 269
Cdd:PRK11022 210 ITHDLALVAEAAHKIIVMYAGQV-VETGKAHDIFRAPrhpyTQALLRALPEFAQDKARLASLPGVV 274
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-511 |
5.50e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.25 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTVK-----------WSENAQIGYYAQDHEYEFDNDLTVFDWMSQWKQEG- 412
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQGi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 413 DDEQAVRSILGRLL-FSQDDIK--KPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD----MESIESLNAALEMYQ 485
Cdd:PRK13642 113 PREEMIKRVDEALLaVNMLDFKtrEPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ 191
|
170 180 190
....*....|....*....|....*....|
gi 490523037 486 GTLIFVSHDREFVSS----LATRVIEITPE 511
Cdd:PRK13642 192 LTVLSITHDLDEAASsdriLVMKAGEIIKE 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-196 |
5.79e-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: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN------------ERIGK 68
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 LRQDQFAFEQYTVLDTVIMG--HSELWEVKQERDRIYSL-PEMseedgykvadlevkygemdgysAESRAgelllgvgip 145
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELfPRL----------------------HERRI---------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 146 leQHYGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQ 196
Cdd:PRK11614 133 --QRAGTMSG---GEQQMLAIGRALMSQPRLLLLDEPSLGLApiiiqqiFDTIEQLRE 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-230 |
5.80e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV--------SLDPNE------RIGKLRQDQFAFEQYTVLDT 84
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltALSEKElrkarrQIGMIFQHFNLLSSRTVFDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 85 VimghselwevkqerdriySLPemseedgykvadLEvkygeMDGYSA---ESRAGELLLGVGIPLEQHYGPmSEVAPGWK 161
Cdd:PRK11153 103 V------------------ALP------------LE-----LAGTPKaeiKARVTELLELVGLSDKADRYP-AQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RD--STMIIISHDRHFLNMVCTHMADLDYGEL 230
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinRElgLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
330-493 |
5.81e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.44 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 330 DNGPLFKNVGLLLEVGEKLA--------------ILGANGVGKSTMLKTLvGELQPD-NGTVKWSENAQIGYYAQdHEY- 393
Cdd:TIGR00954 449 DNGIKFENIPLVTPNGDVLIeslsfevpsgnnllICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQ-RPYm 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 394 ---EFDNDLTVFDWMSQWKQEGDDEQAVRSIL-----GRLL---FSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:TIGR00954 527 tlgTLRDQIIYPDSSEDMKRRGLSDKDLEQILdnvqlTHILereGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 463 DEPTNHLDMESIESLNAALEMYQGTLIFVSH 493
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-210 |
5.96e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERIGKLRQDQFafEQYTVLDTVIMGH-SELW 93
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQD--YQGDEEQNVGMKNvNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 94 EVKQERD-RIYSLPEMSEE---DG-----YKVADLE--------------------VKYGEMDGYSAESRAG-------E 137
Cdd:PTZ00265 1260 LTKEGGSgEDSTVFKNSGKillDGvdicdYNLKDLRnlfsivsqepmlfnmsiyenIKFGKEDATREDVKRAckfaaidE 1339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 138 LLLGVGIPLEQHYGPMSE-VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISH 210
Cdd:PTZ00265 1340 FIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADKTIITIAH 1417
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-215 |
7.03e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 49.78 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 13 SKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLdpNERIGKLrqDQFAFEQY-TVLDTVIMG--- 88
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--PGSIAYV--SQEPWIQNgTIRENILFGkpf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 -HSELWEVKQ----ERDrIYSLPemseeDGykvaDL-EVkyGEMdgysaesragelllgvGIPLEqhyGpmsevapGWKL 162
Cdd:cd03250 93 dEERYEKVIKacalEPD-LEILP-----DG----DLtEI--GEK----------------GINLS---G-------GQKQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWL-EQTLND---RDSTMIIISHDRHFL 215
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGlllNNKTRILVTHQLQLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-211 |
7.41e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQdqfafeqytvldtv 85
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-GENIPAMSR-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 86 imghSELWEVKQERDRIYslpemseEDGYKVADLEVKYGEMDGYSAESRAGELLL---------GVGIPLEQHYGPmSEV 156
Cdd:PRK11831 77 ----SRLYTVRKRMSMLF-------QSGALFTDMNVFDNVAYPLREHTQLPAPLLhstvmmkleAVGLRGAAKLMP-SEL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 157 APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLNDRDS----TMIIISHD 211
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
7.54e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQF-GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPnerigklrqdqfafeqy 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 80 tvLDTVimGHSELWEVKQERDRIYSLPEMS------EED-GYKVADLEVKYGEMdgysaESRAGELLLGVGIPLEQHYGP 152
Cdd:PRK13644 64 --IDTG--DFSKLQGIRKLVGIVFQNPETQfvgrtvEEDlAFGPENLCLPPIEI-----RKRVDRALAEIGLEKYRHRSP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 153 MSeVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT-IRWLE--QTLNDRDSTMIIISHdrhflNMVCTHMAD----L 225
Cdd:PRK13644 135 KT-LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLEriKKLHEKGKTIVYITH-----NLEELHDADriivM 208
|
....*..
gi 490523037 226 DYGELRV 232
Cdd:PRK13644 209 DRGKIVL 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
320-477 |
8.00e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------------SENAQIGYY 387
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpksSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQDHEY--------------EFDNDLTVFDWmSQWKQEGDDeqavrsILGRLLFSQDDiKKPAKVLSGGEKGRMLFGKLM 453
Cdd:PRK10762 85 HQELNLipqltiaeniflgrEFVNRFGRIDW-KKMYAEADK------LLARLNLRFSS-DKLVGELSIGEQQMVEIAKVL 156
|
170 180
....*....|....*....|....*
gi 490523037 454 MQKPNILVMDEPTNHL-DMESiESL 477
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTET-ESL 180
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
320-508 |
1.11e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV----KWSENAQ----IGYYAqdH 391
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDrsrfMAYLG--H 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 392 EYEFDNDLTVFDWMS-----QWKQEGDDEQAVRSILGRLLFSQDDIKKpakvLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK13543 90 LPGLKADLSTLENLHflcglHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490523037 467 NHLDMESIESLNAALEMY---QGTLIFVSHDREFVSSLATRVIEI 508
Cdd:PRK13543 166 ANLDLEGITLVNRMISAHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-211 |
1.59e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFE-----NISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGnvsldpnerigklrqdqfaf 76
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 77 eQYTVLDTVI-MGHSELWEVKQERDRI---YSLPEMS------EEDgykVADLEVKYGEmDGYSAESRAGELLLGVGIPL 146
Cdd:PRK13645 67 -QTIVGDYAIpANLKKIKEVKRLRKEIglvFQFPEYQlfqetiEKD---IAFGPVNLGE-NKQEAYKKVPELLKLVQLPE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 147 EQHYGPMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI----DTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13645 142 DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHN 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
350-493 |
1.65e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 350 ILGANGVGKSTMLKTLVGELQPDNGTVkWSENAQIGYYAQ------DHEYEFDNDLTVFDWMSQWKQEGDDEQAVRSILG 423
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNI-YYKNCNINNIAKpyctyiGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIH 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 424 RLLFsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAALEMYQ---GTLIFVSH 493
Cdd:PRK13541 110 YFKL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKAnsgGIVLLSSH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
340-482 |
1.74e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 340 LLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNG--TVKWSENAQIGYYAQDH--EYEFDNDLTvfDWMSQwkQEGDDE 415
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerQSQFSHITRLSFEQLQKlvSDEWQRNNT--DMLSP--GEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 416 QAVRSILgrllfsQDDIKKPA-------------------KVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIES 476
Cdd:PRK10938 100 RTTAEII------QDEVKDPArceqlaqqfgitalldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
....*.
gi 490523037 477 LNAALE 482
Cdd:PRK10938 174 LAELLA 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
331-480 |
1.75e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 331 NGplFKNVGL-LLEVGEKLAILGANGVGKSTMLKTLVGELQPD----NGTVKWSEnaQIGYYA----QDHEYE-FDNDLT 400
Cdd:COG1245 86 NG--FRLYGLpVPKKGKVTGILGPNGIGKSTALKILSGELKPNlgdyDEEPSWDE--VLKRFRgtelQDYFKKlANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 401 VfdwmSQWKQ-----------------EGDDEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMD 463
Cdd:COG1245 162 V----AHKPQyvdlipkvfkgtvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170
....*....|....*..
gi 490523037 464 EPTNHLDMEsiESLNAA 480
Cdd:COG1245 238 EPSSYLDIY--QRLNVA 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
163-242 |
1.86e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 163 RVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFL-NMVCTHMadLDYGELRVYpGNYDE 239
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITHRLTGLeQFDRICV--MDNGQIIEQ-GTHQE 559
|
...
gi 490523037 240 YMT 242
Cdd:PRK11160 560 LLA 562
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
1.96e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 49.26 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSA---GNVSL----------DPNE-- 64
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGArveGEILLdgediydpdvDVVElr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 65 -RIGKLRQ--DQFAFeqyTVLDTVIMGHselwevkqerdRIYslpemseedGYKvadlevKYGEMDGysaesRAGELLLG 141
Cdd:COG1117 92 rRVGMVFQkpNPFPK---SIYDNVAYGL-----------RLH---------GIK------SKSELDE-----IVEESLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 VGIPleqhygpmSEV-----APGWKL------RVLLAQALFSNPDILLLDEPTNNLD-IDTIRwLEQTLND--RDSTMII 207
Cdd:COG1117 138 AALW--------DEVkdrlkKSALGLsggqqqRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILElkKDYTIVI 208
|
250
....*....|
gi 490523037 208 ISHdrhflNM 217
Cdd:COG1117 209 VTH-----NM 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-493 |
2.44e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 317 RNALEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLvgelqpdNGTVKWSENAQI-GYYAQDHEYEF 395
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-------NRLIELYPEARVsGEVYLDGQDIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 DNDLT--------VFDW------MSQW-------------KQEGDDEQAVRSILGRLLF---SQDDIKKPAKVLSGGEKG 445
Cdd:PRK14247 74 KMDVIelrrrvqmVFQIpnpipnLSIFenvalglklnrlvKSKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 446 RMLFGKLMMQKPNILVMDEPTNHLDMES---IESLNAAL--EMyqgTLIFVSH 493
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELkkDM---TIVLVTH 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
2.71e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.88 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGgDLQPSAGNVSLDPN---------ER---IGKLR-Q 71
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRveffnqniyERrvnLNRLRrQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQ-----YTVLDTVIMGHSEL-WEVKQERDRIYslpemseEDGYKVADL--EVKYgemdgysaesragelllgvg 143
Cdd:PRK14258 90 VSMVHPKpnlfpMSVYDNVAYGVKIVgWRPKLEIDDIV-------ESALKDADLwdEIKH-------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 144 iplEQHYGPMsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT---IRWLEQTLNDRDS-TMIIISHDRHFLNMVC 219
Cdd:PRK14258 143 ---KIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSElTMVIVSHNLHQVSRLS 218
|
250
....*....|...
gi 490523037 220 THMADLDYGELRV 232
Cdd:PRK14258 219 DFTAFFKGNENRI 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-210 |
2.74e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE------------RIGKLRQDQFAFEQ----- 78
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrsKIGVVSQDPLLFSNsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 79 -----YTVLDTVIMGH------SELWEVKQERDRIYSLPEMSEEDGYKVAD----LEVK--YGEMDGYSAESRAGELLLG 141
Cdd:PTZ00265 480 ikyslYSLKDLEALSNyynedgNDSQENKNKRNSCRAKCAGDLNDMSNTTDsnelIEMRknYQTIKDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 142 VGIP-LEQHYGPM-----SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN----DRDSTMIIISH 210
Cdd:PTZ00265 560 DFVSaLPDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENRITIIIAH 638
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-253 |
2.74e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTF-MKILggDLQPSAGNVSLD--PNERIGK------LRQDQFAFEQ-YTV 81
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALL--RLINSQGEIWFDgqPLHNLNRrqllpvRHRIQVVFQDpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 LDTvimghselwevkqerdRIYSLPEMSEedgykvaDLEVKYGEMDGYSAESRAGELLLGVGI-PLEQHYGPmSEVAPGW 160
Cdd:PRK15134 375 LNP----------------RLNVLQIIEE-------GLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 161 KLRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTlndRDSTMIIISHDRHFLNMVCTHMADLDYGELrVY 233
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQK---HQLAYLFISHDLHVVRALCHQVIVLRQGEV-VE 506
|
250 260
....*....|....*....|.
gi 490523037 234 PGNYDEYMTAATQARER-LLA 253
Cdd:PRK15134 507 QGDCERVFAAPQQEYTRqLLA 527
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-233 |
2.86e-06 |
|
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: 48.90 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDPN--ERIGKLR----QDQFAFEQYTVLDTVIMGHSELWEVKQERDRIYS 104
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRgselQNYFTKLLEGDVKVIVKPQYVDLIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 105 LPEMSEEDGYKvaDLEVKYGEMDGYsaesragelllgvgipLEQHygpMSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
Cdd:cd03236 110 LLKKKDERGKL--DELVDQLELRHV----------------LDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 185 NLDID---TIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLdYGELRVY 233
Cdd:cd03236 169 YLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAY 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
337-466 |
3.20e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 337 NVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYE----------------FDNDLT 400
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmtVEENLA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 401 VFDWMSQWKQEGDDEQAVRSILGRLlfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK11614 103 MGGFFAERDQFQERIKWVYELFPRL---HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-230 |
3.85e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 4 TSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSA---GNVSL----------DPNE---R 65
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLfgrniyspdvDPIEvrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 66 IGKLRQDQFAFEQYTVLDTVIMG--HSELWEVKQERDRIYslpemseEDGYKVADL--EVKyGEMDGYSaesragelllg 141
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAIGvkLNGLVKSKKELDERV-------EWALKKAALwdEVK-DRLNDYP----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 142 vgipleqhygpmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISHDRHFLNMVC 219
Cdd:PRK14267 148 ------------SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFElkKEYTIVLVTHSPAQAARVS 215
|
250
....*....|.
gi 490523037 220 THMADLDYGEL 230
Cdd:PRK14267 216 DYVAFLYLGKL 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-494 |
4.08e-06 |
|
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: 48.52 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGELQPDNGTV----KWSEnaQIGYYAQDHEYEFDNDLTVFDWMSQWKQEGDDE--QAV 418
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE--ILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLipKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 419 RSILGRLLFSQDDIKKPAKV----------------LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMEsiESLNAA-- 480
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELvdqlelrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNAArl 181
|
170
....*....|....*..
gi 490523037 481 ---LEMYQGTLIFVSHD 494
Cdd:cd03236 182 ireLAEDDNYVLVVEHD 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-210 |
4.26e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLqPSAGNV--------SLDPN---ERIGKLRQDQFAFEQyTVL 82
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielrELDPEswrKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 83 DTVIMGHselwevkqerdriyslPEMSEEDGYKVADLevkygemdgysaeSRAGE----LLLGVGIPL-EQHYGpmseVA 157
Cdd:PRK11174 441 DNVLLGN----------------PDASDEQLQQALEN-------------AWVSEflplLPQGLDTPIgDQAAG----LS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 158 PGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:PRK11174 488 VGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTH 542
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-254 |
4.32e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 6 NVTMQF----GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdlqpsagnVSLDpNERIgklRQDQFAFEQYTV 81
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKD-NWRV---TADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 LDTV------IMGH--SELWEVKQ---------ERDRIYSLPEMSeedgYKVadlevKYGEMDGYSaESRAGELLLGVGI 144
Cdd:PRK15093 76 LRLSprerrkLVGHnvSMIFQEPQscldpservGRQLMQNIPGWT----YKG-----RWWQRFGWR-KRRAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 145 plEQHYGPMS----EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT----IRWLEQTLNDRDSTMIIISHDRHFLN 216
Cdd:PRK15093 146 --KDHKDAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490523037 217 MVCTHMADLDYGElRVYPGNYDEYMTAA----TQARERLLAD 254
Cdd:PRK15093 224 QWADKINVLYCGQ-TVETAPSKELVTTPhhpyTQALIRAIPD 264
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-506 |
5.06e-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: 47.04 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 317 RNALEVEAMTkgfdNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------------SENAQI 384
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 385 GYYAQDHeyefdndltvfdwmsqwKQEG-DDEQAVRS--ILGRLLfsqddikkpakvlSGGEKGRMLFGKLMMQKPNILV 461
Cdd:cd03215 78 AYVPEDR-----------------KREGlVLDLSVAEniALSSLL-------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 462 MDEPTNHLDMESIES----LNAALEmyQGT-LIFVSHDREFVSSLATRVI 506
Cdd:cd03215 128 LDEPTRGVDVGAKAEiyrlIRELAD--AGKaVLLISSELDELLGLCDRIL 175
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-245 |
5.50e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 47.91 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGdLQPSAGNVSLDpNERIGKLRQDQFA-----FEQYTVLdTVIMGhselwe 94
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-GRPLSDWSAAELArhrayLSQQQSP-PFAMP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 95 VKQERDRIYSLPEMSEEDGYKVADLevkygemdgysaeSRAGELLLGVGIPLEQHYGpmsevapG-WKlRVLLAQALF-- 171
Cdd:COG4138 86 VFQYLALHQPAGASSEAVEQLLAQL-------------AEALGLEDKLSRPLTQLSG-------GeWQ-RVRLAAVLLqv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 172 ---SNPD--ILLLDEPTNNLDI------DtiRWLEQtLNDRDSTMIIISHDrhfLNMVCTHmAD----LDYGELrVYPGN 236
Cdd:COG4138 145 wptINPEgqLLLLDEPMNSLDVaqqaalD--RLLRE-LCQQGITVVMSSHD---LNHTLRH-ADrvwlLKQGKL-VASGE 216
|
....*....
gi 490523037 237 YDEYMTAAT 245
Cdd:COG4138 217 TAEVMTPEN 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
320-530 |
5.76e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGEL---QPDNG-------TVKWSENAQI----- 384
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGarvtgdvTLNGEPLAAIdaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 385 ----GYYAQDHEYEFD---NDLTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDD---IKKPAKVLSGGEKGRMLFGKLMM 454
Cdd:PRK13547 82 arlrAVLPQAAQPAFAfsaREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAtalVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 455 Q---------KPNILVMDEPTNHLDMESIESL-----NAALEMYQGTLIFVsHDREFVSSLATRVIEITPERVVDfSGGY 520
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLldtvrRLARDWNLGVLAIV-HDPNLAARHADRIAMLADGAIVA-HGAP 239
|
250
....*....|
gi 490523037 521 EDYLRSKGIE 530
Cdd:PRK13547 240 ADVLTPAHIA 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
283-528 |
5.90e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 283 TSRARQIDKIKLEEVKASSRQNPFIRfeqDKKLFRNALEVEAMTKGFDN-GPLFKNVGLLLEVGEKLAILGANGVGKSTM 361
Cdd:PRK13657 301 MAAPKLEEFFEVEDAVPDVRDPPGAI---DLGRVKGAVEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 362 LKTLVGELQPDNGTVKW-----------SENAQIGYYAQDHEYeFDNdlTVFDWMSQWKQEGDDE---------QAVRSI 421
Cdd:PRK13657 378 INLLQRVFDPQSGRILIdgtdirtvtraSLRRNIAVVFQDAGL-FNR--SIEDNIRVGRPDATDEemraaaeraQAHDFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 422 LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL-EMYQGTLIFVSHDREFVSS 500
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALdELMKGRTTFIIAHRLSTVR 534
|
250 260
....*....|....*....|....*...
gi 490523037 501 LATRVIEITPERVVDfSGGYEDYLRSKG 528
Cdd:PRK13657 535 NADRILVFDNGRVVE-SGSFDELVARGG 561
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-248 |
6.02e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.62 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 32 LIGANGSGKSTFMKILGGdLQPSAGNVSLDpneriGKlrqdqfAFEQYTvldtvimgHSEL-----WEVKQERDrIYSLP 106
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAG-LLPGSGSIQFA-----GQ------PLEAWS--------AAELarhraYLSQQQTP-PFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 107 -----EMSEEDGYKVADLEVKYGEMdgysAEsragelLLGVGIPLEQHYGPMS--EvapgWKlRVLLAQALF-----SNP 174
Cdd:PRK03695 86 vfqylTLHQPDKTRTEAVASALNEV----AE------ALGLDDKLGRSVNQLSggE----WQ-RVRLAAVVLqvwpdINP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 175 D--ILLLDEPTNNLDIDTIRWLEQTLNDRDS---TMIIISHDrhfLNMVCTHmAD----LDYGELRVYpGNYDEYMTAAT 245
Cdd:PRK03695 151 AgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LNHTLRH-ADrvwlLKQGKLLAS-GRRDEVLTPEN 225
|
...
gi 490523037 246 QAR 248
Cdd:PRK03695 226 LAQ 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-72 |
7.12e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 47.77 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGS-----KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD-------PNER--- 65
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklPEYKrak 80
|
....*...
gi 490523037 66 -IGKLRQD 72
Cdd:COG1101 81 yIGRVFQD 88
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-470 |
7.37e-06 |
|
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: 47.27 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 334 LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPD---NGTV----------KWSENaqIGYYAQD---HEYefdn 397
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkpdQFQKC--VAYVRQDdilLPG---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 398 dLTVFDWM--------------SQWKQEGDDEQ----AVRSILGRLLfsqddikkpaKVLSGGEKGRMLFGKLMMQKPNI 459
Cdd:cd03234 96 -LTVRETLtytailrlprkssdAIRKKRVEDVLlrdlALTRIGGNLV----------KGISGGERRRVSIAVQLLWDPKV 164
|
170
....*....|.
gi 490523037 460 LVMDEPTNHLD 470
Cdd:cd03234 165 LILDEPTSGLD 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
320-482 |
7.48e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.58 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV----------KWSENAQ--IGYY 387
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllPLHARARrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 388 AQdhEYEFDNDLTVFD-WMSQWKQEGDDEQAVRSILGRLLFSQDDIK----KPAKVLSGGEKGRMLFGKLMMQKPNILVM 462
Cdd:PRK10895 84 PQ--EASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEhlrdSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180
....*....|....*....|
gi 490523037 463 DEPTNHLDMESIESLNAALE 482
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIE 181
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
320-513 |
1.02e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFdnGPLF--KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYyaQDHEYE--- 394
Cdd:PRK11300 6 LSVSGLMMRF--GGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 ----FDN-----DLTVFD--WMSQWKQEGDD-----------EQAVRSILGRLLFSQDDI------KKPAKVLSGGEKGR 446
Cdd:PRK11300 82 vvrtFQHvrlfrEMTVIEnlLVAQHQQLKTGlfsgllktpafRRAESEALDRAATWLERVgllehaNRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 447 MLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL----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 |
1.09e-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: 46.16 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 140 LGVG-IPLEQhygPMSEVAPGWKLRVLLAQALFSNPD--ILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRH 213
Cdd:cd03238 74 VGLGyLTLGQ---KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLD 150
|
..
gi 490523037 214 FL 215
Cdd:cd03238 151 VL 152
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
1.37e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdlQPS----AGNV--------SLDPNERIgk 68
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlfkgesilDLEPEERA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 69 lRQDQF-AFeQYTVldtVIMGHSE---LWEVKQERDRIYSLPEMSEEDGYKVADLEVKYGEMDGYSAESRAGELLLGvgi 144
Cdd:CHL00131 83 -HLGIFlAF-QYPI---EIPGVSNadfLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSG--- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 145 pleqhygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHDRHFLNMV 218
Cdd:CHL00131 155 --------------GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINklmTSENSIILITHYQRLLDYI 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-210 |
1.50e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 46.00 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 12 GSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSA--GNVSLD--------PNERIGKLRQDQFAFEQYTV 81
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINgrpldkrsFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 82 LDTvimghseLWevkqerdriyslpemseedgykvadlevkygemdgYSAESRagelllgvGIPLEQhygpmsevapgwK 161
Cdd:cd03213 100 RET-------LM-----------------------------------FAAKLR--------GLSGGE------------R 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLD-------IDTIRWLEQTlndrDSTMIIISH 210
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRLADT----GRTIICSIH 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-485 |
1.56e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 5 SNVTMQF-GSKPLfENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDPNERigklrqdQFAFEQYTVLD 83
Cdd:PRK10982 2 SNISKSFpGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-------DFKSSKEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 84 TVIMGHSELWEVKQER--DRI----YSLPEMSEEDGYKVADLEVKYGEMDgysaesragelllgvgIPLEqhygPMSEVA 157
Cdd:PRK10982 74 GISMVHQELNLVLQRSvmDNMwlgrYPTKGMFVDQDKMYRDTKAIFDELD----------------IDID----PRAKVA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 158 pgwKLRVL------LAQALFSNPDILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYG 228
Cdd:PRK10982 134 ---TLSVSqmqmieIAKAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 229 ELrvypgnydeymtAATQARERLLADnakkkaQIADL---QSFVSRFSANASKSRQATsrarqidkikleevkassrqnp 305
Cdd:PRK10982 211 QW------------IATQPLAGLTMD------KIIAMmvgRSLTQRFPDKENKPGEVI---------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 306 firfeqdkklfrnaLEVEAMTKgfDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKW------- 378
Cdd:PRK10982 251 --------------LEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhgkkinn 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 379 ---------------SENAQIGYYAQ-DHEY-----EFDNDLTVFDWMSQWKQEGDDEQAVRSIlgrllfsqdDIKKPAK 437
Cdd:PRK10982 315 hnaneainhgfalvtEERRSTGIYAYlDIGFnslisNIRNYKNKVGLLDNSRMKSDTQWVIDSM---------RVKTPGH 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490523037 438 -----VLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDmesiesLNAALEMYQ 485
Cdd:PRK10982 386 rtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID------VGAKFEIYQ 432
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
345-494 |
1.58e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 345 GEKLAILGANGVGKSTMLKTLVGeLQPDNGTV--------KWSENAQI---GYYAQDHEYEFDNDltVFDWMSQWKQEGD 413
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIqfagqpleAWSAAELArhrAYLSQQQTPPFAMP--VFQYLTLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 414 DEQAVRSILGRL---LFSQDDIKKPAKVLSGGEKGRM-LFGKLMMQKPNI------LVMDEPTNHLDMESIESLNAAL-E 482
Cdd:PRK03695 99 RTEAVASALNEVaeaLGLDDKLGRSVNQLSGGEWQRVrLAAVVLQVWPDInpagqlLLLDEPMNSLDVAQQAALDRLLsE 178
|
170
....*....|....
gi 490523037 483 MYQ--GTLIFVSHD 494
Cdd:PRK03695 179 LCQqgIAVVMSSHD 192
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-506 |
1.92e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 349 AILGANGVGKSTMLKTLVGELQPDNGTVKWS---------------ENAQIGYYAQDHE----YEFDNDLTVfdWMSqwk 409
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiclppEKRRIGYVFQDARlfphYKVRGNLRY--GMA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 410 qEGDDEQ--------AVRSILGRLLFSqddikkpakvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLNAAL 481
Cdd:PRK11144 103 -KSMVAQfdkivallGIEPLLDRYPGS----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180
....*....|....*....|....*....
gi 490523037 482 EMYQGTL----IFVSHDREFVSSLATRVI 506
Cdd:PRK11144 172 ERLAREInipiLYVSHSLDEILRLADRVV 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-76 |
1.99e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 1.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLR---QDQFAF 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE-RQSIKKDLctyQKQLCF 78
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
336-504 |
2.13e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.31 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTL--VGELQPD---NGTVKWSEN-------------AQIGY-YAQDHEYEFd 396
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlrKEIGMvFQQPNPFPM- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 397 ndlTVFD---WMSQWKQEGD----DEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTN 467
Cdd:PRK14239 101 ---SIYEnvvYGLRLKGIKDkqvlDEAVEKSLKGASIWDEvkDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490523037 468 HLDMESI----ESLNAALEMYqgTLIFVSHDREFVSSLATR 504
Cdd:PRK14239 178 ALDPISAgkieETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-210 |
2.14e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.39 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQF--GSKPLFENISVKFGGGNRYGLIGANGSGKST----FMKILG--GDLQ---PSAGNVSLDP-NERIGKL 69
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNteGDIQidgVSWNSVPLQKwRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 70 RQDQFAFEQYTvldtvimghselwevkqeRDRIYSLPEMSEEDGYKVADlEVkygemdgysaesragelllGVGIPLEQH 149
Cdd:cd03289 83 PQKVFIFSGTF------------------RKNLDPYGKWSDEEIWKVAE-EV-------------------GLKSVIEQF 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490523037 150 YGPMSEV--------APGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RDSTMIIISH 210
Cdd:cd03289 125 PGQLDFVlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEH 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-245 |
2.23e-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: 45.86 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 31 GLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQFAFEQYTVLDtviMGHSELwevkqerDRIYSLPEMSE 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRD---LLSSIT-------KDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 111 E--DGYKVADLevkygeMDGYSAESRAGELllgvgipleQhygpmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:cd03237 98 EiaKPLQIEQI------LDREVPELSGGEL---------Q--------------RVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490523037 189 dtirwlEQTL----------NDRDSTMIIISHDrhFLnmvcthMADLDYGELRVYPGNYDEYMTAAT 245
Cdd:cd03237 149 ------EQRLmaskvirrfaENNEKTAFVVEHD--II------MIDYLADRLIVFEGEPSVNGVANP 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-190 |
2.47e-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: 47.21 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSldPNERIGKLRQDQFAFEQyTVLDTVIMGhselwe 94
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQTSWIMPG-TIKDNIIFG------ 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 95 VKQERDRIYSLPEMS--EEDGYKVADLEvKYGEMDGysaesragelllgvGIPLeqhygpmsevAPGWKLRVLLAQALFS 172
Cdd:TIGR01271 511 LSYDEYRYTSVIKACqlEEDIALFPEKD-KTVLGEG--------------GITL----------SGGQRARISLARAVYK 565
|
170
....*....|....*...
gi 490523037 173 NPDILLLDEPTNNLDIDT 190
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVT 583
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-74 |
2.49e-05 |
|
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: 47.10 E-value: 2.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490523037 32 LIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKLRQDQF 74
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTADNREAY 404
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-212 |
2.92e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.25 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 32 LIGANGSGKSTFMKILGGDLQPSAGNVSLDPNE--------------RIGKLRQDQFAFEQYTVLDTVIMGhselwevkq 97
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrevpflrrQIGMIFQDHHLLMDRTVYDNVAIP--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 98 erdriYSLPEMSEEDgykvadlevkygemdgysAESRAGELLLGVGIPLEQHYGPMsEVAPGWKLRVLLAQALFSNPDIL 177
Cdd:PRK10908 104 -----LIIAGASGDD------------------IRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 490523037 178 LLDEPTNNLD----IDTIRWLEQtLNDRDSTMIIISHDR 212
Cdd:PRK10908 160 LADEPTGNLDdalsEGILRLFEE-FNRVGVTVLMATHDI 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-526 |
3.90e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 334 LFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVkWSENAqIGYYAQ----------DHEYEFDNDLT--V 401
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERS-IAYVPQqawimnatvrGNILFFDEEDAarL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 FDWMSQWKQEGDdeqaVRSILGRLlfsQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMESIESLnaAL 481
Cdd:PTZ00243 753 ADAVRVSQLEAD----LAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV--VE 823
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 482 EMYQGTL-----IFVSHDREFVsSLATRVIEITPERVVdFSGGYEDYLRS 526
Cdd:PTZ00243 824 ECFLGALagktrVLATHQVHVV-PRADYVVALGDGRVE-FSGSSADFMRT 871
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-243 |
4.00e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 27 GNRYGLIGANGSGKS-TFMKILG-----GDLQPSA---GNVSLD-PNERIGKLRQDQFAfeqytvldtVIMghselwevk 96
Cdd:PRK09473 42 GETLGIVGESGSGKSqTAFALMGllaanGRIGGSAtfnGREILNlPEKELNKLRAEQIS---------MIF--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 97 qeRDRIYSL-PEMseedgyKVAD--LEV--KYGEMDGYSAESRAGELLLGVGIPLEQHYGPM--SEVAPGWKLRVLLAQA 169
Cdd:PRK09473 104 --QDPMTSLnPYM------RVGEqlMEVlmLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 170 LFSNPDILLLDEPTNNLDIDTIRWLEQTLND--RD--STMIIISHDRHFLNMVCTHMadldygeLRVYPGNYDEYMTA 243
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNElkREfnTAIIMITHDLGVVAGICDKV-------LVMYAGRTMEYGNA 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-493 |
5.10e-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: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGT-----VKWSE------NAQIGYYAQDHeyefdndlTV 401
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgVDISKiglhdlRSRISIIPQDP--------VL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 402 F--------DWMSQWkqeGDDE--QAVRSILGRLLFSQDDIKKPAKVLSGGEK---G-RMLF--GKLMMQKPNILVMDEP 465
Cdd:cd03244 90 FsgtirsnlDPFGEY---SDEElwQALERVGLKEFVESLPGGLDTVVEEGGENlsvGqRQLLclARALLRKSKILVLDEA 166
|
170 180 190
....*....|....*....|....*....|
gi 490523037 466 TNHLDMESIESLNAAL--EMYQGTLIFVSH 493
Cdd:cd03244 167 TASVDPETDALIQKTIreAFKDCTVLTIAH 196
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-261 |
5.28e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 18 ENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpnERIGKLR--------QDQFAFEQYTVLDTVIMGH 89
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----DRNGEVSviaisaglSGQLTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 90 SelwevkqeRDRIYSL-PEMseedgykvadleVKYGEMdgysaesraGELLlgvgipleqhYGPMSEVAPGWKLRVLLAQ 168
Cdd:PRK13546 116 K--------RKEIKAMtPKI------------IEFSEL---------GEFI----------YQPVKKYSSGMRAKLGFSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 169 ALFSNPDILLLDEPTNNLD-------IDTIrwleQTLNDRDSTMIIISHDRHFLNMVCTHMADLDYGELRVYpGNYDEYM 241
Cdd:PRK13546 157 NITVNPDILVIDEALSVGDqtfaqkcLDKI----YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDDVL 231
|
250 260
....*....|....*....|.
gi 490523037 242 taatQARERLLADNAKK-KAQ 261
Cdd:PRK13546 232 ----PKYEAFLNDFKKKsKAE 248
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
319-473 |
5.82e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.87 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 319 ALEVEAMTKGFDNG-PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENAQIGYYAQ 389
Cdd:PRK15056 6 GIVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 390 DHEYEFDNDLTVFD-----------WMSQWKQEgdDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPN 458
Cdd:PRK15056 86 SEEVDWSFPVLVEDvvmmgryghmgWLRRAKKR--DRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQ 162
|
170
....*....|....*
gi 490523037 459 ILVMDEPTNHLDMES 473
Cdd:PRK15056 163 VILLDEPFTGVDVKT 177
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-231 |
6.26e-05 |
|
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: 43.13 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 27 GNRYGLIGANGSGKSTFMKILGGDLQPSAGNVsldpnerigklrqdqfafeqytvldtvimghselwevkqerdriyslp 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 107 emseedgykvadlevKYGEMDGYSAESRAGELLLGVGIPLEQHYGPMsevapgwKLRVLLAQALFSNPDILLLDEPTNNL 186
Cdd:smart00382 34 ---------------IYIDGEDILEEVLDQLLLIIVGGKKASGSGEL-------RLRLALALARKLKPDVLILDEITSLL 91
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490523037 187 DIDTIRWLEQTLNDRDSTMIIISHDRHFLnMVCTHMADLDYGELR 231
Cdd:smart00382 92 DAEQEALLLLLEELRLLLLLKSEKNLTVI-LTTNDEKDLGPALLR 135
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-367 |
6.28e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 6.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVG 367
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
6.53e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 2 LVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILG--GDLQPSA---GNV----------SLDPNE-- 64
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGFrveGKVtfhgknlyapDVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 65 -RIGKLRQDQFAFEQyTVLDTVIMGhselwevkqerDRIyslpemseeDGYKvadlevkyGEMDGYSAES-RAGELLLGV 142
Cdd:PRK14243 91 rRIGMVFQKPNPFPK-SIYDNIAYG-----------ARI---------NGYK--------GDMDELVERSlRQAALWDEV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 143 GIPLEQHYGPMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLD-IDTIRwLEQTLND--RDSTMIIISHD 211
Cdd:PRK14243 142 KDKLKQSGLSLSG---GQQQRLCIARAIAVQPEVILMDEPCSALDpISTLR-IEELMHElkEQYTIIIVTHN 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-210 |
8.07e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 34 GANGSGKSTFMKILGGDLQPSAGNVSLD-------------PNE--RIGKLRQDQFAFEQYTVLDTVIMGHSElwEVKQE 98
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiclPPEkrRIGYVFQDARLFPHYKVRGNLRYGMAK--SMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 99 RDRIYSLpemseedgykvadlevkygemdgysaesragellLGVGiPLEQHYgPMSeVAPGWKLRVLLAQALFSNPDILL 178
Cdd:PRK11144 109 FDKIVAL----------------------------------LGIE-PLLDRY-PGS-LSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 490523037 179 LDEPTNNLDIDTIR----WLEQTLNDRDSTMIIISH 210
Cdd:PRK11144 152 MDEPLASLDLPRKRellpYLERLAREINIPILYVSH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
439-515 |
1.16e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 439 LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVIEITPE 511
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqaqiLQLLRELQQELNM---GLLFITHNLSIVRKLADRVAVMQNG 233
|
....
gi 490523037 512 RVVD 515
Cdd:PRK15134 234 RCVE 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
32-190 |
1.22e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 43.41 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 32 LIGANGSGKSTFMKILGGDLqpsAGNVSLDPNERIGKLRQDQFAfEQYTvldtvimghselwevkqeRDRIYSlpemSEE 111
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYKEFA-EKYP------------------GEIIYV----SEE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 112 DgYKVADLEVKygEMDGYSAESRAGELLLGvgipleqhygpmseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDT 190
Cdd:cd03233 92 D-VHFPTLTVR--ETLDFALRCKGNEFVRG--------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
434-511 |
1.25e-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: 42.70 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 434 KPAKVLSGGEKGRMLFGKLMMQ--KPNILVMDEPTNHLDMESIESLNAALE--MYQG-TLIFVSHDREFVSSlATRVIEI 508
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLLEVIKglIDLGnTVILIEHNLDVLSS-ADWIIDF 161
|
...
gi 490523037 509 TPE 511
Cdd:cd03238 162 GPG 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
333-493 |
1.26e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.84 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELqPDNGTVK-------------WSEnaQIGYYAQD----HEyef 395
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKingielreldpesWRK--HLSWVGQNpqlpHG--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 dndlTVFDWMSQWKQEGDDEQA--------VRSILGRLLFSQD-DIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPT 466
Cdd:PRK11174 438 ----TLRDNVLLGNPDASDEQLqqalenawVSEFLPLLPQGLDtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|.
gi 490523037 467 NHLDMES----IESLNAAleMYQGTLIFVSH 493
Cdd:PRK11174 514 ASLDAHSeqlvMQALNAA--SRRQTTLMVTH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
333-526 |
1.42e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSE------NAQI------------GYYAQDHEYE 394
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVielseqsaaqmrHVRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 395 FDNDLT----VFDWMSQ------WKQEGDDEQAVRSI-----LGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNI 459
Cdd:PRK10261 110 FQEPMTslnpVFTVGEQiaesirLHQGASREEAMVEAkrmldQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 460 LVMDEPTNHLDM---ESIESLNAAL--EMYQGtLIFVSHDREFVSSLATRVIEITPERVVDfSGGYEDYLRS 526
Cdd:PRK10261 190 LIADEPTTALDVtiqAQILQLIKVLqkEMSMG-VIFITHDMGVVAEIADRVLVMYQGEAVE-TGSVEQIFHA 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
320-483 |
1.54e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGFD-NGPLF--------KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSEN----AQIGY 386
Cdd:PRK15112 5 LEVRNLSKTFRyRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 387 YAQDHEYEFDNDLTVFDWMSQWKQEGD-------------DEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLM 453
Cdd:PRK15112 85 RSQRIRMIFQDPSTSLNPRQRISQILDfplrlntdlepeqREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL 164
|
170 180 190
....*....|....*....|....*....|..
gi 490523037 454 MQKPNILVMDEPTNHLDMeSIES--LNAALEM 483
Cdd:PRK15112 165 ILRPKVIIADEALASLDM-SMRSqlINLMLEL 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-506 |
1.68e-04 |
|
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: 43.89 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 320 LEVEAMTKGF--DNGPLF--KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGeLQPDNGTVKwsenaqiGyyaqdhEYEF 395
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITS-------G------EILF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 DN-DLT-----------------VF-DWMS----------Q-----WKQEGDDEQAVRSILGRLLfSQDDIKKPAKV--- 438
Cdd:COG0444 68 DGeDLLklsekelrkirgreiqmIFqDPMTslnpvmtvgdQiaeplRIHGGLSKAEARERAIELL-ERVGLPDPERRldr 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490523037 439 ----LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD-------MESIESLNAALEMyqgTLIFVSHDREFVSSLATRVI 506
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLNLLKDLQRELGL---AILFITHDLGVVAEIADRVA 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
440-506 |
1.97e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.41 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490523037 440 SGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMeSIES--LNAALEMYQ--GT-LIFVSHDREFVSSLATRVI 506
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqvLNLMMDLQQelGLsYVFISHDLSVVEHIADEVM 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-190 |
2.28e-04 |
|
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: 43.31 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 15 PLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSldPNERIGKLRQDQFAFEQyTVLDTVIMGHSelwe 94
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQFSWIMPG-TIKENIIFGVS---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 95 vkqerdriyslpemseEDGYKvadlevkygemdgYSAESRAGELLLGVGIPLEQHYGPMSE----VAPGWKLRVLLAQAL 170
Cdd:cd03291 124 ----------------YDEYR-------------YKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAV 174
|
170 180
....*....|....*....|
gi 490523037 171 FSNPDILLLDEPTNNLDIDT 190
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFT 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
333-470 |
2.32e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 333 PLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGT-------------VKWSENAQIGyyaqdheyefDNDL 399
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsvvirgsvayvpqVSWIFNATVR----------ENIL 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 400 TVFDWMSQWKQEGDDEQAVRSILGrLLFSQD--DIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD 470
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHDLD-LLPGRDltEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-61 |
2.36e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|
gi 490523037 32 LIGANGSGKSTFMKILGGDLQPSAGNVSLD 61
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-239 |
2.64e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.16 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLdpnerIGKlrqdqfafeqytvlDTVIMGHSELWEVKQER 99
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW-----LGK--------------DLLGMKDDEWRAVRSDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 100 DRIYSLPEMSEEDGYKVAD-----LEVKYGEMDGYSAESRAGELLLGVGI-P-LEQHYgPmSEVAPGWKLRVLLAQALFS 172
Cdd:PRK15079 101 QMIFQDPLASLNPRMTIGEiiaepLRTYHPKLSRQEVKDRVKAMMLKVGLlPnLINRY-P-HEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 173 NPDILLLDEPTNNLDID----TIRWLEQTLNDRDSTMIIISHDrhfLNMVcTHMADldygelRV---YPGN------YDE 239
Cdd:PRK15079 179 EPKLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHD---LAVV-KHISD------RVlvmYLGHavelgtYDE 248
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
2.98e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.26 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKfgGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLD--------PNER-IGKLRQ 71
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 72 DQFAFEQYTVLDTVIMG-HSELWEVKQERDRIYSLPE-MSEEDgykvaDLEVKYGEMDGysaesragelllgvgipleqh 149
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlNPGLKLNAAQREKLHAIARqMGIED-----LLARLPGQLSG--------------------- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 150 ygpmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISH 210
Cdd:PRK10771 133 ---------GQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
411-509 |
3.57e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 411 EGD-DEQAVRSILGRLLFSQ--DDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES---IESLNAALEMy 484
Cdd:PRK14243 121 KGDmDELVERSLRQAALWDEvkDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKE- 199
|
90 100
....*....|....*....|....*
gi 490523037 485 QGTLIFVSHDREfvssLATRVIEIT 509
Cdd:PRK14243 200 QYTIIIVTHNMQ----QAARVSDMT 220
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
162-218 |
4.19e-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: 4.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 162 LRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQTLND--------RDSTMIIISHDRHFLNMV 218
Cdd:TIGR00606 1212 IRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEiiksrsqqRNFQLLVITHDEDFVELL 1276
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-211 |
4.66e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.39 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 20 ISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpNERIGKlrqdqfafeqytvldtvimghSELWEVKQER 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID-GELLTA---------------------ENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 100 DRIYSLPEmSEEDGYKVADlEVKYG-EMDGYSAES---RAGELLLGVGIpLEQHYGPMSEVAPGWKLRVLLAQALFSNPD 175
Cdd:PRK13642 84 GMVFQNPD-NQFVGATVED-DVAFGmENQGIPREEmikRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490523037 176 ILLLDEPTNNLD----IDTIRWLEQTLNDRDSTMIIISHD 211
Cdd:PRK13642 161 IIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
159-236 |
5.47e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD--------IDTIRwLEQTLNdrdSTMIIISHDRhflnMVCTHMAD----LD 226
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIEISR-LHKRLG---RTMIYVTHDQ----VEAMTLADkivvLD 208
|
90
....*....|....*....
gi 490523037 227 YG---------ELRVYPGN 236
Cdd:PRK11000 209 AGrvaqvgkplELYHYPAN 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-367 |
7.77e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 7.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490523037 320 LEVEAMTKGFDNGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVG 367
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-505 |
8.05e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV---------------KWSENAQIGYYAQD-----HEYEF 395
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQSfalmpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 DNdlTVFDW-MSQWKQEGDDEQAVRSIlgRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD---- 470
Cdd:PRK10070 125 DN--TAFGMeLAGINAEERREKALDAL--RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplir 200
|
170 180 190
....*....|....*....|....*....|....*
gi 490523037 471 MESIESLNAALEMYQGTLIFVSHDREFVSSLATRV 505
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-187 |
9.29e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 16 LFENISVKFGGGNRYGLIGANGSGKSTFMKILGGdlQPSAGNVSLDPneRIGKL--RQDQFA-----FEQYTVldtvimg 88
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDI--RISGFpkKQETFArisgyCEQNDI------- 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 89 HSELWEVKQERdrIYS----LP-EMSEEDGYKVADLEVKYGEMDGYSaESRAGelLLGV-GIPLEQhygpmsevapgwKL 162
Cdd:PLN03140 964 HSPQVTVRESL--IYSaflrLPkEVSKEEKMMFVDEVMELVELDNLK-DAIVG--LPGVtGLSTEQ------------RK 1026
|
170 180
....*....|....*....|....*
gi 490523037 163 RVLLAQALFSNPDILLLDEPTNNLD 187
Cdd:PLN03140 1027 RLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-58 |
1.08e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490523037 1 MLVTSNVTMQFGSKPLFeNISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNV 58
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-211 |
1.12e-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: 40.11 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDLQPSAGNVSLDpneriGKlrqdqfafeQYTVLDTvimghselw 93
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-----GK---------PVTRRSP--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 94 evkqeRDRIyslpemseedgykvaDLEVkygemdGYSAESRAGELLLGvGIPLEQHygpmseVAPGWKL------RVLLA 167
Cdd:cd03215 70 -----RDAI---------------RAGI------AYVPEDRKREGLVL-DLSVAEN------IALSSLLsggnqqKVVLA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490523037 168 QALFSNPDILLLDEPTNNLDIDTIRWLEQTLN---DRDSTMIIISHD 211
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRelaDAGKAVLLISSE 163
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
336-494 |
1.34e-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: 40.70 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 336 KNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTV--------KWSENA-------QIGYYAQD-----HEYEF 395
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaAMSRKElrelrrkKISMVFQSfallpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 396 DNdlTVFDWMSQWKQEGDDEQAVRSILGRLLFSQDDIKKPAKvLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD----M 471
Cdd:cd03294 121 EN--VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirR 197
|
170 180
....*....|....*....|...
gi 490523037 472 ESIESLNAALEMYQGTLIFVSHD 494
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHD 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
434-511 |
1.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 434 KPAKVLSGGEKGRM-LFGKLM--MQKPNILVMDEPTNHLDMESIESLNAALE--MYQG-TLIFVSHDREFVsSLATRVIE 507
Cdd:PRK00635 805 RPLSSLSGGEIQRLkLAYELLapSKKPTLYVLDEPTTGLHTHDIKALIYVLQslTHQGhTVVIIEHNMHVV-KVADYVLE 883
|
....
gi 490523037 508 ITPE 511
Cdd:PRK00635 884 LGPE 887
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
159-224 |
1.36e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490523037 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDIdTIRwlEQTLN---DRDSTM----IIISHDrhfLNMVcTHMAD 224
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDV-SVQ--AQVLNlmmDLQQELglsyVFISHD---LSVV-EHIAD 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-521 |
1.41e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 350 ILGANGVGKSTMLKTLVGELQPDNGTV---------KWSENAQIGYYAQDH------------------EYEFDNDLTVF 402
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKiknfkelrrrvsmvfqfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 403 DWM------SQWKQEGddEQAVRSILGRLLFSQDDIKKPAKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLD------ 470
Cdd:PRK13631 137 DIMfgpvalGVKKSEA--KKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehe 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490523037 471 -MESIESLNAAlemyQGTLIFVSHDREFVSSLATRVIEITPERVVDFSGGYE 521
Cdd:PRK13631 215 mMQLILDAKAN----NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-271 |
1.42e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 119 LEVKYG--------EMDGYSAES---------RAGELLLGVGI---PLEQhygPMSEVAPGWKLRVLLAQALFS---NPD 175
Cdd:PRK00635 756 LEVRYKgkniadilEMTAYEAEKffldepsihEKIHALCSLGLdylPLGR---PLSSLSGGEIQRLKLAYELLApskKPT 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 176 ILLLDEPTNNL---DIDTIRWLEQTLNDRDSTMIIISHDRHFLNmVCTHMAdldygELRVYPGNYDEYMTAATQARERLL 252
Cdd:PRK00635 833 LYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL-----ELGPEGGNLGGYLLASCSPEELIH 906
|
170
....*....|....*....
gi 490523037 253 ADNAKKKAqiadLQSFVSR 271
Cdd:PRK00635 907 LHTPTAKA----LRPYLSS 921
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-216 |
1.47e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 14 KPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGGDL--QPSAGNVSLDPNErigklrqdqfaFEQytvlDTVIMghse 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ-----------FGR----EASLI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 92 lwevkqerDRIYSLPEMSEedgykvadlevkygemdgysaesrAGELLLGVGIPLEQHY-GPMSEVAPGWKLRVLLAQAL 170
Cdd:COG2401 104 --------DAIGRKGDFKD------------------------AVELLNAVGLSDAVLWlRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490523037 171 FSNPDILLLDEPTNNLDIDTIRWLEQTLND----RDSTMIIISHDRHFLN 216
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKlarrAGITLVVATHHYDVID 201
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
439-526 |
1.47e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 439 LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDM----ESIESLnaaLEMYQG---TLIFVSHDREFVSSLATRVIEITPE 511
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELL---LELQQKenmALVLITHDLALVAEAAHKIIVMYAG 230
|
90
....*....|....*
gi 490523037 512 RVVDfSGGYEDYLRS 526
Cdd:PRK11022 231 QVVE-TGKAHDIFRA 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
331-473 |
2.04e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 331 NGPLFKNVGLLLEVGEKLAILGANGVGKSTMLKTLVGELQPDNGTVKWSENAQIGYYAQDHEYEFDNDLTV----FDWMS 406
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVgmknVNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 407 QWKQEGD-DEQAVRSILGRLLF------------------------------------------SQDDIKKPAKV----- 438
Cdd:PTZ00265 1260 LTKEGGSgEDSTVFKNSGKILLdgvdicdynlkdlrnlfsivsqepmlfnmsiyenikfgkedaTREDVKRACKFaaide 1339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490523037 439 -------------------LSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES 473
Cdd:PTZ00265 1340 fieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-225 |
2.69e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 19 NISVKFGGGNRYGLIGANGSGKSTFM-KILGGDLQP-------SAGNV-SLDPNERIGKLRQ-DQFAFEQ--------YT 80
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLInDTLYPALARrlhlkkeQPGNHdRIEGLEHIDKVIViDQSPIGRtprsnpatYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 81 VLDTVIMG-----------HSELWEVKQERDRIYSLPEMSEEDGYKVadlevkygeMDGYSAESRAGELLLGVG---IPL 146
Cdd:cd03271 93 GVFDEIRElfcevckgkryNRETLEVRYKGKSIADVLDMTVEEALEF---------FENIPKIARKLQTLCDVGlgyIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 147 EQhygPMSEVAPGWKLRVLLAQALfSNPD----ILLLDEPTNNLDIDTIRWL---EQTLNDRDSTMIIISHDRHFLNmVC 219
Cdd:cd03271 164 GQ---PATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLlevLQRLVDKGNTVVVIEHNLDVIK-CA 238
|
....*.
gi 490523037 220 THMADL 225
Cdd:cd03271 239 DWIIDL 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
164-188 |
3.75e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 3.75e-03
10 20
....*....|....*....|....*
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-218 |
3.81e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 1 MLVTSNVTMQFGSKPLFENISVKFGGGNRYGLIGANGSGKSTFMKILGG--DLQPSAGNVS--------LDPNERIGklr 70
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEfkgkdlleLSPEDRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490523037 71 QDQFAFEQYTVldtVIMGHSELWEVKQERDRIYSLPEMSEEDGYKVADL-EVKYGEMDgysaesRAGELL---LGVGIpl 146
Cdd:PRK09580 78 EGIFMAFQYPV---EIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLmEEKIALLK------MPEDLLtrsVNVGF-- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490523037 147 eqhygpmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIDTIRWLEQ---TLNDRDSTMIIISHDRHFLNMV 218
Cdd:PRK09580 147 ----------SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYI 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
436-473 |
4.59e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.59e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490523037 436 AKVLSGGEKGRMLFGKLMMQKPNILVMDEPTNHLDMES 473
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
164-188 |
7.16e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 7.16e-03
10 20
....*....|....*....|....*
gi 490523037 164 VLLAQALFSNPDILLLDEPTNNLDI 188
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| |
