|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-521 |
3.42e-170 |
|
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: 492.74 E-value: 3.42e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIDpanpGMAGLRRWLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:COG4988 23 VLLGLLSGLLIIAQAWLLASLLAGLII----GGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTARRPSQLAAQRDAAAV-LITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLI 159
Cdd:COG4988 99 EKLLALGPAWLRGKSTGELAtLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 160 GLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVAL 239
Cdd:COG4988 179 GKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSSAVLEFFASLSIAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 240 VAVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLgESPSPTPGRRTVTA---RGGVI 316
Cdd:COG4988 259 VAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALL-DAPEPAAPAGTAPLpaaGPPSI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:COG4988 338 ELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPGTVRHNLVLLGPV---DDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:COG4988 418 QNPYLFAGTIRENLRLGRPDasdEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLL 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15608759 473 DEPTAHLDARTEQHVLGAIvERARAGATVLVVAHRQQVAAAGDRVVEVN 521
Cdd:COG4988 498 DEPTAHLDAETEAEILQAL-RRLAKGRTVILITHRLALLAQADRILVLD 545
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-520 |
5.67e-142 |
|
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: 419.38 E-value: 5.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIdPANPGMAGLRRWLGPLSILLVLwglRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:TIGR02857 9 ALLGVLGALLIIAQAWLLARVVDGLI-SAGEPLAELLPALGALALVLLL---RALLGWLQERAAARAAAAVKSQLRERLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTARRPSQLAAQRDA-AAVLITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLI 159
Cdd:TIGR02857 85 EAVAALGPRWLQGRPSGeLATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 160 GLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVAL 239
Cdd:TIGR02857 165 GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 240 VAVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPSPTPGRRTVT-ARGGVIRL 318
Cdd:TIGR02857 245 VAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTaAPASSLEF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 319 ERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQR 397
Cdd:TIGR02857 325 SGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 PVLVPGTVRHNLVLLGPV---DDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:TIGR02857 405 PFLFAGTIAENIRLARPDasdAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15608759 475 PTAHLDARTEQHVLgAIVERARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:TIGR02857 485 PTAHLDAETEAEVL-EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
2-292 |
1.63e-89 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 276.21 E-value: 1.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 2 ACGVGISGCAIGSAIVLASIVAGVIDPAnpgmAGLRRWLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLT 81
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEG----AGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 82 AVTARRPSQLAAQRDAAAV-LITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIG 160
Cdd:cd18584 79 RLLALGPALLRRQSSGELAtLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 161 LATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALV 240
Cdd:cd18584 159 KAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 241 AVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKA 292
Cdd:cd18584 239 AVYIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-507 |
2.02e-85 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 275.57 E-value: 2.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIdpanpgMAGLRR--WLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQ 78
Cdd:PRK11174 28 ILLGFLSGLLLIAQAWLLATILQALI------IENIPReaLLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIRQQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 79 VLTAVTARRPSQLAaQRDAA--AVLITRGLDGLRPYFTGYLPTLLLAAILTPATVAVI-------GLydlksmaIVVITL 149
Cdd:PRK11174 102 VLDKLQQLGPAWIQ-GKPAGswATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVfpinwaaGL-------ILLGTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 150 PLIPIFMVLIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVL 229
Cdd:PRK11174 174 PLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 230 ELLATLGVALVAVGIGL----RLVFG----EMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLgESPS 301
Cdd:PRK11174 254 EFFASISIALVAVYFGFsylgELNFGhygtGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFL-ETPL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 302 PTP--GRRTVTARGGV-IRLERLSVRGRDGRA---PYDLTadIEPGRVTVLTGRNGAGKSTTLQAIAGLtAPSSGRITVA 375
Cdd:PRK11174 333 AHPqqGEKELASNDPVtIEAEDLEILSPDGKTlagPLNFT--LPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKIN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 376 GVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlVLLGPVD----DLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSL 451
Cdd:PRK11174 410 GIELRELDPESWRKHLSWVGQNPQLPHGTLRDN-VLLGNPDasdeQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 452 GQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIvERARAGATVLVVAHR 507
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL-NAASRRQTTLMVTHQ 543
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-518 |
4.34e-83 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 268.96 E-value: 4.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIDPANpgMAGLRRWLGplsILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:COG1132 27 LLLLLLSALLELLLPLLLGRIIDALLAGGD--LSALLLLLL---LLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTARRPSQLAAQRDAAAV-LITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLI 159
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLsRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 160 GLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVAL 239
Cdd:COG1132 182 GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 240 VAVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPSPT--PGRRTVTARGGVIR 317
Cdd:COG1132 262 VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPdpPGAVPLPPVRGEIE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 318 LERLSVRGRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQ 396
Cdd:COG1132 342 FENVSFSYPGDRPVLkDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 RPVLVPGTVRHNLvLLG----PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:COG1132 422 DTFLFSGTIRENI-RYGrpdaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15608759 473 DEPTAHLDARTEQHVLGAIvERARAGATVLVVAHR-QQVAAAgDRVV 518
Cdd:COG1132 501 DEATSALDTETEALIQEAL-ERLMKGRTTIVIAHRlSTIRNA-DRIL 545
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-518 |
2.20e-71 |
|
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: 241.28 E-value: 2.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 16 IVLASIVAGVIDPANPGM----------AGLRRWLGPLSI-LLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVT 84
Cdd:COG2274 161 VLLASLLINLLALATPLFtqvvidrvlpNQDLSTLWVLAIgLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 85 ARRPSQLAAQRdaAAVLITR--GLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLipifMVLIGLA 162
Cdd:COG2274 241 RLPLSFFESRS--VGDLASRfrDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPL----YVLLGLL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 163 TTNP----SAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVA 238
Cdd:COG2274 315 FQPRlrrlSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 239 LVaVGIGLRLVF-GEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPSPTPGRRTVTARG--GV 315
Cdd:COG2274 395 AL-LWLGAYLVIdGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRlkGD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSW 393
Cdd:COG2274 474 IELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPGTVRHNLVLLGP---VDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:COG2274 554 VLQDVFLFSGTIRENITLGDPdatDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIvERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:COG2274 634 ILDEATSALDAETEAIILENL-RRLLKGRTVIIIAHRLSTIRLADRII 680
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
120-519 |
2.13e-66 |
|
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: 224.65 E-value: 2.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 120 LLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFM-VLIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRAS 198
Cdd:COG4987 136 LLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 199 GPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVAVgIGLRLVFGEMSLTAGLTVLLLAP----EVYWPLRR 274
Cdd:COG4987 216 RALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLW-LAAPLVAAGALSGPLLALLVLAAlalfEALAPLPA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 275 VgvqFHAAADGRTAADKAFALLGESPS-PTPGRRTVTARGGVIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNG 351
Cdd:COG4987 295 A---AQHLGRVRAAARRLNELLDAPPAvTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVldGLSLTLPPGERVAIVGPSG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 352 AGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGP---VDDLERACAAAGFD 428
Cdd:COG4987 372 SGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPdatDEELWAALERVGLG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 429 AVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERArAGATVLVVAHRQ 508
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL 530
|
410
....*....|.
gi 15608759 509 QVAAAGDRVVE 519
Cdd:COG4987 531 AGLERMDRILV 541
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
316-518 |
1.31e-45 |
|
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: 157.54 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRgRDGRAPY---DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLS 392
Cdd:cd03228 1 IEFKNVSFS-YPGRPKPvlkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPGTVRHNLvllgpvddleracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 473 DEPTAHLDARTEQHVLGAIvERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03228 121 DEATSALDPETEALILEAL-RALAKGKTVIVIAHRLSTIRDADRII 165
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
104-518 |
3.18e-45 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 168.89 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 104 RGLDGLRPYFTGylpTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIfMVLIGLATTNP----SAAALAAMTAVQA 179
Cdd:TIGR03375 250 REFESVRDFFTS---ATLTALIDLPFALLFLLVIAIIGGPLVWVPLVAIPL-ILLPGLLLQRPlsrlAEESMRESAQRNA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 180 RLLDLIAGIPTLRALGrASGPEQRIAELSADHrrSAMATLRIAFLSALVLELLATL----GVALVAVGIGLRLVfGEMSL 255
Cdd:TIGR03375 326 VLVESLSGLETIKALN-AEGRFQRRWEQTVAA--LARSGLKSRFLSNLATNFAQFIqqlvSVAIVVVGVYLISD-GELTM 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 256 TAGLTVLLLAPEVYWPLRRVG---VQFHAAADGRTAADKAFALlgesPSPTPGRRTVTARG---GVIRLERLSVR--GRD 327
Cdd:TIGR03375 402 GGLIACVMLSGRALAPLGQLAgllTRYQQAKTALQSLDELMQL----PVERPEGTRFLHRPrlqGEIEFRNVSFAypGQE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 328 GRAPYDLTADIEPG-RVTVLtGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVR 406
Cdd:TIGR03375 478 TPALDNVSLTIRPGeKVAII-GRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLR 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNLVLLGP-VDDLE--RACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDART 483
Cdd:TIGR03375 557 DNIALGAPyADDEEilRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRS 636
|
410 420 430
....*....|....*....|....*....|....*
gi 15608759 484 EQHVLgAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:TIGR03375 637 EERFK-DRLKRWLAGKTLVLVTHRTSLLDLVDRII 670
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
314-518 |
1.77e-44 |
|
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: 156.50 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 314 GVIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQL 391
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVlkNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVPGTVRHNLVLLGPVDD--LERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDeeLWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15608759 470 LLLDEPTAHLDARTEQHVLGAIvERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTIIDSDRIL 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
45-517 |
1.13e-43 |
|
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: 163.00 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 45 ILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVTARrpSQLAAQRDAAAVLitRGLDGLRPYFTGYLPTLLLAA 124
Cdd:COG4618 65 LALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRA--ALRGGGGAAAQAL--RDLDTLRQFLTGPGLFALFDL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 125 ILTPATVAVIGLYD--LKSMAIVVItlplipIFMVLIGL----ATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRAS 198
Cdd:COG4618 141 PWAPIFLAVLFLFHplLGLLALVGA------LVLVALALlnerLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 199 GPEQRIAELSADHRR-SAMATLRIAFLSALVLELLATLGVALVAVGIGLRLvfgEMSLTAGL----TVLL---LAPEVY- 269
Cdd:COG4618 215 ALRRRWQRANARALAlQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVI---QGEITPGAmiaaSILMgraLAPIEQa 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 270 ---WPlrrvgvQFHAAadgRTAADKAFALLGESPSPTPGRRTVTARGgVIRLERLSVRGRDGRAP--YDLTADIEPGRVT 344
Cdd:COG4618 292 iggWK------QFVSA---RQAYRRLNELLAAVPAEPERMPLPRPKG-RLSVENLTVVPPGSKRPilRGVSFSLEPGEVL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 345 VLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDD--LERAC 422
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPekVVAAA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 423 AAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARAL-GSPaAVLLLDEPTAHLDARTEQHVLGAIVERARAGATV 501
Cdd:COG4618 442 KLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALyGDP-RLVVLDEPNSNLDDEGEAALAAAIRALKARGATV 520
|
490
....*....|....*.
gi 15608759 502 LVVAHRQQVAAAGDRV 517
Cdd:COG4618 521 VVITHRPSLLAAVDKL 536
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
316-506 |
3.94e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSWLP 395
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:COG1131 80 QEPALYPDlTVRENLRFFARLYGLPRKEARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTH 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-522 |
2.48e-41 |
|
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: 147.74 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GP-VDD--LERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03245 102 APlADDerILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE 181
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 490 AIvERARAGATVLVVAHRQQVAAAGDRVVEVNS 522
Cdd:cd03245 182 RL-RQLLGDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
316-525 |
3.86e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPGTVRHNLV----LLGPVDDLERACAAagfdavLDELprGLDT-VLGRGGVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:COG4619 81 QEPALWGGTVRDNLPfpfqLRERKFDRERALEL------LERL--GLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH-RQQVAAAGDRVVEVNSDGF 525
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
315-518 |
1.54e-39 |
|
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: 143.84 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLaPAAWWRQLSWL 394
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLD 473
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 474 EPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVV 203
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
202-518 |
5.33e-39 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 149.87 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 202 QRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVAVGIGLRLVFGemSLTAG-LTVLLLAP-EVYWPLRRVGVQF 279
Cdd:TIGR02203 217 RRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAG--SLTAGdFTAFITAMiALIRPLKSLTNVN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 280 HAAADGRTAADKAFALLGESPSPTPGRRTVTARGGVIRLERLSVR--GRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTT 357
Cdd:TIGR02203 295 APMQRGLAAAESLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRypGRDRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 358 LQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVD----DLERACAAAGFDAVLDE 433
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQadraEIERALAAAYAQDFVDK 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 434 LPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIvERARAGATVLVVAHRQQVAAA 513
Cdd:TIGR02203 455 LPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL-ERLMQGRTTLVIAHRLSTIEK 533
|
....*
gi 15608759 514 GDRVV 518
Cdd:TIGR02203 534 ADRIV 538
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
120-507 |
8.11e-39 |
|
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: 148.66 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 120 LLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLI-GLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRAS 198
Cdd:TIGR02868 134 AGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVsLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 199 GPEQRIAELSADHRRSAMATLRIAFLSALVLEL---LATLGVALVAVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRV 275
Cdd:TIGR02868 214 AALAQVEEADRELTRAERRAAAATALGAALTLLaagLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 276 GVQFHAAadgRTAADKAFALLG-ESPSPT---PGRRTVTARGGVIRLERLSVRGRDG-RAPYDLTADIEPGRVTVLTGRN 350
Cdd:TIGR02868 294 AQQLTRV---RAAAERIVEVLDaAGPVAEgsaPAAGAVGLGKPTLELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 351 GAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPV---DDLERACAAAGF 427
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDatdEELWAALERVGL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 428 DAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVErARAGATVLVVAHR 507
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-507 |
1.37e-38 |
|
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: 141.14 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlVLL 412
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN-IRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 G----PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:cd03249 100 GkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQ 179
|
170
....*....|....*....
gi 15608759 489 GAIvERARAGATVLVVAHR 507
Cdd:cd03249 180 EAL-DRAMKGRTTIVIAHR 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-507 |
1.50e-38 |
|
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: 140.82 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GP---VDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03254 101 RPnatDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
170
....*....|....*...
gi 15608759 490 AIvERARAGATVLVVAHR 507
Cdd:cd03254 181 AL-EKLMKGRTSIIIAHR 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
315-520 |
1.74e-37 |
|
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: 136.84 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRgRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSW 393
Cdd:COG4133 2 MLEAENLSCR-RGERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPG-TVRHNLVLL-------GPVDDLERACAAAGFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARALGS 465
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWaalyglrADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 466 PAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHrQQVAAAGDRVVEV 520
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH-QPLELAAARVLDL 202
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
316-518 |
1.03e-36 |
|
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: 136.08 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRdGRAPY---DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLS 392
Cdd:cd03252 1 ITFEHVRFRYK-PDGPVildNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPGTVRHNLVLLGPVDDLERACAA---AGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAaklAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15608759 470 LLLDEPTAHLDARTEqHVLGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03252 160 LIFDEATSALDYESE-HAIMRNMHDICAGRTVIIIAHRLSTVKNADRII 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
316-518 |
2.45e-35 |
|
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: 130.03 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSW 393
Cdd:cd03246 1 LEVENVSFRYPGAEPPvlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPGTVRHNLvllgpvddleracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARAL-GSPaAVLLL 472
Cdd:cd03246 81 LPQDDELFSGSIAENI---------------------------------------LSGGQRQRLGLARALyGNP-RILVL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 473 DEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRIL 166
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
333-477 |
1.37e-34 |
|
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: 127.38 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 412 LGPVDDLERACAAAGFDAVLDELPRG--LDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTA 477
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-518 |
1.79e-34 |
|
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: 129.66 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GP---VDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03251 100 RPgatREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQA 179
|
170 180
....*....|....*....|....*....
gi 15608759 490 AIvERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03251 180 AL-ERLMKNRTTFVIAHRLSTIENADRIV 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
45-524 |
2.10e-34 |
|
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: 136.32 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 45 ILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAV---TARRPSQLAAQrdaaavlITRGLDGLRPYFTGYLPTLL 121
Cdd:TIGR01842 51 LALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASfsaTLRRGSGDGLQ-------ALRDLDQLRQFLTGPGLFAF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 122 LAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPE 201
Cdd:TIGR01842 124 FDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 202 QRIAELSADHRRS-AMATLRIAFLSALVLELLATLGVALVAVGiGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFH 280
Cdd:TIGR01842 204 KRWGRFHSKYLSAqSAASDRAGMLSNLSKYFRIVLQSLVLGLG-AYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 281 AAADGRTAADKAFALLGESPSPTPgRRTVTARGGVIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTL 358
Cdd:TIGR01842 283 QFSGARQAYKRLNELLANYPSRDP-AMPLPEPEGHLSVENVTIVPPGGKKPTlrGISFSLQAGEALAIIGPSGSGKSTLA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 359 QAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDDLERACAAA---GFDAVLDELP 435
Cdd:TIGR01842 362 RLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAklaGVHELILRLP 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 436 RGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGD 515
Cdd:TIGR01842 442 DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVD 521
|
....*....
gi 15608759 516 RVVeVNSDG 524
Cdd:TIGR01842 522 KIL-VLQDG 529
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
316-521 |
7.65e-34 |
|
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: 125.97 E-value: 7.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSWLP 395
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVllgpvddleracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03230 80 EEPSLYENlTVRENLK--------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAG-DRVVEVN 521
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLcDRVAILN 169
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
315-521 |
8.30e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 8.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDvtnlaPAAWWRQLSWL 394
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVL---VPGTVRhNLVLLG---------PVDDLERACAaagfDAVLDELprGLDTVLGRGgVG-LSLGQRQRLGLAR 461
Cdd:COG1121 81 PQRAEVdwdFPITVR-DVVLMGrygrrglfrRPSRADREAV----DEALERV--GLEDLADRP-IGeLSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH-RQQVAAAGDRVVEVN 521
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHdLGAVREYFDRVLLLN 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
315-518 |
8.52e-34 |
|
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: 128.62 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLVPG-TVRhNLVLLG----------PVDDLERACAAAgFDAV-LDEL-PRGLDTvlgrggvgLSLGQRQRLGLAR 461
Cdd:COG1120 81 PQEPPAPFGlTVR-ELVALGryphlglfgrPSAEDREAVEEA-LERTgLEHLaDRPVDE--------LSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERAR-AGATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDlNLAARYADRLV 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
316-518 |
2.29e-33 |
|
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: 126.09 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03259 79 QDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 475 PTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03259 157 PLSALDAKLREELREELKElQRELGITTIYVTHDQEEALAlADRIA 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-507 |
2.59e-33 |
|
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: 126.58 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlVLL 412
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYN-IRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVD----DLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:cd03253 98 GRPDatdeEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ 177
|
170
....*....|....*....
gi 15608759 489 GAIvERARAGATVLVVAHR 507
Cdd:cd03253 178 AAL-RDVSKGRTTIVIAHR 195
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
315-524 |
4.25e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAP---AAW 387
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQ-LSWLPQRPVLVPG-TVRHNLVL------LGPVDDLERAcaaagfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGL 459
Cdd:COG1136 84 RRRhIGFVFQFFNLLPElTALENVALplllagVSRKERRERA------RELLERV--GLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 460 ARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAAAGDRVVEVnSDG 524
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRL-RDG 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
317-518 |
4.76e-33 |
|
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: 123.12 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQ 396
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 rpvlvpgtvrhnlvllgpvddleracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDEPT 476
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 477 AHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAA-AGDRVV 518
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVI 151
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
317-521 |
1.54e-32 |
|
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: 123.80 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLapaawWRQLSWLPQ 396
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 RPVL---VPGTVRHnLVLLGPVDD--LERACAAAGFDAVldelprglDTVLGRGGVG---------LSLGQRQRLGLARA 462
Cdd:cd03235 76 RRSIdrdFPISVRD-VVLMGLYGHkgLFRRLSKADKAKV--------DEALERVGLSeladrqigeLSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 463 LGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH-RQQVAAAGDRVVEVN 521
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHdLGLVLEYFDRVLLLN 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
316-524 |
3.85e-32 |
|
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: 122.98 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWW--- 388
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 389 -RQLSWLPQRPVLVPG-TVRHNLVL---LGPVDDLERACAAAgfdAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARAL 463
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELpllLAGVPKKERRERAE---ELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 464 GSPAAVLLLDEPTAHLDARTEQHVLGAIVERAR-AGATVLVVAHRQQVAAAGDRVVEVnSDG 524
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEYADRIIEL-RDG 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
317-518 |
1.60e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.85 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQ 396
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 rpvlvpgtvrhnlvllgpvddlerACAAAGfdaVLDELPRGLDTvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDEPT 476
Cdd:cd03214 81 ------------------------ALELLG---LAHLADRPFNE--------LSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 477 AHLDARTEQHVLGAIVERARA-GATVLVVAHR-QQVAAAGDRVV 518
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDlNLAARYADRVI 169
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
317-521 |
2.45e-30 |
|
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: 117.57 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVR--GRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:cd03225 1 ELKNLSFSypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPvlvpgtvRHNLVLLGPVDDLERACAAAGFDAvlDELPRGLDTVLGRGGVG---------LSLGQRQRLGLARALGS 465
Cdd:cd03225 81 FQNP-------DDQFFGPTVEEEVAFGLENLGLPE--EEIEERVEEALELVGLEglrdrspftLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 466 PAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLE 208
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
333-524 |
5.16e-30 |
|
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: 124.47 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLvLL 412
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL-LL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 G-----PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV 487
Cdd:TIGR01193 571 GakenvSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI 650
|
170 180 190
....*....|....*....|....*....|....*..
gi 15608759 488 LGAIVERARagATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:TIGR01193 651 VNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-518 |
7.03e-30 |
|
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: 116.76 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLV 410
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVEENLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LlgPVDDLERACAAAGFDAVLDELPRgLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGA 490
Cdd:cd03224 98 L--GAYARRRAKRKARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180
....*....|....*....|....*....
gi 15608759 491 IVERARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03224 175 IRELRDEGVTILLVEQNARFALEiADRAY 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-518 |
7.61e-30 |
|
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: 116.03 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwrQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGTIRENILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDD--LERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG- 489
Cdd:cd03250 90 KPFDEerYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEn 169
|
170 180
....*....|....*....|....*....
gi 15608759 490 AIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03250 170 CILGLLLNNKTRILVTHQLQLLPHADQIV 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-522 |
8.33e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 295 LLGESPSPTPGRRTVTA--RGGVIRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSG 370
Cdd:PLN03232 1212 LPSEATAIIENNRPVSGwpSRGSIKFEDVHLRYRPGLPPvlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKG 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 371 RITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDD--LERACAAAGFDAVLDELPRGLDTVLGRGGVG 448
Cdd:PLN03232 1292 RIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDadLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 449 LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAgATVLVVAHRQQVAAAGDRVVEVNS 522
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIIDCDKILVLSS 1444
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
287-507 |
1.13e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.63 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 287 TAADKAFALLGESPSPT-PGRRTVTARGGVIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAG 363
Cdd:PRK11160 309 ASARRINEITEQKPEVTfPTTSTAAADQVSLTLNNVSFTYPDQPQPVlkGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 364 LTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDDLERACAA---AGFDAVLDElPRGLDT 440
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVlqqVGLEKLLED-DKGLNA 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 441 VLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARaGATVLVVAHR 507
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR 533
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-524 |
4.16e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 121.07 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 294 ALLGESPSPTPGRRTVTARGGVIRLERLSVRGRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRI 372
Cdd:COG4178 341 ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 373 TVagvdvtnlaPAAwwRQLSWLPQRPVLVPGTVRHNLVLLGPVDDLERACAAAGFDAV-LDELPRGLDTVLGRGGVgLSL 451
Cdd:COG4178 421 AR---------PAG--ARVLFLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVgLGHLAERLDEEADWDQV-LSL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 452 GQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERaRAGATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
316-518 |
4.48e-29 |
|
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: 114.74 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPV--LVPGTVRHNlVLLGPVD-DLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:COG1122 81 FQNPDdqLFAPTVEED-VAFGPENlGLPREEIRERVEEALELV--GLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 472 LDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVI 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
315-518 |
1.17e-28 |
|
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: 119.24 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS---SGRITVAGVDVTNLAPAAWWR 389
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 390 QLSWLPQRP--VLVPGTVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPA 467
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 468 AVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAG-DRVV 518
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIaDRVV 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
185-518 |
1.52e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 120.21 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 185 IAGIPTLRALG----RASGPEQRIAELSADHRRSAMAtlRIAFLsaLVLELLAtLGVALVAVGIGLRLVF-GEMSLTAGL 259
Cdd:TIGR00958 347 LSGMRTVRSFAaeegEASRFKEALEETLQLNKRKALA--YAGYL--WTTSVLG-MLIQVLVLYYGGQLVLtGKVSSGNLV 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 260 TVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPS-PTPGRRTVTARGGVIRLERLSV---RGRDGRAPYDLT 335
Cdd:TIGR00958 422 SFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNiPLTGTLAPLNLEGLIEFQDVSFsypNRPDVPVLKGLT 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 336 ADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlVLLG-- 413
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN-IAYGlt 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 414 --PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAi 491
Cdd:TIGR00958 581 dtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES- 659
|
330 340
....*....|....*....|....*..
gi 15608759 492 veRARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:TIGR00958 660 --RSRASRTVLLIAHRLSTVERADQIL 684
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
316-521 |
1.65e-28 |
|
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: 112.31 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAawWRQLSWLP 395
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAaagfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03268 79 EAPGFYPNlTARENLRLLARLLGIRKKRI----DEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAHR----QQVAaagDRVVEVN 521
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLlseiQKVA---DRIGIIN 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
316-518 |
2.03e-28 |
|
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: 112.66 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL-----TAPSSGRITVAGVDVTNLAPAAWW-- 388
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 389 RQLSWLPQRPVLVPGTVRHNlVLLGP----------VDDLERACA--AAGFDAVLDELprgldtvlgrGGVGLSLGQRQR 456
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDN-VAYGLrlhgiklkeeLDERVEEALrkAALWDEVKDRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 457 LGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAgATVLVVAHR-QQVAAAGDRVV 518
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNmQQAARVADRTA 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
316-518 |
2.16e-28 |
|
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: 112.46 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVtNLAPAAWWRQL 391
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
333-518 |
2.62e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVdvtnlapaawwRQLSWLPQR---PVLVPGTVRhNL 409
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRsevPDSLPLTVR-DL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VLLG--PVDDLERACAAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:NF040873 78 VAMGrwARRGLWRRLTRDDRAAVDDALERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 487 VLGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:NF040873 158 IIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
234-507 |
6.05e-28 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 117.61 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 234 TLGVALVAVGIGLRLVFGEMSLtaGLTVL--LLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPSPT--PGRRTV 309
Cdd:COG5265 274 ALGLTAMMLMAAQGVVAGTMTV--GDFVLvnAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVAdaPDAPPL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 310 TARGGVIRLERLSVrGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAW 387
Cdd:COG5265 352 VVGGGEVRFENVSF-GYDPERPilKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQLSWLPQRPVLVPGTVRHNLVLLGP---VDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALG 464
Cdd:COG5265 431 RAAIGIVPQDTVLFNDTIAYNIAYGRPdasEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIvERARAGATVLVVAHR 507
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAAL-REVARGRTTLVIAHR 552
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
4-291 |
1.34e-27 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 111.99 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 4 GVGISGCAIGSAIVLASIVAGVIdpanpGMAGLRRWLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAV 83
Cdd:cd18561 5 GLLITALYIAQAWLLARALARIF-----AGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 84 TARRPSQLAAQRDAAAVLI-TRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIGLA 162
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTvVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 163 TTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVAV 242
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15608759 243 GIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADK 291
Cdd:cd18561 240 VGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADS 288
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
201-507 |
1.86e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 116.27 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 201 EQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVAVGIGLRLVFGEmsLTAG-LTVL------LLAPevYWPLR 273
Cdd:PRK11176 227 TKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDT--LTAGtITVVfssmiaLMRP--LKSLT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 274 RVGVQFHAaadGRTAADKAFALLGESPSPTPGRRTVTARGGVIRLERLSV--RGRDGRAPYDLTADIEPGRVTVLTGRNG 351
Cdd:PRK11176 303 NVNAQFQR---GMAACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFtyPGKEVPALRNINFKIPAGKTVALVGRSG 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 352 AGKSTtlqaIAGLTAP----SSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLG----PVDDLERACA 423
Cdd:PRK11176 380 SGKST----IANLLTRfydiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteqySREQIEEAAR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 424 AAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIvERARAGATVLV 503
Cdd:PRK11176 456 MAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL-DELQKNRTSLV 534
|
....
gi 15608759 504 VAHR 507
Cdd:PRK11176 535 IAHR 538
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
316-518 |
3.23e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHN----LVLLG-PVDDLERACAAA----GFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLARALGS 465
Cdd:COG3839 82 QSYALYPHmTVYENiafpLKLRKvPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608759 466 PAAVLLLDEPTAHLDA------RTEqhvlgaIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:COG3839 151 EPKVFLLDEPLSNLDAklrvemRAE------IKRlHRRLGTTTIYVTHDQVEAMTlADRIA 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
218-517 |
3.45e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 116.76 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 218 TLRIAFLSALVLELLATLGV---------ALVAVGIGLRLVFGeMSLTAGLTVLL----LAPEVYWPLRRVGVQFHAAAD 284
Cdd:PLN03130 1140 AIRLETLGGLMIWLTASFAVmqngraenqAAFASTMGLLLSYA-LNITSLLTAVLrlasLAENSLNAVERVGTYIDLPSE 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 285 GrtaadkafALLGESPSPTPGRRTvtarGGVIRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIA 362
Cdd:PLN03130 1219 A--------PLVIENNRPPPGWPS----SGSIKFEDVVLRYRPELPPvlHGLSFEISPSEKVGIVGRTGAGKSSMLNALF 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 363 GLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDD------LERacaaAGFDAVLDELPR 436
Cdd:PLN03130 1287 RIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDadlwesLER----AHLKDVIRRNSL 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 437 GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAgATVLVVAHRQQVAAAGDR 516
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS-CTMLIIAHRLNTIIDCDR 1441
|
.
gi 15608759 517 V 517
Cdd:PLN03130 1442 I 1442
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
314-521 |
1.07e-26 |
|
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: 107.50 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 314 GVIRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQL 391
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPvlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVPGTVRHNLVLLGPVDDleracaaagfdavlDELPRGLDtvLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDEYSD--------------EEIYGALR--VSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15608759 472 LDEPTAHLDARTEqHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVEVN 521
Cdd:cd03369 149 LDEATASIDYATD-ALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMD 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
333-504 |
1.17e-26 |
|
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: 108.15 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLv 410
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSlTVEENL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LLGPVDDLERACAAAGFDAVLDELPRgLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGA 490
Cdd:COG0410 100 LLGAYARRDRAEVRADLERVYELFPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEI 178
|
170
....*....|....
gi 15608759 491 IVERARAGATVLVV 504
Cdd:COG0410 179 IRRLNREGVTILLV 192
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-518 |
1.26e-26 |
|
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: 106.24 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLApAAWWRQLSWLPQRPVLVPGTVRHNLvll 412
Cdd:cd03247 20 NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 gpvddleracaaagfdavldelprgldtvlgrgGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIV 492
Cdd:cd03247 96 ---------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
|
170 180
....*....|....*....|....*.
gi 15608759 493 ERARaGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03247 143 EVLK-DKTLIWITHHLTGIEHMDKIL 167
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
315-518 |
2.35e-26 |
|
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: 106.82 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPA---AW 387
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQLSWLPQRP--VLVPG-TVRHN----LVLLGPVDDLERACAAAGFDAVLDELPRgldTVLGRGGVGLSLGQRQRLGLA 460
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRmTIGEQiaepLRIHGKLSKKEARKEAVLLLLVGVGLPE---EVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 461 RALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKiADRVA 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
313-525 |
2.68e-26 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 107.69 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 313 GGVIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ 390
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVlkHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSWLPQRPVLVPGTVRHNLvllgpvdDLERACA---------AAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLAR 461
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL-------DPECKCTddrlwealeIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEqHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVeVNSDGF 525
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVSTILDADLVL-VLSRGI 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
316-522 |
3.89e-26 |
|
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: 106.88 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVR-GRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAA---WWRQL 391
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVPG-TV----------RHNL--VLLGPVDDLERACAAAGFDAVldelprGLDTVLGRGGVGLSLGQRQRLG 458
Cdd:cd03256 81 GMIFQQFNLIERlSVlenvlsgrlgRRSTwrSLFGLFPKEEKQRALAALERV------GLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 459 LARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAAA-GDRVVEVNS 522
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREyADRIVGLKD 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-518 |
4.18e-26 |
|
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: 106.40 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVL- 411
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LG--PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03248 112 LQscSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170 180
....*....|....*....|....*....
gi 15608759 490 AIVERARAgATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03248 192 ALYDWPER-RTVLVIAHRLSTVERADQIL 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
316-518 |
5.22e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.03 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNlVLLGP-VDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLD 473
Cdd:COG3842 84 QDYALFPHlTVAEN-VAFGLrMRGVPKAEIRARVAELLELV--GLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15608759 474 EPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:COG3842 161 EPLSALDAKLREEMREELRRlQRELGITFIYVTHDQEEALAlADRIA 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
333-518 |
6.52e-26 |
|
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: 105.98 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLV 410
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 L------------LGPVDDLERACAAAgfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:cd03219 98 VaaqartgsglllARARREEREARERA--EELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 479 LDARTEQHVLGAIVERARAGATVLVVAHRQQ-VAAAGDRVV 518
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVLLVEHDMDvVMSLADRVT 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
310-506 |
6.94e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 310 TARGGVIRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPa 385
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVtaldDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 386 awwrQLSWLPQRPVLVP-GTVRHNlVLLGP-VDDLERACAAAGFDAVLDELprGLdtvlgrGGVG------LSLGQRQRL 457
Cdd:COG1116 81 ----DRGVVFQEPALLPwLTVLDN-VALGLeLRGVPKAERRERARELLELV--GL------AGFEdayphqLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 458 GLARALGSPAAVLLLDEPTAHLDARTE---QHVLGAIVEraRAGATVLVVAH 506
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRerlQDELLRLWQ--ETGKTVLFVTH 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
106-507 |
7.60e-26 |
|
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: 112.31 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 106 LDGLRPYFTGYLPTLLLAAILTPATVAVIGLYdlksmaIVVITLPLIPIFMVLIG--LATTNP-SAAALAAMTAVQARLL 182
Cdd:TIGR01271 995 IDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPY------IFIAAIPVAVIFIMLRAyfLRTSQQlKQLESEARSPIFSHLI 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 183 DLIAGIPTLRALGRASGPEQRIAELSADHRRS---AMATLR----------IAFLSALVLELLATLGVALVAVGIGLRLV 249
Cdd:TIGR01271 1069 TSLKGLWTIRAFGRQSYFETLFHKALNLHTANwflYLSTLRwfqmridiifVFFFIAVTFIAIGTNQDGEGEVGIILTLA 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 250 fgeMSLTAGLTvlllapevyWplrrvGVQFHAAADG-RTAADKAFALLG---ESPSPTPGRRTVTA-------------- 311
Cdd:TIGR01271 1149 ---MNILSTLQ---------W-----AVNSSIDVDGlMRSVSRVFKFIDlpqEEPRPSGGGGKYQLstvlvienphaqkc 1211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 312 --RGGVIRLERLSVR-GRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLtAPSSGRITVAGVDVTNLAPAAW 387
Cdd:TIGR01271 1212 wpSGGQMDVQGLTAKyTEAGRAVLqDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTW 1290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQLSWLPQRPVLVPGTVRHNLVLLGPVDDLE--RACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGS 465
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEiwKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15608759 466 PAAVLLLDEPTAHLDARTEQhVLGAIVERARAGATVLVVAHR 507
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQ-IIRKTLKQSFSNCTVILSEHR 1411
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
316-522 |
1.96e-25 |
|
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: 103.04 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT--NLAPAAWWRQLSW 393
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPG-TVRHNLVLlgpvddleracaaagfdavldelprgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:cd03229 81 VFQDFALFPHlTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 473 DEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQ-QVAAAGDRVVEVNS 522
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLdEAARLADRVVVLRD 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
316-524 |
2.18e-25 |
|
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: 102.12 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQlswlp 395
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 qrpvlvpgtvrhnlvllgpvddleracaaagfdavldelprgldtvlgrgGVG----LSLGQRQRLGLARALGSPAAVLL 471
Cdd:cd03216 76 --------------------------------------------------GIAmvyqLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15608759 472 LDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVVeVNSDG 524
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVT-VLRDG 158
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
316-522 |
2.56e-25 |
|
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: 103.49 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03301 79 QNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15608759 475 PTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVVEVNS 522
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRlQQRLGTTTIYVTHDQVEAMTmADRIAVMND 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
316-506 |
4.51e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPGTVRHNLVLLG-----------PVDD---LERACAAAGFDAVLDelpRGLDTvlgrggvgLSLGQRQRLGLAR 461
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwlslwgrlSAEDnarVNQAMEQTRINHLAD---RRLTD--------LSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
316-506 |
5.46e-25 |
|
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: 102.66 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGrVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSWLP 395
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03264 79 QEFGVYPNfTVREFLDYIAWLKGIPSKEVKARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 475 PTAHLDARtEQHVLGAIVERARAGATVLVVAH 506
Cdd:cd03264 157 PTAGLDPE-ERIRFRNLLSELGEDRIVILSTH 187
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
315-518 |
1.30e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLV-PGTVrHNLVLLGPVDD-LERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARAL------GSP 466
Cdd:PRK13548 82 PQHSSLSfPFTV-EEVVAMGRAPHgLSRAEDDALVAAALAQV--DLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15608759 467 AAVLLLDEPTAHLDARTEQHVLGAIVERAR-AGATVLVVAHRQQVAAA-GDRVV 518
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNLAARyADRIV 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-507 |
1.32e-24 |
|
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: 103.40 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTApSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLE--RACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQhVLGA 490
Cdd:cd03289 101 GKWSDEEiwKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ-VIRK 179
|
170
....*....|....*..
gi 15608759 491 IVERARAGATVLVVAHR 507
Cdd:cd03289 180 TLKQAFADCTVILSEHR 196
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
316-518 |
2.03e-24 |
|
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: 101.39 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaawwrQL 391
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVP-GTVRHNlVLLGP-VDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:cd03293 76 GYVFQQDALLPwLTVLDN-VALGLeLQGVPKAEARERAEELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 470 LLLDEPTAHLDARTEQHV---LGAIVERARagATVLVVAHrqQVAAA---GDRVV 518
Cdd:cd03293 153 LLLDEPFSALDALTREQLqeeLLDIWRETG--KTVLLVTH--DIDEAvflADRVV 203
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-518 |
2.56e-24 |
|
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: 101.04 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQ-LSWLPQRPVLVPG-TVRHNLV 410
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA--RQsLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTeQHVLGA 490
Cdd:cd03263 98 FYARLKGLPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS-RRAIWD 174
|
170 180
....*....|....*....|....*....
gi 15608759 491 IVERARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03263 175 LILEVRKGRSIILTTHSMDEAEAlCDRIA 203
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
105-518 |
8.86e-24 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 105.42 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 105 GLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKsMAIVVITLPLIPI-FMVLIGLATTNPSAAALAAMTAVQARLLD 183
Cdd:TIGR03797 241 GISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWK-LALVAVALALVAIaVTLVLGLLQVRKERRLLELSGKISGLTVQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 184 LIAGIPTLR-------ALGRASGP--EQRIAELSADHRRSAMATLRIAF--LSALVLELLATLGVALVAVGIGLRLVF-- 250
Cdd:TIGR03797 320 LINGISKLRvagaenrAFARWAKLfsRQRKLELSAQRIENLLTVFNAVLpvLTSAALFAAAISLLGGAGLSLGSFLAFnt 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 251 -------GEMSLTAGLTVLLLAPEVYwplRRVGVQFHAAADGRTAadkafallgespSPTPGRRTvtargGVIRLERLSV 323
Cdd:TIGR03797 400 afgsfsgAVTQLSNTLISILAVIPLW---ERAKPILEALPEVDEA------------KTDPGKLS-----GAIEVDRVTF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 324 RGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLV 401
Cdd:TIGR03797 460 RYRPDGPLIldDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLM 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 PGTVRHNLVLLGPV--DDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:TIGR03797 540 SGSIFENIAGGAPLtlDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
410 420 430
....*....|....*....|....*....|....*....
gi 15608759 480 DARTEQHVLGAIverARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:TIGR03797 620 DNRTQAIVSESL---ERLKVTRIVIAHRLSTIRNADRIY 655
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
316-518 |
9.96e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRgRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:COG4559 2 LEAENLSVR-LGGRTLLdDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLV-PGTVRhNLVLLG--PVDDLERACAAAgFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARAL-------G 464
Cdd:COG4559 81 PQHSSLAfPFTVE-EVVALGraPHGSSAAQDRQI-VREALALV--GLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRIL 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
316-521 |
1.68e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTadIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAawwrqlswlp 395
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPV--------LVPG-TVRHNLVL-------LGPVD--DLERACAAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRL 457
Cdd:COG3840 70 ERPVsmlfqennLFPHlTVAQNIGLglrpglkLTAEQraQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 458 GLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDpEDAARIADRVLLVA 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
332-518 |
2.93e-23 |
|
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: 98.56 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 332 YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHNL- 409
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVYKNIa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 --VLLGPVDDLERacaaagfDAVLDELPR--GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQ 485
Cdd:cd03299 94 ygLKKRKVDKKEI-------ERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 486 HVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03299 167 KLREELKKiRKEFGVTVLHVTHDFEEAWAlADKVA 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
294-518 |
3.03e-23 |
|
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: 103.06 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 294 ALLGESPSPTPGRRTVTARGG----VIRLERLSVRGRDGRAPY-----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL 364
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAaaepLLEVRNLSKRYPVRGKGGvravdDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 365 TAPSSGRITVAGVDVTNL---APAAWWRQLSWLPQRPV--LVPG-TVRHN----LVLLGPVDDLER-ACAAAGFDAVlde 433
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNPRmTVGDIiaepLRLHGLLSRAERrERVAELLERV--- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 434 lprGLDT-VLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVA 511
Cdd:COG1123 392 ---GLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVV 468
|
....*...
gi 15608759 512 AA-GDRVV 518
Cdd:COG1123 469 RYiADRVA 476
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
316-518 |
4.40e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 98.34 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVR----GRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQL 391
Cdd:COG1124 2 LEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRP--VLVPgtvRHNL--VLLGPVDDLERACAAAGFDAVLDELprGLD-TVLGRGGVGLSLGQRQRLGLARALGSP 466
Cdd:COG1124 82 QMVFQDPyaSLHP---RHTVdrILAEPLRIHGLPDREERIAELLEQV--GLPpSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15608759 467 AAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDlREERGLTYLFVSHDLAVVAHlCDRVA 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
333-518 |
4.65e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.19 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLV 410
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 L-----------------LGPVDDLERACAAAgfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLD 473
Cdd:COG0411 102 VaaharlgrgllaallrlPRARREEREARERA--EELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 474 EPTAHLDArTEQHVLGAIVERARA--GATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG0411 178 EPAAGLNP-EETEELAELIRRLRDerGITILLIEHDmDLVMGLADRIV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
317-518 |
7.63e-23 |
|
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: 96.56 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDG-RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVtnlapAAWWRQlswlp 395
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERR----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPGTVRHNL--------VLLGpVDDLERACAAAgfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPA 467
Cdd:cd03226 71 KSIGYVMQDVDYQLftdsvreeLLLG-LKELDAGNEQA--ETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 468 AVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAA-AGDRVV 518
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAkVCDRVL 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
315-519 |
8.81e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 8.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVR-GRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPA--AWWR-- 389
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReiPYLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 390 --------QLswLPQRpvlvpgTVRHNLVL------LGPVDDLERAcaaagfDAVLDELprGLDTVLGRGGVGLSLGQRQ 455
Cdd:COG2884 81 igvvfqdfRL--LPDR------TVYENVALplrvtgKSRKEIRRRV------REVLDLV--GLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 456 RLGLARAL-GSPaAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH-RQQVAAAGDRVVE 519
Cdd:COG2884 145 RVAIARALvNRP-ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdLELVDRMPKRVLE 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-518 |
1.10e-22 |
|
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: 96.06 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlaPAAWWRQL----SWLPQRPVLVPG-TVRH 407
Cdd:cd03262 18 GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DKKNINELrqkvGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NlVLLGPVDDLERACAAAGFDAvLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:cd03262 96 N-ITLAPIKVKGMSKAEAEERA-LELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 487 VLGAIVERARAGATVLVVAHRQQVA-AAGDRVV 518
Cdd:cd03262 174 VLDVMKDLAEEGMTMVVVTHEMGFArEVADRVI 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-518 |
1.11e-22 |
|
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: 96.02 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 323 VRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVP 402
Cdd:cd03298 6 IRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 403 G-TVRHNLVL-------LGPVDD--LERACAAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:cd03298 84 HlTVEQNVGLglspglkLTAEDRqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 473 DEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVV 200
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
316-513 |
1.61e-22 |
|
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: 96.81 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRgRDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:TIGR03873 2 LRLSRVSWS-AGGRLIVDgVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQR-PVLVPGTVRhNLVLLGPVDDLER-ACAAAGFDAVLDEL--PRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:TIGR03873 81 EQDsDTAVPLTVR-DVVALGRIPHRSLwAGDSPHDAAVVDRAlaRTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAA 513
Cdd:TIGR03873 160 LLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAAS 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
316-522 |
1.72e-22 |
|
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: 96.15 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHN----LVLLG-PVDDLERACAAAgFDAVldelprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:cd03300 79 QNYALFPHlTVFENiafgLRLKKlPKAEIKERVAEA-LDLV------QLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 470 LLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVA-AAGDRVVEVNS 522
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRlQKELGITFVFVTHDQEEAlTMSDRIAVMNK 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
327-518 |
7.57e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.27 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 327 DGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGT 404
Cdd:PRK13657 345 DNSRQgvEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 405 VRHNLvLLGPVD----DLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK13657 425 IEDNI-RVGRPDatdeEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190
....*....|....*....|....*....|....*...
gi 15608759 481 ARTEQHVLGAIvERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13657 504 VETEAKVKAAL-DELMKGRTTFIIAHRLSTVRNADRIL 540
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
338-521 |
8.28e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 94.15 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVdvtnlAPAAWWRQLSWLPQR-------PVLVPGTVRHNLV 410
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdfPISVAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 -LLGPvddLERACAAaGFDAVLDELPRGLDTVLGRGGVG-LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:TIGR03771 78 gHIGW---LRRPCVA-DFAAVRDALRRVGLTELADRPVGeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 489 GAIVERARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDlAQAMATCDRVVLLN 187
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
316-521 |
1.06e-21 |
|
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: 93.11 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlapAAWWRQLSWLP 395
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03269 77 EERGLYPKmKVIDQLVYLAQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLN 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
311-506 |
1.21e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 311 ARGGVIRLERLSVrgrdgrapydltaDIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwrQ 390
Cdd:PRK13539 11 VRGGRVLFSGLSF-------------TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSWLPQR----PVLvpgTVRHNLVLLGPVDDLERACAAAGFDAVldelprGLDTVLGRGGVGLSLGQRQRLGLARALGSP 466
Cdd:PRK13539 75 CHYLGHRnamkPAL---TVAENLEFWAAFLGGEELDIAAALEAV------GLAPLAHLPFGYLSAGQKRRVALARLLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15608759 467 AAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-524 |
1.82e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLl 412
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIF- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 gP-------------VDDLERacaaagFdavldELPrglDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK10247 104 -PwqirnqqpdpaifLDDLER------F-----ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 480 DARTEQHVLGAIVERAR-AGATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:PRK10247 169 DESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
316-518 |
2.61e-21 |
|
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: 93.13 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWL 394
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLD 473
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15608759 474 EPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVA-AAGDRVV 518
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIA 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
317-519 |
3.62e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAP---SSGRITVAGVDVTNLAPAAwwRQLSW 393
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPG-TVRHNLvLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:COG4136 81 LFQDDLLFPHlSVGENL-AFALPPTIGRAQRRARVEQALEEA--GLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 473 DEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAAAGDRVVE 519
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLD 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
316-506 |
3.90e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.60 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGrapyDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTaPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:COG4138 1 LQLNDVAVAGRLG----PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPvddleRACAAAGFDAVLDELPR--GLDTVLGRGGVGLSLGQRQRLGLARAL-------GS 465
Cdd:COG4138 76 QQQSPPFAmPVFQYLALHQP-----AGASSEAVEQLLAQLAEalGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 466 PAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSH 191
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
47-507 |
4.09e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.71 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 47 LVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAvtARRPSQLAAQRDAAAVLITR---GLDGLRPYFTGYLPTLLLA 123
Cdd:PRK10790 72 VGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA--ALRQPLSAFDTQPVGQLISRvtnDTEVIRDLYVTVVATVLRS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 124 AILTPATVAVIGLYDLKsMAIVVITL-PLIPIFMVLIGLATTnpsaaalAAMTAVQARLLDL-------IAGIPTLRALG 195
Cdd:PRK10790 150 AALIGAMLVAMFSLDWR-MALVAIMIfPAVLVVMVIYQRYST-------PIVRRVRAYLADIndgfnevINGMSVIQQFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 196 RASGPEQRIAELSADHRRSAMATLRiafLSALVLELLATLGVALVAVGigLRLVFG-EMSLTAGLTVLLlAPEVYW---- 270
Cdd:PRK10790 222 QQARFGERMGEASRSHYMARMQTLR---LDGFLLRPLLSLFSALILCG--LLMLFGfSASGTIEVGVLY-AFISYLgrln 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 271 -PLRRVGVQFHAAADGRTAADKAFALLgESPSPTPGRRTVTARGGVIRLERLSVRGRDGR-APYDLTADIEPGRVTVLTG 348
Cdd:PRK10790 296 ePLIELTTQQSMLQQAVVAGERVFELM-DGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 349 RNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLLGPVDD--LERACAAAG 426
Cdd:PRK10790 375 HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEeqVWQALETVQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 427 FDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVErARAGATVLVVAH 506
Cdd:PRK10790 455 LAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA-VREHTTLVVIAH 533
|
.
gi 15608759 507 R 507
Cdd:PRK10790 534 R 534
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-518 |
4.23e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLVL--- 411
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENIFLgre 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 ---LGPVDD--LERACAaagfdAVLDELprGLD----TVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:COG1129 106 prrGGLIDWraMRRRAR-----ELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 15608759 483 tEQHVLGAIVERARA-GATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG1129 175 -EVERLFRIIRRLKAqGVAIIYISHRlDEVFEIADRVT 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-506 |
5.85e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvDVTnlapaawwrqLSWLPQRPVLVPG-TVRHNlVL 411
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQEPPLDDDlTVLDT-VL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 --LGPVDDLERACAAA-------------------------GFDA------VLDELprGLDTVLGRGGVG-LSLGQRQRL 457
Cdd:COG0488 84 dgDAELRALEAELEELeaklaepdedlerlaelqeefealgGWEAearaeeILSGL--GFPEEDLDRPVSeLSGGWRRRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 458 GLARALGSPAAVLLLDEPTAHLDART----EQHVlgaiveRARAGaTVLVVAH 506
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESiewlEEFL------KNYPG-TVLVVSH 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
239-507 |
6.06e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 96.32 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 239 LVAVGIGLRLVF-GEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADKAFALLGESPSPTPGRRTVTARGGV-- 315
Cdd:PRK10789 236 LLAIGGGSWMVVnGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGEld 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPGTVRHNLVLLGPVDDLERACAAAGFDAVLDE---LPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDilrLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
250 260 270
....*....|....*....|....*....|....*
gi 15608759 473 DEPTAHLDARTEQHVLGAIvERARAGATVLVVAHR 507
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNL-RQWGEGRTVIISAHR 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
316-524 |
6.92e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.52 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVdvtnlapaawwRQLSWL 394
Cdd:cd03223 1 IELENLSLATPDGRVLLkDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLVPGTVRHNLVLlgPVDDLeracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15608759 475 PTAHLDARTEQHVLGAIVERaraGATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-518 |
1.05e-20 |
|
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: 96.52 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwrQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLE-----RACAaagFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV 487
Cdd:TIGR01271 511 LSYDEYRytsviKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|.
gi 15608759 488 LGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSKLEHLKKADKIL 618
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-518 |
1.63e-20 |
|
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: 91.84 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwrQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLE-----RACAaagFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV 487
Cdd:cd03291 122 VSYDEYRyksvvKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|.
gi 15608759 488 LGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:cd03291 199 FESCVCKLMANKTRILVTSKMEHLKKADKIL 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
315-510 |
1.78e-20 |
|
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: 90.33 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSV----RGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAW--- 387
Cdd:cd03258 1 MIELKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 -------WRQLSWLPQRpvlvpgTVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLA 460
Cdd:cd03258 81 rrrigmiFQHFNLLSSR------TVFENVALPLEIAGVPKAEIEERVLELLELV--GLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15608759 461 RALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQV 510
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDiNRELGLTIVLITHEMEV 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
315-522 |
1.84e-20 |
|
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: 90.19 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAP----YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNL---APAAW 387
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQ-LSWLPQRPVLVPG-TVRHNlVLLgPvddLERACAAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALG 464
Cdd:COG4181 88 RARhVGFVFQSFQLLPTlTALEN-VML-P---LELAGRRDARARARALLERvGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVVEVNS 522
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVTHDPALAARCDRVLRLRA 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-518 |
1.95e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGR-VTVLtGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVL--VPG-TVRHN 408
Cdd:COG1101 24 GLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtAPSmTIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVL---------LGP-VDDLERacaaAGFDAVLDELPRGLDTVLGRgGVG-LSLGQRQRLGLARALGSPAAVLLLDEPTA 477
Cdd:COG1101 103 LALayrrgkrrgLRRgLTKKRR----ELFRELLATLGLGLENRLDT-KVGlLSGGQRQALSLLMATLTKPKLLLLDEHTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15608759 478 HLDARTEQHVLGA---IVERARagATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG1101 178 ALDPKTAALVLELtekIVEENN--LTTLMVTHNmEQALDYGNRLI 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
316-522 |
3.42e-20 |
|
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: 89.71 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLP 395
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELPR--GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 473 DEPTAHLDARTEQHvLGAIVERA--RAGATVLVVAHRQQVA-AAGDRVVEVNS 522
Cdd:cd03296 161 DEPFGALDAKVRKE-LRRWLRRLhdELHVTTVFVTHDQEEAlEVADRVVVMNK 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
321-488 |
3.44e-20 |
|
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: 92.09 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 321 LSVRGRDGRAPYDLTAD--IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDV------TNLAPAAwwRQLS 392
Cdd:COG4148 3 LEVDFRLRRGGFTLDVDftLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHR--RRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPG-TVRHNLvLLGpVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:COG4148 81 YVFQEARLFPHlSVRGNL-LYG-RKRAPRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170
....*....|....*..
gi 15608759 472 LDEPTAHLDARTEQHVL 488
Cdd:COG4148 157 MDEPLAALDLARKAEIL 173
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
323-524 |
7.91e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.99 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 323 VRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaaWWRQLSWLPQRPVLVP 402
Cdd:TIGR01277 6 VRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP--YQRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 403 G-TVRHNLVL-LGP--------VDDLERACAAAGFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARALGSPAAVLLL 472
Cdd:TIGR01277 84 HlTVRQNIGLgLHPglklnaeqQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 473 DEPTAHLDARTEQHVLGAIVERA-RAGATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
332-506 |
9.13e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 87.74 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 332 YDLTADIE-PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGV------DVTNLAPAAwwRQLSWLPQRPVLVPG- 403
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrKKINLPPQQ--RKIGLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 404 TVRHNLV--LLGPVDDLERACaaagFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDA 481
Cdd:cd03297 91 NVRENLAfgLKRKRNREDRIS----VDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*.
gi 15608759 482 RTEQHVLGAIVER-ARAGATVLVVAH 506
Cdd:cd03297 165 ALRLQLLPELKQIkKNLNIPVIFVTH 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
333-507 |
1.44e-19 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 92.70 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLE--RACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEqHVLGA 490
Cdd:TIGR00957 1384 SQYSDEEvwWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-NLIQS 1462
|
170
....*....|....*..
gi 15608759 491 IVERARAGATVLVVAHR 507
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAHR 1479
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
316-517 |
2.17e-19 |
|
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: 87.04 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSWLP 395
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QRPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:cd03265 80 QDLSVDDElTGWENLYIHARLYGVPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15608759 475 PTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRV 517
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQlCDRV 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-520 |
2.73e-19 |
|
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: 86.31 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNL---APAAWWRQLSWLPQRPVLVPG-TVRHN 408
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDFRLLPDrNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:cd03292 99 VAFALEVTGVPPREIRKRVPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 489 GAIVERARAGATVLVVAH-RQQVAAAGDRVVEV 520
Cdd:cd03292 177 NLLKKINKAGTTVVVATHaKELVDTTRHRVIAL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
315-518 |
3.67e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 86.57 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRgRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaawwRQLSW 393
Cdd:COG1127 5 MIEVRNLTKS-FGDRVVLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSE----KELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQR-PVLVPG-------TVRHNLVL-------LGP--VDDLERAC-AAAGFDAVLDELPRGLdtvlgrggvglSLGQRQ 455
Cdd:COG1127 80 LRRRiGMLFQGgalfdslTVFENVAFplrehtdLSEaeIRELVLEKlELVGLPGAADKMPSEL-----------SGGMRK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 456 RLGLARALGSPAAVLLLDEPTAHLDARTeqhvLGAIVE-----RARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPIT----SAVIDElirelRDELGLTSVVVTHDlDSAFAIADRVA 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-480 |
4.27e-19 |
|
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: 86.44 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLV 410
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKlTVEENIL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:cd03218 98 AVLEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
316-506 |
5.28e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.84 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlAPAAwwrql 391
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpalqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 swlpQRPV------LVPG-TVRHNLVL---LGPVDDLERACAAAGFDAVLdelprGLDTVLGRGGVGLSLGQRQRLGLAR 461
Cdd:COG4525 77 ----DRGVvfqkdaLLPWlNVLDNVAFglrLRGVPKAERRARAEELLALV-----GLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDvWQRTGKGVFLITH 193
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
333-518 |
6.75e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 85.82 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlAPAAWWRQLswlpQRPV--------LVPG- 403
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKL----RRKVgmvfqqfnLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 404 TVRHNlVLLGPVD----DLERACAAAgfdavlDELprgLDTVlgrgGVG---------LSLGQRQRLGLARALG-SPAaV 469
Cdd:COG1126 93 TVLEN-VTLAPIKvkkmSKAEAEERA------MEL---LERV----GLAdkadaypaqLSGGQQQRVAIARALAmEPK-V 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 470 LLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR----QQVAaagDRVV 518
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREVA---DRVV 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
315-506 |
7.91e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.31 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAA---WWRQ 390
Cdd:PRK10908 1 MIRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSWLPQ-RPVLVPGTVRHN----LVLLGPV-DDLERACAAAgfdavLDELprGLDTVLGRGGVGLSLGQRQRLGLARALG 464
Cdd:PRK10908 81 IGMIFQdHHLLMDRTVYDNvaipLIIAGASgDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
315-521 |
8.09e-19 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 85.10 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYD----LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWW-- 388
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRvlkgVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 389 --RQLSWLPQRPVLVPG-TVRHNL---VLLGPVDDLERACAAAgfdAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARA 462
Cdd:TIGR02211 81 rnKKLGFIYQFHHLLPDfTALENVampLLIGKKSVKEAKERAY---EMLEKV--GLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 463 LGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAAAGDRVVEVN 521
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLELAKKLDRVLEMK 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-523 |
1.02e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.22 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAgvdvtnlapaawwRQLSWLPQRPVLVPGTVRHNLVLL 412
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVD--DLERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV--- 487
Cdd:PTZ00243 745 DEEDaaRLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVvee 824
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15608759 488 --LGAIVERARAGAT--VLVVAHRQQVAAAGDRVVEVNSD 523
Cdd:PTZ00243 825 cfLGALAGKTRVLAThqVHVVPRADYVVALGDGRVEFSGS 864
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
316-481 |
1.62e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDV-TNLAPAAwwRQLSWL 394
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE--RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVLVPG-TVRHNlVLLGPVDdleRACAAAGFDAVLDELprgLDTVlGRGGVG------LSLGQRQRLGLARALGSPA 467
Cdd:COG1118 81 FQHYALFPHmTVAEN-IAFGLRV---RPPSKAEIRARVEEL---LELV-QLEGLAdrypsqLSGGQRQRVALARALAVEP 152
|
170
....*....|....
gi 15608759 468 AVLLLDEPTAHLDA 481
Cdd:COG1118 153 EVLLLDEPFGALDA 166
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
333-506 |
1.75e-18 |
|
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: 84.24 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL---TAPSSGRITVAGVDVTnlaPAAWWRQLSWLPQRPVLVPG-TVRHN 408
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGlTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 L----VLLGPVddleraCAAAGFDAVLDELPRGLDTVLGRGG----VGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:cd03234 102 LtytaILRLPR------KSSDAIRKKRVEDVLLRDLALTRIGgnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*.
gi 15608759 481 ARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
307-518 |
3.82e-18 |
|
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: 83.54 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 307 RTVTARGGVIRLERLSVRG--RDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnLAP 384
Cdd:cd03267 11 RVYSKEPGLIGSLKSLFKRkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 385 aawWRQLSWLPQRPVLVPGT---------VRHNLVLLGPVDDLERACAAAGFDAVLD--ELPRGLDTVLGRggvgLSLGQ 453
Cdd:cd03267 86 ---WKRRKKFLRRIGVVFGQktqlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSEllDLEELLDTPVRQ----LSLGQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 454 RQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHR-QQVAAAGDRVV 518
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARRVL 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
330-511 |
4.03e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 330 APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG--VDVTNLAPAAWWRQLswlpQRPV-------- 399
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDKAIREL----RRNVgmvfqqyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 400 LVPG-TVRHNLV-----LLGpvddLERACAAAGFDAVLDELPrgLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLD 473
Cdd:PRK11124 93 LWPHlTVQQNLIeapcrVLG----LSKDQALARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 15608759 474 EPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVA 511
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVA 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-507 |
7.42e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.00 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaawwRQLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR----RRIGYLPEERGLYPKmKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARAL-GSPaAVLLLDEPTAHLDARTEQHVLGA 490
Cdd:COG4152 95 LARLKGLSKAEAKRRADEWLERL--GLGDRANKKVEELSKGNQQKVQLIAALlHDP-ELLILDEPFSGLDPVNVELLKDV 171
|
170
....*....|....*..
gi 15608759 491 IVERARAGATVLVVAHR 507
Cdd:COG4152 172 IRELAAKGTTVIFSSHQ 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
219-518 |
8.69e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.14 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 219 LRIAFLSALVLELLATLGVA---LVAVGIGLRLVfgEMSLTAGLTvllLAPEVYWPLRRVG-----------VQFH---- 280
Cdd:PTZ00243 1186 VRVEFLSNIVVTVIALIGVIgtmLRATSQEIGLV--SLSLTMAMQ---TTATLNWLVRQVAtveadmnsverLLYYtdev 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 281 ------------AAADGRT--AADKAFALLGESPSPT-PGRRTVTArgGVIRLERLSVRGRDGrAPYDL---TADIEPGR 342
Cdd:PTZ00243 1261 phedmpeldeevDALERRTgmAADVTGTVVIEPASPTsAAPHPVQA--GSLVFEGVQMRYREG-LPLVLrgvSFRIAPRE 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 343 VTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlvllgpVDDLERAC 422
Cdd:PTZ00243 1338 KVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN------VDPFLEAS 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 423 AAAGFDAVldEL----------PRGLDTVLGRGGVGLSLGQRQRLGLARAL---GSpaAVLLLDEPTAHLDARTEQHVlG 489
Cdd:PTZ00243 1412 SAEVWAAL--ELvglrervaseSEGIDSRVLEGGSNYSVGQRQLMCMARALlkkGS--GFILMDEATANIDPALDRQI-Q 1486
|
330 340
....*....|....*....|....*....
gi 15608759 490 AIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PTZ00243 1487 ATVMSAFSAYTVITIAHRLHTVAQYDKII 1515
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
333-518 |
1.58e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPG-TVRhNLVL 411
Cdd:COG4604 19 DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRlTVR-ELVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LG--P-------VDD---LERACAAagFDavLDELP-RGLDTvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:COG4604 98 FGrfPyskgrltAEDreiIDEAIAY--LD--LEDLAdRYLDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 479 LDARteqHVLgAIVERAR-----AGATVLVVAHRQQVAAA-GDRVV 518
Cdd:COG4604 166 LDMK---HSV-QMMKLLRrladeLGKTVVIVLHDINFASCyADHIV 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
346-522 |
1.72e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 346 LTGRNGAGKSTTLqaiagltAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHNlVLLGPVD----DLERA 421
Cdd:PTZ00265 1260 LTKEGGSGEDSTV-------FKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN-IKFGKEDatreDVKRA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 422 CAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGAT 500
Cdd:PTZ00265 1332 CKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDiKDKADKT 1411
|
170 180
....*....|....*....|..
gi 15608759 501 VLVVAHRQQVAAAGDRVVEVNS 522
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVVFNN 1433
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
316-506 |
2.05e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPY----DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ- 390
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaldDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 -----------LswLPQRpvlvpgTVRHN----LVLLGpVDDLERacaaagfDAVLDELprgLDTV--LGRGGV---GLS 450
Cdd:COG1135 82 rkigmifqhfnL--LSSR------TVAENvalpLEIAG-VPKAEI-------RKRVAEL---LELVglSDKADAypsQLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 451 LGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDiNRELGLTIVLITH 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
333-511 |
2.13e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaaWWRQLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPHmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTE---QHVL 488
Cdd:PRK11607 115 GLKQDKLPKAEIASRVNEMLGLV--HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmQLEV 192
|
170 180
....*....|....*....|...
gi 15608759 489 GAIVEraRAGATVLVVAHRQQVA 511
Cdd:PRK11607 193 VDILE--RVGVTCVMVTHDQEEA 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
318-506 |
2.19e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.48 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 318 LERLSVRgRDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAaWWRQLSWLPQ 396
Cdd:TIGR01189 3 ARNLACS-RGERMLFEgLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 RPVLVPG-TVRHNLVLLGPVDDLERACAAAGFDAVldelprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEP 475
Cdd:TIGR01189 81 LPGLKPElSALENLHFWAAIHGGAQRTIEDALAAV------GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 15608759 476 TAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
333-518 |
2.41e-17 |
|
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: 80.29 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS--SGRITVAGvdvTNLAPAAWWRQLSWLPQRPVLVPG-TVRHNL 409
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTlTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VllgpvddleracaaagFDAVLDelprgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03213 104 M----------------FAAKLR---------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|.
gi 15608759 490 AIVERARAGATVLVVAH--RQQVAAAGDRVV 518
Cdd:cd03213 153 LLRRLADTGRTIICSIHqpSSEIFELFDKLL 183
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
320-518 |
2.70e-17 |
|
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: 83.24 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 320 RLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTN------LAPAAwwRQLSW 393
Cdd:TIGR02142 2 SARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQRPVLVPG-TVRHNLVL-LGPVDDLERAcaaAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:TIGR02142 80 VFQEARLFPHlSVRGNLRYgMKRARPSERR---ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15608759 472 LDEPTAHLDARTEQHVLgAIVERARA--GATVLVVAHR-QQVAAAGDRVV 518
Cdd:TIGR02142 155 MDEPLAALDDPRKYEIL-PYLERLHAefGIPILYVSHSlQEVLRLADRVV 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
316-512 |
3.19e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 Q----------RPVLVPGTVRHnLVLLGPVDD-----LERACAAAGFDAVLDelpRGLDTvlgrggvgLSLGQRQRLGLA 460
Cdd:PRK09536 84 QdtslsfefdvRQVVEMGRTPH-RSRFDTWTEtdraaVERAMERTGVAQFAD---RPVTS--------LSGGERQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 461 RALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAA 512
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAA 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
337-521 |
4.67e-17 |
|
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: 80.17 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITV----AGVDVTNLAPaawwRQ---------------LSWLPQR 397
Cdd:COG4778 33 SVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP----REilalrrrtigyvsqfLRVIPRV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 PVLvpGTVRHNLVLLGpvDDLERACAAAGfdAVLD--ELPRGL-----DTVLGrggvglslGQRQRLGLARALGSPAAVL 470
Cdd:COG4778 109 SAL--DVVAEPLLERG--VDREEARARAR--ELLArlNLPERLwdlppATFSG--------GEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH----RQQVAaagDRVVEVN 521
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHdeevREAVA---DRVVDVT 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
316-518 |
6.20e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 80.24 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWW---RQLS 392
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPG-TVRHNLVLL---------GPVDDLERAC-AAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLAR 461
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPlrehtrlseEEIREIVLEKlEAVGLRGAEDLYPA-----------ELSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTeqhvLGAIVE-----RARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIA----SGVIDDlirslKKELGLTSIMVTHDlDTAFAIADRIA 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
316-506 |
6.29e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGrapyDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTaPSSGRITVAGVDVTNLAPAAWWRQLSWLP 395
Cdd:PRK03695 1 MQLNDVAVSTRLG----PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QR---PVLVPgtVRHNLVLLGPVddlerACAAAGFDAVLDELPR--GLDTVLGRGGVGLSLGQRQRLGLA-------RAL 463
Cdd:PRK03695 76 QQqtpPFAMP--VFQYLTLHQPD-----KTRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 464 GSPAAVLLLDEPTAHLDArTEQHVLGAIVER-ARAGATVLVVAH 506
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDV-AQQAALDRLLSElCQQGIAVVMSSH 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
333-524 |
7.76e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.68 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ----LSWLPQRPVLVPGTVRHN 408
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVLLGPVDD--LERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:cd03290 99 ITFGSPFNKqrYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15608759 487 VLGA-IVERARAGA-TVLVVAHRQQVAAAGDRVVEVNsDG 524
Cdd:cd03290 179 LMQEgILKFLQDDKrTLVLVTHKLQYLPHADWIIAMK-DG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
315-507 |
9.70e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 79.74 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRgRDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSG-RITV-----AGVDVTNLapaaw 387
Cdd:COG1119 3 LLELRNVTVR-RGGKTILDdISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 wRQL-----SWLpQRPVLVPGTVRhNLVLLG---------PVDDLERACAaagfDAVLDELprGLDTVLGRGGVGLSLGQ 453
Cdd:COG1119 77 -RKRiglvsPAL-QLRFPRDETVL-DVVLSGffdsiglyrEPTDEQRERA----RELLELL--GLAHLADRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 454 RQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLV-VAHR 507
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHH 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
315-526 |
1.53e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVrGRDGRAPY-DLTADIEPG-RVtVLTGRNGAGKSTTLQAIAGLTAPSSGRITVaGVDVtnlapaawwrQLS 392
Cdd:COG0488 315 VLELEGLSK-SYGDKTLLdDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQrpvlvpgtvrHNLVLlgpvdDLERacaaagfdAVLDELPRGLD--------TVLGRGG---------VG-LSLGQR 454
Cdd:COG0488 382 YFDQ----------HQEEL-----DPDK--------TVLDELRDGAPggteqevrGYLGRFLfsgddafkpVGvLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 455 QRLGLARALGSPAAVLLLDEPTAHLDARTeqhvLGAIVE--RARAGaTVLVVAH-RQQVAAAGDRVVEVNSDGFR 526
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEalDDFPG-TVLLVSHdRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
337-506 |
1.92e-16 |
|
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: 78.99 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVtnlapaawwrqlSWLPQR-PVLVPGTVRHnlvLLGPV 415
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYiKADYEGTVRD---LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 416 DDleRACAAAGFDA-VLDelPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDarTEQHVLGAIVER 494
Cdd:cd03237 86 TK--DFYTHPYFKTeIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASKVIR 159
|
170
....*....|....*
gi 15608759 495 ---ARAGATVLVVAH 506
Cdd:cd03237 160 rfaENNEKTAFVVEH 174
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
315-480 |
2.00e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.93 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQA-------IAGLTApsSGRITVAG-------VDVT 380
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEILLDGediydpdVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 381 NLApaawwRQLSWLPQRPVLVPGTVRHNlVLLGP----------VDDL-ERACAAAG-FDAVLDELprgldtvlGRGGVG 448
Cdd:COG1117 89 ELR-----RRVGMVFQKPNPFPKSIYDN-VAYGLrlhgikskseLDEIvEESLRKAAlWDEVKDRL--------KKSALG 154
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 449 LSLGQRQRLGLARALG-SPaAVLLLDEPTAHLD 480
Cdd:COG1117 155 LSGGQQQRLCIARALAvEP-EVLLMDEPTSALD 186
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
331-512 |
2.17e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 331 PYDLTADIEPG-RVTVLtGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHN 408
Cdd:PRK10771 15 PMRFDLTVERGeRVAIL-GPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVL-LGP--------VDDLERACAAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK10771 92 IGLgLNPglklnaaqREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 480 DARTEQHVLGAIVERARA-GATVLVVAHRQQVAA 512
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAA 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
315-506 |
2.36e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPY----------------------DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRI 372
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 373 TVAGvdvtnlapaawwrQLSWLpqrpvLVPG-------TVRHNLVLLGPVDDLERACAAAGFDAVLD--ELPRGLDTVLG 443
Cdd:COG1134 84 EVNG-------------RVSAL-----LELGagfhpelTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELGDFIDQPVK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 444 RggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:COG1134 146 T----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSH 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-524 |
2.67e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.08 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNL---APAAWWRQ-LSWLPQRPVLVPG-TVRH 407
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV 487
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 15608759 488 LgAIVERARA-GATVLVVAHRQQVAAAGDRVVEVNsDG 524
Cdd:PRK10535 184 M-AILHQLRDrGHTVIIVTHDPQVAAQAERVIEIR-DG 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
346-518 |
2.73e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 79.85 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 346 LTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHNLVLLGPVDDLERACAA 424
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHmTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 425 AGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTE---QHVLGAIVEraRAGATV 501
Cdd:TIGR01187 79 PRVLEALRLV--QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRdqmQLELKTIQE--QLGITF 154
|
170
....*....|....*...
gi 15608759 502 LVVAHRQQVA-AAGDRVV 518
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIA 172
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
315-522 |
2.89e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDG-RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWR-QLS 392
Cdd:PRK13647 4 IIEVEDLHFRYKDGtKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRsKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRP--VLVPGTVRHNlVLLGPV------DDLER----ACAAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLA 460
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDD-VAFGPVnmgldkDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 461 RALGSPAAVLLLDEPTAHLDARTeQHVLGAIVER-ARAGATVLVVAHRQQVAAA-GDRVVEVNS 522
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRG-QETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKE 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
315-521 |
5.34e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.13 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAP--YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvTNLAPAAWW---R 389
Cdd:PRK13635 5 IIRVEHISFRYPDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWdvrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 390 QLSWLPQRP--VLVPGTVRHNlVLLG------PVDDL-ERAcaaagfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLA 460
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDD-VAFGlenigvPREEMvERV------DQALRQV--GMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 461 RALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVVEVN 521
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQlKEQKGITVLSITHDLDEAAQADRVIVMN 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-524 |
6.49e-16 |
|
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: 74.79 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVdvtnlapaawwRQLSWLPQrpvlvpgtvrhnlvll 412
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYFEQ---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 gpvddleracaaagfdavldelprgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIV 492
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 493 ERARagaTVLVVAH-RQQVAAAGDRVVEVNSDG 524
Cdd:cd03221 115 EYPG---TVILVSHdRYFLDQVATKIIELEDGK 144
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
337-480 |
7.92e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.99 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaawWRQ----LSWLPQRPVLVPG-TVRHNL-- 409
Cdd:COG1137 25 EVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM---HKRarlgIGYLPQEASIFRKlTVEDNIla 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 410 VL-LGPVDDLERacaAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:COG1137 102 VLeLRKLSKKER---EERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
329-507 |
1.24e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 329 RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT-NLAPAAWWRQLSWLPQRPVLVPG-TVR 406
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEmTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNLVL------LGPVDdleRACAAAGFDAVLDELprGLD----TVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPT 476
Cdd:PRK11288 98 ENLYLgqlphkGGIVN---RRLLNYEAREQLEHL--GVDidpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 477 AHLDARtEQHVLGAIVERARA-GATVLVVAHR 507
Cdd:PRK11288 169 SSLSAR-EIEQLFRVIRELRAeGRVILYVSHR 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-506 |
1.45e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDvtnlaPaawWR-----------------QLSW-L 394
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----P---FKrrkefarrigvvfgqrsQLWWdL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PqrpvlvpgtVRHNLVLLGPVDDLERacaaAGFDAVLDElprgLDTVLGRGGV------GLSLGQRQRLGLARAL-GSPa 467
Cdd:COG4586 112 P---------AIDSFRLLKAIYRIPD----AEYKKRLDE----LVELLDLGELldtpvrQLSLGQRMRCELAAALlHRP- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15608759 468 AVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSH 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
333-506 |
1.55e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.65 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwrQLSWLPQ-----RPVLvpgTVRH 407
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLLGlgggfNPEL---TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLVLLGPVDDLERACAAAGFDAVLD--ELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQ 485
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEfsELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180
....*....|....*....|.
gi 15608759 486 HVLGAIVERARAGATVLVVAH 506
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSH 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
326-506 |
2.03e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 326 RDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAaWWRQLSWLPQRPVLVpgt 404
Cdd:cd03231 10 RDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 405 vrhnlVLLGPVDDLERACAAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDART 483
Cdd:cd03231 86 -----TTLSVLENLRFWHADHSDEQVEEALARvGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 15608759 484 EQHVLGAIVERARAGATVLVVAH 506
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTH 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
333-511 |
2.47e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVtnLAPAAWWR-----------QLSWLPQRPVLv 401
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERlirqeagmvfqQFYLFPHLTAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 pgtvrHNlVLLGP--VDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK09493 96 -----EN-VMFGPlrVRGASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 480 DARTEQHVLGAIVERARAGATVLVVAHRQQVA 511
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-506 |
2.67e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRqLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLDLEfTVRENLLV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LGPVDDLERACAAAGFDAVLD--ELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDArteqHVLG 489
Cdd:PRK13536 138 FGRYFGMSTREIEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDP----HARH 209
|
170 180
....*....|....*....|.
gi 15608759 490 AIVERARA----GATVLVVAH 506
Cdd:PRK13536 210 LIWERLRSllarGKTILLTTH 230
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
16-291 |
3.32e-15 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 76.04 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 16 IVLASIVAGVIDPANPGMAGLRRWLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVTARRPSQLAAQR 95
Cdd:cd18781 13 IAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSYQEKVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 96 DAAAV-LITRGLDGLRPYFTGYLPTLLLAaILTPATV-AVIGLYDLKSMAIVVITLPLIPIFMVLIG------LAT---- 163
Cdd:cd18781 93 TAEVVqLSVEGVEQLEIYFGRYLPQFFYS-MLAPLTLfVVLAPINWKAALVLLICVPLIPISIIAVQkiakklLSKywgs 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 164 -TNpsaaalaamtaVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALvav 242
Cdd:cd18781 172 yTD-----------LGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAAL--- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 243 GIGLRLV---FGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAADK 291
Cdd:cd18781 238 GIILALLqfaNGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDK 289
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
333-513 |
3.32e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLtapSSGRITVAGVDVtnlapaaWWRQLSwlPQRPVLvpgtvrHNLVLL 412
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---LKGTPVAGCVDV-------PDNQFG--REASLI------DAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLERACAAAGF-DAVL-----DELprgldtvlgrggvglSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQh 486
Cdd:COG2401 110 GDFKDAVELLNAVGLsDAVLwlrrfKEL---------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK- 173
|
170 180
....*....|....*....|....*....
gi 15608759 487 VLGAIVERA--RAGATVLVVAHRQQVAAA 513
Cdd:COG2401 174 RVARNLQKLarRAGITLVVATHHYDVIDD 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
316-506 |
3.82e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlAPAA----WWRQL 391
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAergvVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLvpGTVRHNLVLLGpVDDLERACAAAGFDAVLdelprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:PRK11248 80 GLLPWRNVQ--DNVAFGLQLAG-VEKMQRLEIAHQMLKKV-----GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 15608759 472 LDEPTAHLDARTEQHVLGAIVER-ARAGATVLVVAH 506
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITH 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-508 |
5.03e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 346 LTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlAPAAWWRQLSWLPQRPVLVPG-TVRHNLVLlgpvdDLERACAA 424
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYlTLRENCLY-----DIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 425 AGFDAV--LDELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVL 502
Cdd:PRK13540 106 VGITELcrLFSLEHLIDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVL 181
|
....*.
gi 15608759 503 VVAHRQ 508
Cdd:PRK13540 182 LTSHQD 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
333-506 |
5.05e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRqLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLDPDfTVRENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LGPVDDLERACAAAGFDAVLD--ELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTeQHVlg 489
Cdd:PRK13537 104 FGRYFGLSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA-RHL-- 176
|
170 180
....*....|....*....|.
gi 15608759 490 aIVERAR----AGATVLVVAH 506
Cdd:PRK13537 177 -MWERLRsllaRGKTILLTTH 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
333-520 |
1.64e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.93 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWW----RQLSWLPQRPVLVPG-TVRH 407
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDfTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NL---VLLG---PVDDLERA---CAAAGFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:PRK11629 107 NVampLLIGkkkPAEINSRAlemLAAVGLEHRANHRPS-----------ELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 479 LDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:PRK11629 176 LDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
329-524 |
2.50e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 329 RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPA--------AWWRQLSwlpqrpVL 400
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaqlgigIIYQELS------VI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 401 VPGTVRHNL---------VLLGPVDDLE--RACAAAGFDAVldELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAV 469
Cdd:PRK09700 93 DELTVLENLyigrhltkkVCGVNIIDWRemRVRAAMMLLRV--GLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 470 LLLDEPTAHL-DARTEQhvLGAIVERARA-GATVLVVAHR-QQVAAAGDRVVeVNSDG 524
Cdd:PRK09700 167 IIMDEPTSSLtNKEVDY--LFLIMNQLRKeGTAIVYISHKlAEIRRICDRYT-VMKDG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
333-521 |
3.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT--NLAPAAWWRQLSWLPQRP--VLVPGTVRHN 408
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVL----LGPVDD-----LERACAAAGFDavldelprgLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK13637 105 IAFgpinLGLSEEeienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 480 DARTEQHVLGAIVE-RARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:PRK13637 176 DPKGRDEILNKIKElHKEYNMTIILVSHSmEDVAKLADRIIVMN 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
333-505 |
3.60e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 70.91 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG--VDVTNLAPAAWWRQLSWLPQRP--VLVPGTVRHN 408
Cdd:TIGR01166 10 GLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQLFAADVDQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 lVLLGPVD-DLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTeQHV 487
Cdd:TIGR01166 90 -VAFGPLNlGLSEAEVERRVREALTAV--GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG-REQ 165
|
170
....*....|....*...
gi 15608759 488 LGAIVERARAGATVLVVA 505
Cdd:TIGR01166 166 MLAILRRLRAEGMTVVIS 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
315-504 |
3.67e-14 |
|
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: 70.92 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGrapyDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSW 393
Cdd:cd03215 4 VLEVRGLSVKGAVR----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LP---QRPVLVPG-TVRHNLVLlgpvddleracaaagfdavldelprgldtvlgrgGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:cd03215 80 VPedrKREGLVLDlSVAENIAL----------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 470 LLLDEPTAHLDARTEQHVLGAIVERARAGATVLVV 504
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
333-524 |
3.79e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLapAAWWRQLSWLPQRPVLvpgtVRHNLVL- 411
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYAL----FRHMTVFd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 -----LGPVDDLERACAAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDA--RT 483
Cdd:PRK10851 94 niafgLTVLPRRERPNAAAIKAKVTQLLEMvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 484 E-QHVLGAIVERARagATVLVVAHRQQVA-AAGDRVVeVNSDG 524
Cdd:PRK10851 174 ElRRWLRQLHEELK--FTSVFVTHDQEEAmEVADRVV-VMSQG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
315-526 |
4.14e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL-----TAPSSGRITVAGVDV--TNLAPAAW 387
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLyaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQLSWLPQRPVLVPGTVRHNLV-------LLGPVDDL-ERAC-AAAGFDAVLDELPRGldtvlgrgGVGLSLGQRQRLG 458
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAygaringYKGDMDELvERSLrQAALWDEVKDKLKQS--------GLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 459 LARALGSPAAVLLLDEPTAHLDA----RTEQhVLGAIVERaragATVLVVAHR-QQVAAAGDRV----VEVNSDGFR 526
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPistlRIEE-LMHELKEQ----YTIIIVTHNmQQAARVSDMTaffnVELTEGGGR 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
333-521 |
5.10e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVP-----GTVRH 407
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPhmslgENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLVLLG-PVDDL-ERACAA------AGFDavldelPRGLDTVLGrggvglslGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK11432 102 GLKMLGvPKEERkQRVKEAlelvdlAGFE------DRYVDQISG--------GQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 480 DARTEQHVLGAIVE-RARAGATVLVVAHRQQVA-AAGDRVVEVN 521
Cdd:PRK11432 168 DANLRRSMREKIRElQQQFNITSLYVTHDQSEAfAVSDTVIVMN 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
337-518 |
5.32e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWwRQL--SWLPQRPVLVPG-TVRHNLVL-- 411
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDA-IALgiGMVHQHFMLVPNlTVAENIVLgl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 ---LGPVDDLERA-------CAAAGFDavLDelprgLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLda 481
Cdd:COG3845 106 eptKGGRLDRKAArarirelSERYGLD--VD-----PDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVL-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 482 rTEQHV--LGAIVER-ARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:COG3845 173 -TPQEAdeLFEILRRlAAEGKSIIFITHKlREVMAIADRVT 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
315-518 |
5.65e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSW 393
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LP-QRP--VLVPGTVRHNLVL------LGPVDDLERAcaaagfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALG 464
Cdd:PRK13644 81 IVfQNPetQFVGRTVEEDLAFgpenlcLPPIEIRKRV------DRALAEI--GLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
315-506 |
6.01e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDG-RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlAPAAWWRQ-LS 392
Cdd:PRK13636 5 ILKVEELNYNYSDGtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG------KPIDYSRKgLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPGTVRHNLVLLGPVDDLERACAAAGFDAvlDELPRGLDTVLGRGGVG---------LSLGQRQRLGLARAL 463
Cdd:PRK13636 79 KLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPE--DEVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 464 GSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAH 506
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
337-520 |
6.60e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAG-LTAPSSGRITVAGVdvtnlapAAWWRQLSWLpqrpvlVPGTVRHNLVLLGPV 415
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-------VAYVPQVSWI------FNATVRDNILFGSPF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 416 DD--LERACAAAGFDAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE 493
Cdd:PLN03130 706 DPerYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK 785
|
170 180
....*....|....*....|....*..
gi 15608759 494 RARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:PLN03130 786 DELRGKTRVLVTNQLHFLSQVDRIILV 812
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
341-511 |
9.57e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 341 GRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLA------PAAWWRQLSWLPQRPVLV--------PGTVR 406
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlKVADKNQLRLLRTRLTMVfqhfnlwsHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNlVLLGPVDDLERACAAAGFDAVLDELPRGLD-TVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQ 485
Cdd:PRK10619 111 EN-VMEAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
|
170 180
....*....|....*....|....*.
gi 15608759 486 HVLGAIVERARAGATVLVVAHRQQVA 511
Cdd:PRK10619 190 EVLRIMQQLAEEGKTMVVVTHEMGFA 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
334-506 |
1.24e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.21 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 334 LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwrQLSWLPQRPVLVPGTVRHNLVLLG 413
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 414 PVDD-----LERACAAAgfdAVLDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:TIGR00957 724 ALNEkyyqqVLEACALL---PDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180
....*....|....*....|
gi 15608759 489 GAIV--ERARAGATVLVVAH 506
Cdd:TIGR00957 801 EHVIgpEGVLKNKTRILVTH 820
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
297-504 |
1.63e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 297 GESPSPTPGRRTVTARGGVIRLERLSVRGRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVA 375
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALkDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 376 GVDVTNLAPAAWWRQ-LSWLP---QRPVLVPG-TVRHNLVLL---------GPVDDLERACAAAgfDAVLDEL---PRGL 438
Cdd:COG3845 319 GEDITGLSPRERRRLgVAYIPedrLGRGLVPDmSVAENLILGryrrppfsrGGFLDRKAIRAFA--EELIEEFdvrTPGP 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 439 DTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVV 504
Cdd:COG3845 397 DTPARS----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
315-510 |
1.74e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLS----VRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAawwrQ 390
Cdd:PRK11153 1 MIELKNISkvfpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEK----E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSwLPQRPV---------LVPGTVRHNLVLlgPvddLERA-CAAAGFDAVLDELprgLDTVlgrgGVG---------LSL 451
Cdd:PRK11153 77 LR-KARRQIgmifqhfnlLSSRTVFDNVAL--P---LELAgTPKAEIKARVTEL---LELV----GLSdkadrypaqLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 452 GQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQV 510
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRELGLTIVLITHEMDV 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
316-517 |
1.86e-13 |
|
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: 69.09 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTA--PSSGRITVAGVDVTNLAPAAWWRQ--- 390
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSWlpQRPVLVPGtVRhnlvllgpvddleracaaagfdavLDELPRGLDtvlgrggVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:cd03217 81 LAF--QYPPEIPG-VK------------------------NADFLRYVN-------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAA--GDRV 517
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-524 |
2.25e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.52 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHNlVL 411
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYALFPHmTVFEN-VA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LG------PVDDLERacaaagfdAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR-- 482
Cdd:PRK09452 109 FGlrmqktPAAEITP--------RVMEALRMvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKlr 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 483 -TEQHVLGAIvERaRAGATVLVVAHRQQVA-AAGDRVVeVNSDG 524
Cdd:PRK09452 181 kQMQNELKAL-QR-KLGITFVFVTHDQEEAlTMSDRIV-VMRDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
340-479 |
2.37e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPA-AWWRQLSWLPQRPVLVPG-TVRHNLV--LLGPV 415
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIYLVPQEPLLFPNlSVKENILfgLPKRQ 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 416 DDLERacaaagFDAVLDELPRGLDTVLGRGgvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK15439 116 ASMQK------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
333-506 |
3.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT----NLAPAAWWRQLSWLPQRP--VLVPGTVR 406
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPeaQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNlVLLGPV-----DDLERACAAAGFDAVldelprGLDT-VLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK13641 105 KD-VEFGPKnfgfsEDEAKEKALKWLKKV------GLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180
....*....|....*....|....*.
gi 15608759 481 ARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
337-518 |
5.59e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAP----AAWWRQL-----------SWLPQR---- 397
Cdd:PRK11264 25 EVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqKGLIRQLrqhvgfvfqnfNLFPHRtvle 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 -----PVLVPGTVRHNLVLLGpvddlERACAAAGFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARALGSPAAVLLL 472
Cdd:PRK11264 105 niiegPVIVKGEPKEEATARA-----RELLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15608759 473 DEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAA-AGDRVV 518
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAI 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-512 |
5.71e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 322 SVRGRDGRAPYDLTadIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLV 401
Cdd:PRK10575 20 RVPGRTLLHPLSLT--FPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 PGTVRHNLVLLG-----------PVDDLERACAAAGFdavldelpRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVL 470
Cdd:PRK10575 98 EGMTVRELVAIGrypwhgalgrfGAADREKVEEAISL--------VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAA 512
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAA 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
328-518 |
5.97e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.28 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 328 GRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITV------AGVDVTNLAPaawwrqlswLPQRPVLV 401
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP---------LRKKVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 PGTVRHNL--------VLLGPV-------DDLERAcaaagfDAVLDELprGLD-TVLGRGGVGLSLGQRQRLGLARALGS 465
Cdd:PRK13634 91 FQFPEHQLfeetvekdICFGPMnfgvseeDAKQKA------REMIELV--GLPeELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 466 PAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAA-GDRVV 518
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARyADQIV 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
330-506 |
6.04e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 69.21 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 330 APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWwRQL------------SWLPQR 397
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKEL-RELrrkkismvfqsfALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 pvlvpgTVRHNLVL---LGPVDDLERACAAA------GFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARALGSPAA 468
Cdd:cd03294 118 ------TVLENVAFgleVQGVPRAEREERAAealelvGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 469 VLLLDEPTAHLDA--RTE-QHVLGAIVerARAGATVLVVAH 506
Cdd:cd03294 181 ILLMDEAFSALDPliRREmQDELLRLQ--AELQKTIVFITH 219
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1-290 |
8.14e-13 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 69.12 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIDPANPGmAGLRRWLGPLSILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA-GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTARRPSQLAAQRDAAAV-LITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLI 159
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMsRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 160 GLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVAL 239
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15608759 240 VAVGIGLRLVFGEMSLTAGLTVLLLAPEVYWPLRRVGVQFHAAADGRTAAD 290
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
338-516 |
9.25e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNL----APAAWWRQLSWLPQRPVLVPG-----TVRHN 408
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSFMLIPTlnaleNVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVLLGPVDDLERACAAAgfdaVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:PRK10584 113 ALLRGESSRQSRNGAKA----LLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180
....*....|....*....|....*....
gi 15608759 489 GAIVERARAGATVLV-VAHRQQVAAAGDR 516
Cdd:PRK10584 187 DLLFSLNREHGTTLIlVTHDLQLAARCDR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
316-506 |
9.52e-13 |
|
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: 70.60 E-value: 9.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGrapydLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITV----AGVDVTNLAPAAWWRQ- 390
Cdd:TIGR03269 290 ISVDRGVVKAVDN-----VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAk 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 --LSWLPQRPVLVP-GTVRHNL---VLLGPVDDLERACA-----AAGFD-----AVLDELPrglDTvlgrggvgLSLGQR 454
Cdd:TIGR03269 365 ryIGILHQEYDLYPhRTVLDNLteaIGLELPDELARMKAvitlkMVGFDeekaeEILDKYP---DE--------LSEGER 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 455 QRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKaREEMEQTFIIVSH 486
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
333-480 |
9.61e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIE-PGR-VTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG---VDV---TNLAPAAwwRQLSWLPQRPVLVPG- 403
Cdd:PRK11144 14 CLTVNLTlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAekgICLPPEK--RRIGYVFQDARLFPHy 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 404 TVRHNLVL-LGPVDDleracaaAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK11144 92 KVRGNLRYgMAKSMV-------AQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
315-512 |
1.08e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAG-LTAPS-------SGRITVAGVDVTNLAPAA 386
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 387 WWRQLSWLPQ--RPVLvPGTVRhNLVLLGPVDDLERACAAAGFDA--VLDELPR-GLDTVLGRGGVGLSLGQRQRLGLAR 461
Cdd:PRK13547 81 LARLRAVLPQaaQPAF-AFSAR-EIVLLGRYPHARRAGALTHRDGeiAWQALALaGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608759 462 ALG---------SPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAA 512
Cdd:PRK13547 159 VLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAA 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
327-506 |
1.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.23 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 327 DGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQL----SWLPQRP--VL 400
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIrkkvGLVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 401 VPGTVRHNlVLLGPVD---DLERACAAAGFDAVLdelpRGLDTVL-GRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPT 476
Cdd:PRK13649 99 FEETVLKD-VAFGPQNfgvSQEEAEALAREKLAL----VGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190
....*....|....*....|....*....|
gi 15608759 477 AHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
339-506 |
1.69e-12 |
|
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: 69.81 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 339 EPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITvagvdvtnlAPAAW---------------WRQL-------SWLPQ 396
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWdevlkrfrgtelqdyFKKLangeikvAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 397 RPVLVP----GTVRHnlvLLGPVDdlERACAaagfDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:COG1245 168 YVDLIPkvfkGTVRE---LLEKVD--ERGKL----DELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 473 DEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-517 |
1.82e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.25 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 334 LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLT-----APSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVLVPGTVRHN 408
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVLLGP---------VDDLERACAAAGFDAVLDELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK14247 102 NVALGLklnrlvkskKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 15608759 480 DARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRV 517
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
328-517 |
2.04e-12 |
|
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: 70.43 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 328 GRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDV-TNLapAAWWRQLSWLPQRPVLVPG-T 404
Cdd:TIGR01257 942 GRPAVDrLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNL--DAVRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 405 VRHNLVLLGPVDDLERACAAAGFDAVLDElpRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTE 484
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 485 QHVLGAIVeRARAGATVLVVAHRQQVA-AAGDRV 517
Cdd:TIGR01257 1098 RSIWDLLL-KYRSGRTIIMSTHHMDEAdLLGDRI 1130
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
329-504 |
3.70e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 329 RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQ-RPVLVPGTVR 406
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEgRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNLVLLGPVDDleRACAAAGFDAVLDELPRGLDTVLGRGGVgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:PRK11614 99 ENLAMGGFFAE--RDQFQERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170
....*....|....*...
gi 15608759 487 VLGAIVERARAGATVLVV 504
Cdd:PRK11614 176 IFDTIEQLREQGMTIFLV 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
338-506 |
4.51e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAawwRQLSWLPQRPVLVPGtvrhnlvlLGPVDD 417
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAD--------LSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 418 LERACAAAGFDAvlDELPRGLDTVLGRGGVG------LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAI 491
Cdd:PRK13543 103 LHFLCGLHGRRA--KQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 15608759 492 VERARAGATVLVVAH 506
Cdd:PRK13543 181 SAHLRGGGAALVTTH 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
333-518 |
5.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLP-QRP--VLVPGTVRHNl 409
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVfQNPdnQIVATIVEED- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VLLGPvDDLeracaaaGFDAvlDELPRGLDTVLGRGGVG---------LSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK13633 107 VAFGP-ENL-------GIPP--EEIRERVDESLKKVGMYeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 15608759 481 ARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13633 177 PSGRREVVNTIKElNKKYGITIILITHYMEEAVEADRII 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
338-506 |
5.77e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITvagvdvtnlAPAAW---------------WRQL-------SWLP 395
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE---------EEPSWdevlkrfrgtelqnyFKKLyngeikvVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 396 QR----PVLVPGTVRhnlvllgpvDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLL 471
Cdd:PRK13409 167 QYvdliPKVFKGKVR---------ELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 472 LDEPTAHLDARTEQHVLGAIVERARaGATVLVVAH 506
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
333-524 |
8.29e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSgritVAGVDVTNlapaawwrQLSWLPQRPVLVPGTVRHNlVLL 412
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----TSSVVIRG--------SVAYVPQVSWIFNATVREN-ILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVDDLERACAAAGFDAV---LDELPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:PLN03232 702 GSDFESERYWRAIDVTALqhdLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 490 AIVERARAGATVLVVAHRQQVAAAGDRVVEVnSDG 524
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQLHFLPLMDRIILV-SEG 815
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
315-506 |
1.07e-11 |
|
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: 65.84 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVR--GRDG--RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAP---SSGRITVAGVDVTNLAPAAW 387
Cdd:COG0444 1 LLEVRNLKVYfpTRRGvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 ----WRQLSWLPQ------RPVLvpgTVRH----NLVLLGPVDDLE-RACAAAGFDAVldELPRGLDtVLGRGGVGLSLG 452
Cdd:COG0444 81 rkirGREIQMIFQdpmtslNPVM---TVGDqiaePLRIHGGLSKAEaRERAIELLERV--GLPDPER-RLDRYPHELSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15608759 453 QRQRLGLARAL-GSPaAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:COG0444 155 MRQRVMIARALaLEP-KLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITH 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-506 |
1.20e-11 |
|
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: 66.88 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVaGVDVtnlapaawwrQLSWLPQ-RPVLVPG-TV----- 405
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQsRDALDPNkTVweeis 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 406 -RHNLVLLGPVDDLERA-CAAAGFdavldelpRGLDTvlgRGGVG-LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:TIGR03719 409 gGLDIIKLGKREIPSRAyVGRFNF--------KGSDQ---QKKVGqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
170 180
....*....|....*....|....
gi 15608759 483 TEQHVLGAIVERAragATVLVVAH 506
Cdd:TIGR03719 478 TLRALEEALLNFA---GCAVVISH 498
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
339-506 |
1.48e-11 |
|
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: 64.70 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 339 EPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRIT-----------VAGVDVTNLAPAAWWRQLSWL--PQRPVLVPGTV 405
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVKVIvkPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 406 RHNLV-LLGPVDDLERacaaagFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTE 484
Cdd:cd03236 104 KGKVGeLLKKKDERGK------LDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|..
gi 15608759 485 QHVLGAIVERARAGATVLVVAH 506
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
316-506 |
1.66e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGR-APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNlapAAWWRQLSWL 394
Cdd:PRK15056 7 IVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQR-------PVLVpgtvrHNLVLLGPVDDLE--RACAAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALG 464
Cdd:PRK15056 84 PQSeevdwsfPVLV-----EDVVMMGRYGHMGwlRRAKKRDRQIVTAALARvDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
338-506 |
2.18e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVagvDVTnlapaawwrqLSWLPQRpvLVPGTvrhnlvlLGPVDD 417
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK----------ISYKPQY--IKPDY-------DGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 418 LERACAAAgFDA--VLDEL--PRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDArtEQHVLGAIVE 493
Cdd:PRK13409 420 LLRSITDD-LGSsyYKSEIikPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAVAKAI 496
|
170
....*....|....*.
gi 15608759 494 RARA---GATVLVVAH 506
Cdd:PRK13409 497 RRIAeerEATALVVDH 512
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
319-504 |
2.83e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 319 ERLSVRG-RDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRqlswlpQR 397
Cdd:COG1129 255 VVLEVEGlSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIR------AG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 PVLVPG-----------TVRHNLVL--------LGPVDD-LERACAaagfDAVLDEL---PRGLDTVLGRggvgLSLGQR 454
Cdd:COG1129 329 IAYVPEdrkgeglvldlSIRENITLasldrlsrGGLLDRrRERALA----EEYIKRLrikTPSPEQPVGN----LSGGNQ 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15608759 455 QRLGLARALGSPAAVLLLDEPTAHLD--ARTEqhVLGAIVERARAGATVLVV 504
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRELAAEGKAVIVI 450
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
333-508 |
3.36e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHNLVL 411
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHlSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 ---LGPVDDLERACAAAGFDAVLDelprgLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDA--RTEQH 486
Cdd:PRK11000 99 glkLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMR 173
|
170 180
....*....|....*....|..
gi 15608759 487 VLGAIVERaRAGATVLVVAHRQ 508
Cdd:PRK11000 174 IEISRLHK-RLGRTMIYVTHDQ 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
333-506 |
3.97e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS---SGRITVAGVDVTnlapAAWWRQLS-WLPQRPVLVPG-TVRH 407
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID----AKEMRAISaYVQQDDLFIPTlTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLVLLGPV---DDLERACAAAGFDAVLDELprGL----DTVLGRGGV--GLSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180
....*....|....*....|....*...
gi 15608759 479 LDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
348-506 |
4.07e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 348 GRNGAGKSTTLQAIAGLTAPSSGRITVA-GVDVtnlapaawwrqlSWLPQRPVLVPG-TVRHNlVLLG---PVDDLER-- 420
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV------------GYLPQEPQLDPEkTVREN-VEEGvaeVKAALDRfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 421 ------ACAAAGFDAVLDELPR-----------GLDTVL-----------GRGGVG-LSLGQRQRLGLARALGSPAAVLL 471
Cdd:PRK11819 107 eiyaayAEPDADFDALAAEQGElqeiidaadawDLDSQLeiamdalrcppWDAKVTkLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 15608759 472 LDEPTAHLDART----EQHVlgaiveRARAGaTVLVVAH 506
Cdd:PRK11819 187 LDEPTNHLDAESvawlEQFL------HDYPG-TVVAVTH 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
348-506 |
4.11e-11 |
|
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: 65.34 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 348 GRNGAGKSTTLQAIAGLTAPSSGRITVA-GVDVtnlapaawwrqlSWLPQRPVLVPG-TVRHNlVLLG---PVDDLER-- 420
Cdd:TIGR03719 38 GLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV------------GYLPQEPQLDPTkTVREN-VEEGvaeIKDALDRfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 421 ------ACAAAGFDAVLDE---------------LPRGLDTVL-------GRGGVG-LSLGQRQRLGLARALGSPAAVLL 471
Cdd:TIGR03719 105 eisakyAEPDADFDKLAAEqaelqeiidaadawdLDSQLEIAMdalrcppWDADVTkLSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 15608759 472 LDEPTAHLDART----EQHVlgaiverARAGATVLVVAH 506
Cdd:TIGR03719 185 LDEPTNHLDAESvawlERHL-------QEYPGTVVAVTH 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
333-518 |
4.94e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAgvDVTNLAPAAWWRQLSWLPQRPV------------- 399
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIYIGDKKNNHELITNPYSKKIknfkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 400 -------LVPGTVRHNlVLLGPVD---DLERACAAAGFdaVLDELprGLD-TVLGRGGVGLSLGQRQRLGLARALGSPAA 468
Cdd:PRK13631 122 fqfpeyqLFKDTIEKD-IMFGPVAlgvKKSEAKKLAKF--YLNKM--GLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15608759 469 VLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVI 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
315-521 |
5.37e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVdvtnlapaawwRQLSWL 394
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 PQRPVL---VPGTVRHNLVLLGPVDD------LERACAAAGFDAVLDElprgldtvlgrggvgLSLGQRQRLGLARALGS 465
Cdd:PRK09544 73 PQKLYLdttLPLTVNRFLRLRPGTKKedilpaLKRVQAGHLIDAPMQK---------------LSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 466 PAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQlRRELDCAVLMVSHDlHLVMAKTDEVLCLN 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
337-506 |
6.61e-11 |
|
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: 64.81 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRV---TVLT--GRNGAGKSTTLQAIAGLTAPSSGRITvAGVDVtnlapaawwrqlSWLPQRPV-LVPGTVRHNLv 410
Cdd:COG1245 357 EVEGGEIregEVLGivGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI------------SYKPQYISpDYDGTVEEFL- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 llgpvddleRACAAAGFDA--VLDEL--PRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDArtEQH 486
Cdd:COG1245 423 ---------RSANTDDFGSsyYKTEIikPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQR 491
|
170 180
....*....|....*....|...
gi 15608759 487 VLGAIVERARA---GATVLVVAH 506
Cdd:COG1245 492 LAVAKAIRRFAenrGKTAMVVDH 514
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
315-516 |
9.91e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL-----TAPSSGRITVAG-------VDVTNL 382
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniysprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 383 ApaawwRQLSWLPQRPVLVPGTVRHNLVL---LGPVDDLERacaaagFDAVLDELPRGL---DTVLGR---GGVGLSLGQ 453
Cdd:PRK14239 85 R-----KEIGMVFQQPNPFPMSIYENVVYglrLKGIKDKQV------LDEAVEKSLKGAsiwDEVKDRlhdSALGLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 454 RQRLGLARALGSPAAVLLLDEPTAHLD----ARTEQHVLGaiverARAGATVLVVAHR-QQVAAAGDR 516
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDpisaGKIEETLLG-----LKDDYTMLLVTRSmQQASRISDR 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1-272 |
1.22e-10 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 62.28 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIDPANPGMAGLRRWLGplsILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSL---ALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTaRRPSQLAAQRDAAAVL--ITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVL 158
Cdd:pfam00664 82 KKIL-RQPMSFFDTNSVGELLsrLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 159 IGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVA 238
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 15608759 239 LVAVgIGLRLVF-GEMSLTAGLTVLLLAPEVYWPL 272
Cdd:pfam00664 241 LALW-FGAYLVIsGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
329-506 |
1.26e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 329 RAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTN------LAPAAwwRQLSWLPQRP--VL 400
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVR--KKVGVVFQFPesQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 401 VPGTVRHNlVLLGPVD-----DLERACAAAGFDAVldelprGLDTVL-GRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:PRK13643 98 FEETVLKD-VAFGPQNfgipkEKAEKIAAEKLEMV------GLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190
....*....|....*....|....*....|..
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
333-507 |
1.37e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAgvDVTNLAPA--AWWR-QLSWLPQRPVLVPGTVRHNL 409
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDInlKWWRsKIGVVSQDPLLFSNSIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VL-LGPVDDLE-----------------------RACAAAGFDAVLDE-------------------------------- 433
Cdd:PTZ00265 481 KYsLYSLKDLEalsnyynedgndsqenknkrnscRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvskkvlihd 560
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 434 ----LPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHR 507
Cdd:PTZ00265 561 fvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlKGNENRITIIIAHR 639
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
326-521 |
1.57e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 326 RDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPaAWWRQLSWLPQRPVLVPgt 404
Cdd:PRK13538 11 RDERILFSgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKT-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 405 vrhnlvLLGPVDDLERACAAAGF---DAVLDELPR-GLdtvLGRGGV---GLSLGQRQRLGLARALGSPAAVLLLDEPTA 477
Cdd:PRK13538 88 ------ELTALENLRFYQRLHGPgddEALWEALAQvGL---AGFEDVpvrQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15608759 478 HLD----ARTEQHvlgaIVERARAGATVLVVAHrQQVAAAGDRVVEVN 521
Cdd:PRK13538 159 AIDkqgvARLEAL----LAQHAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-515 |
1.68e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 334 LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSS-----GRITVAG-------VDVTNLApaawwRQLSWLPQRPVLV 401
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqniyerrVNLNRLR-----RQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 PGTVRHNLV----LLG--PVDDLERACAAAGFDAVL-DELPRGLDtvlgRGGVGLSLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:PRK14258 101 PMSVYDNVAygvkIVGwrPKLEIDDIVESALKDADLwDEIKHKIH----KSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15608759 475 PTAHLDARTEQHVLGAIVE-RARAGATVLVVAHR-QQVAAAGD 515
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-521 |
1.71e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAwwRQLSWLPQRPVLVPG-TVRHN--- 408
Cdd:PRK11650 22 GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYPHmSVRENmay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 -LVLLG-PVDDLERACAAA----GFDAVLDELPRgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:PRK11650 100 gLKIRGmPKAEIEERVAEAarilELEPLLDRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15608759 483 TEQHVLGAIVE-RARAGATVLVVAHrQQVAAA--GDRVVEVN 521
Cdd:PRK11650 169 LRVQMRLEIQRlHRRLKTTSLYVTH-DQVEAMtlADRVVVMN 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
340-506 |
2.19e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGRVTVLTGRNGAGKSTTLQAIAGLTapSSGRITvAGVDVTNLAP--AAWWRQLSWLPQRPVLVP-GTVRHNLV----LL 412
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERV--TTGVIT-GGDRLVNGRPldSSFQRSIGYVQQQDLHLPtSTVRESLRfsayLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GP--VDDLERAcaaAGFDAVLD--ELPRGLDTVLGRGGVGLSLGQRQRLGLARAL-GSPAAVLLLDEPTAHLDARTEQHV 487
Cdd:TIGR00956 865 QPksVSKSEKM---EYVEEVIKllEMESYADAVVGVPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQTAWSI 941
|
170
....*....|....*....
gi 15608759 488 LGAIVERARAGATVLVVAH 506
Cdd:TIGR00956 942 CKLMRKLADHGQAILCTIH 960
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
315-513 |
2.30e-10 |
|
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: 63.49 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLS--VRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDV-TNLAPAAwwRQL 391
Cdd:TIGR01257 1937 ILRLNELTkvYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVH--QNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPV---LVPGtvRHNLVLLG-----PVDDLERAcAAAGFDAVldelprGLDTVLGRGGVGLSLGQRQRLGLARAL 463
Cdd:TIGR01257 2015 GYCPQFDAiddLLTG--REHLYLYArlrgvPAEEIEKV-ANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15608759 464 GSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAA 513
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEA 2135
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
333-505 |
2.75e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS---SGRITVAGVDVTNlAPAAWWRQLSWLPQRPVLVPG-TVRHN 408
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHFPTlTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 lvllgpvddLERACAAAGfdavlDELPRgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:cd03233 104 ---------LDFALRCKG-----NEFVR-----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170
....*....|....*..
gi 15608759 489 GAIVERARAGATVLVVA 505
Cdd:cd03233 159 KCIRTMADVLKTTTFVS 175
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
333-506 |
2.85e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRPVlVPGTVR-HNLVL 411
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT-TPGDITvQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LG--PVDDLERACAAAGFDAVLDELPRGLDTVLGRGGVG-LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVL 488
Cdd:PRK10253 104 RGryPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170
....*....|....*....
gi 15608759 489 GAIVERARA-GATVLVVAH 506
Cdd:PRK10253 184 ELLSELNREkGYTLAAVLH 202
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
406-511 |
2.90e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 406 RHNLVLLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQ 485
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
90 100
....*....|....*....|....*.
gi 15608759 486 HVLGAIVERARAGATVLVVAHRQQVA 511
Cdd:NF000106 182 EVWDEVRSMVRDGATVLLTTQYMEEA 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
312-480 |
4.28e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 61.29 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 312 RGGVIRLERLSVRGRDGrapydLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWwRQL 391
Cdd:COG4608 20 RGGLFGRTVGVVKAVDG-----VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGREL-RPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 -------------SWLPQRPVlvpG-TVRHNLVLLGPVDDLERAcaaagfDAVLDELPRgldtvlgrggVGL-------- 449
Cdd:COG4608 94 rrrmqmvfqdpyaSLNPRMTV---GdIIAEPLRIHGLASKAERR------ERVAELLEL----------VGLrpehadry 154
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 450 ----SLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:COG4608 155 phefSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
333-506 |
4.41e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.18 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS--SGRITVAGVDVtnlaPAAWWRQLSWLPQRPVLVPG-TVRHNL 409
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRSTGYVEQQDVHSPNlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VllgpvddleracaaagFDAVLDelprgldtvlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLG 489
Cdd:cd03232 101 R----------------FSALLR---------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170
....*....|....*..
gi 15608759 490 AIVERARAGATVLVVAH 506
Cdd:cd03232 150 FLKKLADSGQAILCTIH 166
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
324-506 |
5.42e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 324 RGRdgRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRP-VLV 401
Cdd:PRK10895 14 KGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEAsIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 PGTVRHNLV-LLGPVDDLERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK10895 92 RLSVYDNLMaVLQIRDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180
....*....|....*....|....*.
gi 15608759 481 ARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
333-517 |
5.64e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAW----WRQLSWLPQRPVLVPgtvrHN 408
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMP----HM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVLLGPVDDLERACAAAG--FDAVLDELPR-GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQ 485
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEerREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 486 HVLGAIVE-RARAGATVLVVAHR-QQVAAAGDRV 517
Cdd:PRK10070 202 EMQDELVKlQAKHQRTIVFISHDlDEAMRIGDRI 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
338-518 |
6.30e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.69 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRItVAGVdvtnlAPAAWWRQLSWLP-QRPVLVPGTVRHNLVLLGPVD 416
Cdd:PRK11247 35 IPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-----APLAEAREDTRLMfQDARLLPWKKVIDNVGLGLKG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 417 DLeRACAAAGFDAVldelprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERAR 496
Cdd:PRK11247 109 QW-RDAALQALAAV------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQ 181
|
170 180
....*....|....*....|....*
gi 15608759 497 A-GATVLVVAH--RQQVAAAgDRVV 518
Cdd:PRK11247 182 QhGFTVLLVTHdvSEAVAMA-DRVL 205
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
304-507 |
6.99e-10 |
|
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: 61.69 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 304 PGRRTVTARGGVIRLERLSVRGRDGRAPY-DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVagvdvtnl 382
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFENIPLVTPNGDVLIeSLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK-------- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 383 aPAAwwRQLSWLPQRPVLVPGTVRHNLVLLGPVDDL-ERACAAAGFDAVLDELPrgLDTVLGRGGvG----------LSL 451
Cdd:TIGR00954 512 -PAK--GKLFYVPQRPYMTLGTLRDQIIYPDSSEDMkRRGLSDKDLEQILDNVQ--LTHILEREG-GwsavqdwmdvLSG 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 452 GQRQRLGLARALGSPAAVLLLDEPTAHLDARTEqhvlGAIVERAR-AGATVLVVAHR 507
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCReFGITLFSVSHR 638
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
321-506 |
8.70e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 321 LSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG--VDVTNLAPAAWWRQLSWLPQRP 398
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 399 vlvpgtvrHNLVLLGPVDDlERACAAAGFDAVLDELPRGLDTVLGRGGVG---------LSLGQRQRLGLARALGSPAAV 469
Cdd:PRK13638 87 --------EQQIFYTDIDS-DIAFSLRNLGVPEAEITRRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 15608759 470 LLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
330-521 |
1.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.41 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 330 APYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQL----SWLPQRP--VLVPG 403
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVrkriGMVFQFPesQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 404 TVRHNlVLLGPVD---DLERACAAAgFDAVLD-ELPRgldTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK13646 102 TVERE-IIFGPKNfkmNLDEVKNYA-HRLLMDlGFSR---DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15608759 480 DARTEQHVLGAIVE-RARAGATVLVVAHR-QQVAAAGDRVVEVN 521
Cdd:PRK13646 177 DPQSKRQVMRLLKSlQTDENKTIILVSHDmNEVARYADEVIVMK 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
334-507 |
1.38e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 334 LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSS--GRITVAGVDVTNLApaawWRQLSWLPQRPVLVPG-TVRHNLV 410
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI----LKRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 ---LLGPVDDLERACAAAGFDAVLDELprGL----DTVLGRGGV-GLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:PLN03211 163 fcsLLRLPKSLTKQEKILVAESVISEL--GLtkceNTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180
....*....|....*....|....*
gi 15608759 483 TEQHVLGAIVERARAGATVLVVAHR 507
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
333-518 |
2.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.59 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlaPAAWW---RQLSWLPQRP--VLVPGTVRh 407
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWdirHKIGMVFQNPdnQFVGATVE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 nlvllgpvDDLERACAAAGFDavLDELPRGLDTVLGRGGVG---------LSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:PRK13650 101 --------DDVAFGLENKGIP--HEEMKERVNEALELVGMQdfkereparLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 479 LDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13650 171 LDPEGRLELIKTIKGiRDDYQMTVISITHDLDEVALSDRVL 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
332-506 |
2.98e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.80 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 332 YDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLapaawwrqlswlpQRPVLvpGTVRHNLVL 411
Cdd:PRK13541 17 FDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKPYC--TYIGHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 LGPVDDLERACAAAGFDAVLDELPRG-----LDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:PRK13541 82 KLEMTVFENLKFWSEIYNSAETLYAAihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 15608759 487 VLGAIVERARAGATVLVVAH 506
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
318-524 |
3.06e-09 |
|
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: 56.85 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 318 LERLSVRGRdgRAPYDLTA-DIEPGrVTVLTGRNGAGKSTTLQAIA----GLTAPSSGRitvaGVDVTNLApaawwRQLS 392
Cdd:cd03240 1 IDKLSIRNI--RSFHERSEiEFFSP-LTLIVGQNGAGKTTIIEALKyaltGELPPNSKG----GAHDPKLI-----REGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRPVLVPGTVRHNLVLLGPVDDLERA--CAAAGFDAVLdELPRGLdtvlgrggvgLSLGQRQ------RLGLARALG 464
Cdd:cd03240 69 VRAQVKLAFENANGKKYTITRSLAILENVifCHQGESNWPL-LDMRGR----------CSGGEKVlasliiRLALAETFG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGAT--VLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:cd03240 138 SNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfqLIVITHDEELVDAADHIYRVEKDG 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
315-483 |
3.19e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSvRGRDGRAPYD-LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVaGVDVtnlapaawwrQLSW 393
Cdd:PRK11819 324 VIEAENLS-KSFGDRLLIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 LPQ-RPVLVPG-TV------RHNLVLLGPVDDLERA-CAAAGFdavldelprgldtvlgRGG-----VG-LSLGQRQRLG 458
Cdd:PRK11819 392 VDQsRDALDPNkTVweeisgGLDIIKVGNREIPSRAyVGRFNF----------------KGGdqqkkVGvLSGGERNRLH 455
|
170 180
....*....|....*....|....*
gi 15608759 459 LARALGSPAAVLLLDEPTAHLDART 483
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
338-492 |
1.29e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvDVTnlapaawwrqLSWLPQRPVL-VPGTV----------- 405
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLI----------VARLQQDPPRnVEGTVydfvaegieeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 406 ------RHNLVLLGPVDDLERACAA-AGFDAVLD-----ELPRGLDTVLGRGGV-------GLSLGQRQRLGLARALGSP 466
Cdd:PRK11147 95 aeylkrYHDISHLVETDPSEKNLNElAKLQEQLDhhnlwQLENRINEVLAQLGLdpdaalsSLSGGWLRKAALGRALVSN 174
|
170 180 190
....*....|....*....|....*....|...
gi 15608759 467 AAVLLLDEPTAHLDART----EQHVL---GAIV 492
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETiewlEGFLKtfqGSII 207
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
328-520 |
1.43e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 328 GRAPYDLTADIE--PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRitvagvdvtnlapaawwrqlswlpqrpvlvpgTV 405
Cdd:cd03227 6 RFPSYFVPNDVTfgEGSLTIITGPNGSGKSTILDAIGLALGGAQSA--------------------------------TR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 406 RHNLVLLGpvddLERACAAAGFDAVLdelprgldtvlgrggVGLSLGQRQRLGLARALGS----PAAVLLLDEPTAHLDA 481
Cdd:cd03227 54 RRSGVKAG----CIVAAVSAELIFTR---------------LQLSGGEKELSALALILALaslkPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 15608759 482 RTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-517 |
1.64e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGV------DVTNLAPAAWW 388
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 389 RQLSWLPQRPVLVPGtvrhnlvlLGPVDDLERACAAAGFDAVlDELPRGLDTVLGRGGV-------------GLSLGQRQ 455
Cdd:PRK14246 90 KEVGMVFQQPNPFPH--------LSIYDNIAYPLKSHGIKEK-REIKKIVEECLRKVGLwkevydrlnspasQLSGGQQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 456 RLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRV 517
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYV 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
294-480 |
2.38e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.62 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 294 ALLGESPSPTPgRRTVTARGGVIRLERLSV-----RGRDGRAPYDLTA------DIEPGRVTVLTGRNGAGKSTTLQAIA 362
Cdd:COG4172 255 KLLAAEPRGDP-RPVPPDAPPLLEARDLKVwfpikRGLFRRTVGHVKAvdgvslTLRRGETLGLVGESGSGKSTLGLALL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 363 GLTaPSSGRITVAGVDVTNLAPAAW--WRQ------------LSwlPQRPVLvpGTVRHNLVLLGP-VDDLERACAAAgf 427
Cdd:COG4172 334 RLI-PSEGEIRFDGQDLDGLSRRALrpLRRrmqvvfqdpfgsLS--PRMTVG--QIIAEGLRVHGPgLSAAERRARVA-- 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15608759 428 dAVLDELprGLD-TVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:COG4172 407 -EALEEV--GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
315-511 |
2.88e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL----TAPSSgRITVAGVDVTNLAPAAW--- 387
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGS-HIELLGRTVQREGRLARdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 --WRQLSWLPQRPVLVPG-TVRHNlVLLGPVDD--LERAC----AAAGFDAVLDELPR-GLDTVLGRGGVGLSLGQRQRL 457
Cdd:PRK09984 83 ksRANTGYIFQQFNLVNRlSVLEN-VLIGALGStpFWRTCfswfTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 458 GLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVA 511
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYA 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
333-507 |
3.08e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS--SGRITVAGVDVTNLAPAawwRQLSWLPQRPVLVPG-TVRHNL 409
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFA---RISGYCEQNDIHSPQvTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 V------LLGPVDDLERACAAagfDAVLD--ELPRGLDTVLGRGGV-GLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PLN03140 975 IysaflrLPKEVSKEEKMMFV---DEVMElvELDNLKDAIVGLPGVtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*..
gi 15608759 481 ARTEQHVLGAIVERARAGATVLVVAHR 507
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-507 |
3.47e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQRPVLVPG-TVRHNLVL------ 411
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlTIAENIFLgrefvn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 -LGPVdDLERACAAAgfDAVLDEL--PRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHL-DARTEQhV 487
Cdd:PRK10762 109 rFGRI-DWKKMYAEA--DKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETES-L 180
|
170 180
....*....|....*....|
gi 15608759 488 LGAIVERARAGATVLVVAHR 507
Cdd:PRK10762 181 FRVIRELKSQGRGIVYISHR 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
333-503 |
5.02e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS----SGRITVAGVDVTNLAPaAWWRQLSWLPQRPVLVPG-TVRH 407
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKK-HYRGDVVYNAETDVHFPHlTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLV----LLGP------VDDLERACAAAGFDAVLDELPRGLDTVLGRGGV-GLSLGQRQRLGLARALGSPAAVLLLDEPT 476
Cdd:TIGR00956 158 TLDfaarCKTPqnrpdgVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVrGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180
....*....|....*....|....*...
gi 15608759 477 AHLDARTEQHVLGAIVERAR-AGATVLV 503
Cdd:TIGR00956 238 RGLDSATALEFIRALKTSANiLDTTPLV 265
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-518 |
6.58e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlAPAAW--WRQLSWLPQRP--VLVPGTVRHNLVLLG 413
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWnlRRKIGMVFQNPdnQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 414 PVDDLERACAAAGFDAVLdeLPRGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE 493
Cdd:PRK13642 108 ENQGIPREEMIKRVDEAL--LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180
....*....|....*....|....*.
gi 15608759 494 -RARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13642 186 iKEKYQLTVLSITHDLDEAASSDRIL 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-517 |
6.64e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 343 VTVLTGRNGAGKSTTLQAIAGL-----TAPSSGRITVAGVDVTN--LAPAAWWRQLSWLPQRPVLVPG-TVRHNLV---- 410
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFPHlTIYDNVAigvk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 ---LLGPVDDL-ERACAAAGFDAVLDELPRGLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQH 486
Cdd:PRK14267 112 lngLVKSKKELdERVEWALKKAALWDEVKDRLNDYPSN----LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190
....*....|....*....|....*....|.
gi 15608759 487 VLGAIVERARAGATVLVVAHRQQVAAAGDRV 517
Cdd:PRK14267 188 IEELLFELKKEYTIVLVTHSPAQAARVSDYV 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-506 |
6.81e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVA-GVDVTNLAPaawwRQLSWLpqRPVLVPgtVRHnLVLLGPVD-- 416
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQ----HQLEFL--RADESP--LQH-LARLAPQEle 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 417 -DLERACAAAGF--DAVLDELPRgldtvlgrggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE 493
Cdd:PRK10636 408 qKLRDYLGGFGFqgDKVTEETRR------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170
....*....|...
gi 15608759 494 raRAGATVlVVAH 506
Cdd:PRK10636 476 --FEGALV-VVSH 485
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
315-524 |
9.67e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 53.65 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAP---SSGRITVAGVDVTnlAPAAW-- 387
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPAlnDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT--AKTVWdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 388 WRQLSWLPQRP--VLVPGTVRhnlvllgpvDDLeracaAAGFD--AV-LDELPRGLDTVLGRGGV---------GLSLGQ 453
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVG---------DDV-----AFGLEnrAVpRPEMIKIVRDVLADVGMldyidsepaNLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15608759 454 RQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVVEVNsDG 524
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLD-DG 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
337-521 |
1.31e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGvdvtnlapaawwRQLSWLPQRPVLVPGTVR--HNLVLLGP 414
Cdd:PRK11300 27 EVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG------------QHIEGLPGHQIARMGVVRtfQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 415 VDDLERACAA------AGFDAVLDELPR-------------------GLDTVLGRGGVGLSLGQRQRLGLARALGSPAAV 469
Cdd:PRK11300 95 MTVIENLLVAqhqqlkTGLFSGLLKTPAfrraesealdraatwlervGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15608759 470 LLLDEPTAHLDARtEQHVLGAIVERARA--GATVLVVAHRQQ-VAAAGDRVVEVN 521
Cdd:PRK11300 175 LMLDEPAAGLNPK-ETKELDELIAELRNehNVTVLLIEHDMKlVMGISDRIYVVN 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-480 |
2.05e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 342 RVTVLtGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRP---VLVPgTVRHNlVLLGPVD-D 417
Cdd:PRK13652 32 RIAVI-GPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddqIFSP-TVEQD-IAFGPINlG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 418 LERACAAAGFDAVLDELprGLDTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK13652 109 LDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-507 |
2.16e-07 |
|
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: 50.45 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQlswlpqrpvlvpgtvrhnlvllgpvddle 419
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 420 racaaagfdavldelprgldTVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERA---- 495
Cdd:smart00382 52 --------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllll 111
|
170
....*....|....
gi 15608759 496 --RAGATVLVVAHR 507
Cdd:smart00382 112 ksEKNLTVILTTND 125
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
336-506 |
2.41e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 52.28 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 336 ADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAP-----SSGRITVAgvdvtnLAPAAWWRQLSWLPQRPVLVPGTVRHNLV 410
Cdd:COG4938 15 AELELKPLTLLIGPNGSGKSTLIQALLLLLQSnfiylPAERSGPA------RLYPSLVRELSDLGSRGEYTADFLAELEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LlgPVDDLERACAAAGFDAVLDELPRGLDTV-LGRGGVGLSL----------------GQRQRLGL---ARALGSPAAVL 470
Cdd:COG4938 89 L--EILDDKSKELLEQVEEWLEKIFPGKVEVdASSDLVRLVFrpsgngkriplsnvgsGVSELLPIllaLLSAAKPGSLL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 15608759 471 LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:COG4938 167 IIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
315-518 |
2.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.92 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPY--DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT--NLAPAAwwRQ 390
Cdd:PRK13632 7 MIKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIR--KK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 391 LSWLPQRP--VLVPGTVRhnlvllgpvDD----LERACAAAG-FDAVLDELPR--GLDTVLGRGGVGLSLGQRQRLGLAR 461
Cdd:PRK13632 85 IGIIFQNPdnQFIGATVE---------DDiafgLENKKVPPKkMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVV 518
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDMDEAILADKVI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
316-510 |
3.02e-07 |
|
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: 52.88 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 316 IRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTA--PSSGRItvagvdVTNLA--PAAWWRQL 391
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRI------IYHVAlcEKCGYVER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 392 SWLPQRPVLVPG-TVRHNLVLLGPVDD-------------LERACAAAGFDAVLDELPRGLDTV--LGRGGVG------- 448
Cdd:TIGR03269 75 PSKVGEPCPVCGgTLEPEEVDFWNLSDklrrrirkriaimLQRTFALYGDDTVLDNVLEALEEIgyEGKEAVGravdlie 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 449 --------------LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQV 510
Cdd:TIGR03269 155 mvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
338-506 |
3.23e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG--VDVTNLAPAAWWRQLSWLPQRP---VLVPgTVRHNlVLL 412
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddqLFAP-TVEED-VAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPV------DDLER----ACAAAGFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:PRK13639 103 GPLnlglskEEVEKrvkeALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180
....*....|....*....|....
gi 15608759 483 TEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-516 |
3.73e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 340 PGR-VTVLTGRNGAGKSTTLQAIAGLTAPSSG-----RITVAGVDVTNLAPA-AWWRQLSWLPQRPVLVPGTVRHNLVL- 411
Cdd:PRK14271 45 PARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVLAg 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 412 -----LGPVDDLE-----RACAAAGFDAVLDELprgldtvlGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDA 481
Cdd:PRK14271 125 vrahkLVPRKEFRgvaqaRLTEVGLWDAVKDRL--------SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 482 RTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDR 516
Cdd:PRK14271 197 TTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDR 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
304-480 |
4.93e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 304 PGRRTVTARGG-VIRLERLSvrgrdGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNL 382
Cdd:PRK15439 256 PGNRRQQAAGApVLTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 383 APAAWWRQ-LSWLP---QRPVL---------VPGTVRHNLVL-LGPVDD---LERACAAAGFDAVLDELPRGldtvlgrg 445
Cdd:PRK15439 331 STAQRLARgLVYLPedrQSSGLyldaplawnVCALTHNRRGFwIKPAREnavLERYRRALNIKFNHAEQAAR-------- 402
|
170 180 190
....*....|....*....|....*....|....*
gi 15608759 446 gvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK15439 403 --TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
348-482 |
5.31e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 348 GRNGAGKSTTLQAIAGLTAPSSGRITVAG--VDVTNLAPaawwrqlswlpQRPVlvpG------------TVRHNLVLLG 413
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT-----------RRRV---GymsqafslygelTVRQNLELHA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 414 -----PVDDLERACAAA----GFDAVLDELPRGLdtvlgrggvglSLGQRQRLGLARA-LGSPaAVLLLDEPTAHLD--A 481
Cdd:NF033858 365 rlfhlPAAEIAARVAEMlerfDLADVADALPDSL-----------PLGIRQRLSLAVAvIHKP-ELLILDEPTSGVDpvA 432
|
.
gi 15608759 482 R 482
Cdd:NF033858 433 R 433
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
329-518 |
6.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.16 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 329 RAPYDLTA------DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITV------AGV----DVTNLApaawwRQLS 392
Cdd:PRK13645 19 KTPFEFKAlnntslTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLkkikEVKRLR-----KEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 WLPQRP--VLVPGTVRHNLVLlGPVDdleracAAAGFDAVLDELPRGLDTV------LGRGGVGLSLGQRQRLGLARALG 464
Cdd:PRK13645 94 LVFQFPeyQLFQETIEKDIAF-GPVN------LGENKQEAYKKVPELLKLVqlpedyVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 465 SPAAVLLLDEPTAHLDARTEQHVLGaIVER--ARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFIN-LFERlnKEYKKRIIMVTHNmDQVLRIADEVI 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
338-506 |
7.56e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.84 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAW--WRQLSWL----------PQRPV--LVPG 403
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkaFRRDIQMvfqdsisavnPRKTVreIIRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 404 TVRHNLvllgpvdDLERACAAAGFDAVLDELprGLD-TVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:PRK10419 115 PLRHLL-------SLDKAERLARASEMLRAV--DLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180
....*....|....*....|....*
gi 15608759 483 TEQHVLGAIVE-RARAGATVLVVAH 506
Cdd:PRK10419 186 LQAGVIRLLKKlQQQFGTACLFITH 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
338-507 |
7.83e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVT-NLAPAAWWRQLSWLPQrpvlvpgtvRHNLVLLGPVD 416
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQ---------ELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 417 D---LERACAAAGF----------DAVLDELPRGLDTvlgRGGVG-LSLGQRQRLGLARALGSPAAVLLLDEPTAHLDAR 482
Cdd:PRK10982 92 DnmwLGRYPTKGMFvdqdkmyrdtKAIFDELDIDIDP---RAKVAtLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180
....*....|....*....|....*
gi 15608759 483 TEQHVLGAIVERARAGATVLVVAHR 507
Cdd:PRK10982 169 EVNHLFTIIRKLKERGCGIVYISHK 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
321-520 |
9.05e-07 |
|
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: 49.24 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 321 LSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIagltapssgritvagvdvtnLAPAAWWRQLSWLPQRPvl 400
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--------------------LYASGKARLISFLPKFS-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 401 vpgtvRHNLVLLGPVDDLeracaaagFDAVLDELPrgldtvLGRGGVGLSLGQRQRLGLARALGSPA--AVLLLDEPTAH 478
Cdd:cd03238 59 -----RNKLIFIDQLQFL--------IDVGLGYLT------LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15608759 479 LDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-521 |
1.17e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLSWLPQRP--VLVPGTVRHNlV 410
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdnQFVGSIVKYD-V 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 411 LLG------PVDDLERACAAAGFDAVL----DELPRGLdtvlgrggvglSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK13648 106 AFGlenhavPYDEMHRRVSEALKQVDMleraDYEPNAL-----------SGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15608759 481 ARTEQHVLGAIVE-RARAGATVLVVAHRQQVAAAGDRVVEVN 521
Cdd:PRK13648 175 PDARQNLLDLVRKvKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
315-503 |
1.20e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGRDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDvtnLAPAAWWRQLS-- 392
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD---MADARHRRAVCpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 393 --WLPQ------RPVLvpgTVRHNLV----LLGpVDDLERAcaaagfdAVLDELPR--GLDTVLGRGGVGLSLGQRQRLG 458
Cdd:NF033858 78 iaYMPQglgknlYPTL---SVFENLDffgrLFG-QDAAERR-------RRIDELLRatGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15608759 459 LARALGSPAAVLLLDEPTAHLD--ARTEQHVLGAIVERARAGATVLV 503
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDplSRRQFWELIDRIRAERPGMSVLV 193
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
333-520 |
2.33e-06 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKST----TLQA------IAGLTAPSSGRITVAG---VD-VTNLAPAAWWRQLSwLPQRP 398
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSlafdTIYAegqrryVESLSAYARQFLGQMDkpdVDsIEGLSPAIAIDQKT-TSRNP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 399 VLVPGTVRhnlvllGPVDDLERACAAAGFDAVLDELPR-GLDTV-LGRGGVGLSLGQRQRLGLARALGSPAAVLL--LDE 474
Cdd:cd03270 92 RSTVGTVT------EIYDYLRLLFARVGIRERLGFLVDvGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15608759 475 PTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:cd03270 166 PSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-524 |
2.58e-06 |
|
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: 49.15 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 437 GLDTV-LGRGGVGLSLGQRQRLGLARALGSPA---AVLLLDEPTAHL---DARTEQHVLGAIVERaraGATVLVVAHRQQ 509
Cdd:cd03271 157 GLGYIkLGQPATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKKLLEVLQRLVDK---GNTVVVIEHNLD 233
|
90
....*....|....*
gi 15608759 510 VAAAGDRVVEVNSDG 524
Cdd:cd03271 234 VIKCADWIIDLGPEG 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
335-480 |
3.71e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 335 TADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVagvdvtnlaPAAWwrQLSWLPQR-PVL-VPGTvrhNLVLL 412
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNW--QLAWVNQEtPALpQPAL---EYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 413 GPVD--DLERACAAAG--------------FDAV--------LDELPRGL---DTVLGRGGVGLSLGQRQRLGLARALGS 465
Cdd:PRK10636 87 GDREyrQLEAQLHDANerndghaiatihgkLDAIdawtirsrAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170
....*....|....*
gi 15608759 466 PAAVLLLDEPTAHLD 480
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
331-480 |
4.10e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 331 PYDLTadIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQLS------WLPQRpvlvpgt 404
Cdd:PRK10522 341 PINLT--IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSavftdfHLFDQ------- 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 405 vrhnlvLLGPVDDLERACAAAGFDAVLdELPRGLDTVLGR-GGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PRK10522 412 ------LLGPEGKPANPALVEKWLERL-KMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
5-255 |
4.12e-06 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 48.54 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 5 VGISGCAIGSAIVLASIVAGVIDPANPGMAGLRRWLGplsILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVT 84
Cdd:cd18544 9 LLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLAL---LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 85 ARRPSQLaaQRDAAAVLITR---GLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIGL 161
Cdd:cd18544 86 RLPLSFF--DRTPVGRLVTRvtnDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 162 ATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVA 241
Cdd:cd18544 164 KSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
250
....*....|....
gi 15608759 242 VGIGLRLVFGEMSL 255
Cdd:cd18544 244 WYGGGQVLSGAVTL 257
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-276 |
4.44e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 48.72 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 179 ARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVAVGIGLRLVFGEMSLTAG 258
Cdd:cd18565 194 ARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGT 273
|
90 100
....*....|....*....|....
gi 15608759 259 LTV------LLLAPEVYWPLRRVG 276
Cdd:cd18565 274 LTVgtlvtfLFYTQRLLWPLTRLG 297
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
338-517 |
6.64e-06 |
|
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: 48.67 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGL--TAPSSGRITVAGV--------DVTNLAPAAWWRQLSWLPQRPVLVPGTVRH 407
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSplkasnirDTERAGIVIIHQELTLVPELSVAENIFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 408 NLVLLGPV---DDLERACAAAGFDAVLDELPrgldtvLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTE 484
Cdd:TIGR02633 104 EITLPGGRmayNAMYLRAKNLLRELQLDADN------VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET 177
|
170 180 190
....*....|....*....|....*....|....
gi 15608759 485 QHVLGAIVERARAGATVLVVAHR-QQVAAAGDRV 517
Cdd:TIGR02633 178 EILLDIIRDLKAHGVACVYISHKlNEVKAVCDTI 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
315-524 |
1.29e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 315 VIRLERLSVRGrDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAP----SSGRITVAGVDVtnlAPAAW-WR 389
Cdd:PRK10418 4 QIELRNIALQA-AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV---APCALrGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 390 QLSWLPQ------RPVLVPGT-VRHNLVLLGPVDDLERACAAagFDAV-LDELPRgldtVLGRGGVGLSLGQRQRLGLAR 461
Cdd:PRK10418 80 KIATIMQnprsafNPLHTMHThARETCLALGKPADDATLTAA--LEAVgLENAAR----VLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 462 ALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARA-GATVLVVAHRQQVAAAGDRVVEVNSDG 524
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
333-509 |
1.30e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAgvdvTNLApAAWWRQ----LSwlPQRPVL-------- 400
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE-VAYFDQhraeLD--PEKTVMdnlaegkq 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 401 ---VPGTVRHnlvLLGPVDDL----ERAcaaagfdavldelprgldtvlgRGGV-GLSLGQRQRLGLARALGSPAAVLLL 472
Cdd:PRK11147 410 evmVNGRPRH---VLGYLQDFlfhpKRA----------------------MTPVkALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 15608759 473 DEPTAHLDARTEQhvlgaIVERARAG--ATVLVVAHRQQ 509
Cdd:PRK11147 465 DEPTNDLDVETLE-----LLEELLDSyqGTVLLVSHDRQ 498
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
431-524 |
1.56e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 431 LDELPrgldtvLGRGGVGLSLGQRQRLGLARALGSPA---AVLLLDEPTAHL---DARTEQHVLGAIVERaraGATVLVV 504
Cdd:PRK00635 798 LDYLP------LGRPLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLhthDIKALIYVLQSLTHQ---GHTVVII 868
|
90 100
....*....|....*....|
gi 15608759 505 AHRQQVAAAGDRVVEVNSDG 524
Cdd:PRK00635 869 EHNMHVVKVADYVLELGPEG 888
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-520 |
2.31e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 437 GLDTV-LGRGGVGLSLGQRQRLGLARALGSP-AAVL-LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAA 513
Cdd:TIGR00630 476 GLDYLsLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA 555
|
....*..
gi 15608759 514 GDRVVEV 520
Cdd:TIGR00630 556 ADYVIDI 562
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-524 |
2.83e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTaPS---SGRITVAGVDVTnlapAAWWRQ-----LSWLPQRPVLVPG-TVRHN 408
Cdd:PRK13549 28 VRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQ----ASNIRDteragIAIIHQELALVKElSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 409 LVL------LGPVDDLE---RAcaaagfDAVLDELPRGLDTVLGRGGVGLslGQRQRLGLARALGSPAAVLLLDEPTAHL 479
Cdd:PRK13549 103 IFLgneitpGGIMDYDAmylRA------QKLLAQLKLDINPATPVGNLGL--GQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15608759 480 DARtEQHVLGAIVERARA-GATVLVVAHR-QQVAAAGDRVVeVNSDG 524
Cdd:PRK13549 175 TES-ETAVLLDIIRDLKAhGIACIYISHKlNEVKAISDTIC-VIRDG 219
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
316-373 |
3.34e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 45.76 E-value: 3.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 316 IRLERLSVRGRdgRAPYDLTADIE-PGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRIT 373
Cdd:COG3950 1 MRIKSLTIENF--RGFEDLEIDFDnPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
321-519 |
4.54e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.30 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 321 LSVRG-----RDGRAPYDLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTnlapaawWRQLSWL- 394
Cdd:PRK11701 7 LSVRGltklyGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ-------LRDLYALs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 395 -PQRPVLVP---GTVRHNlvllgPVDDLE------------------------RACAAAGFDAV------LDELPRgldt 440
Cdd:PRK11701 80 eAERRRLLRtewGFVHQH-----PRDGLRmqvsaggnigerlmavgarhygdiRATAGDWLERVeidaarIDDLPT---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 441 vlgrggvGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLD----AR---------TEQHVLGAIVERARAGATVLvvAHR 507
Cdd:PRK11701 151 -------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARlldllrglvRELGLAVVIVTHDLAVARLL--AHR 221
|
250
....*....|..
gi 15608759 508 QQVAAAGdRVVE 519
Cdd:PRK11701 222 LLVMKQG-RVVE 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
101-275 |
7.35e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.89 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 101 LITR--GLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIGLATTNPSAAALAAMTAVQ 178
Cdd:cd18782 101 LSTRisELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 179 ARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVaVGIGLRLVF-GEMSLTA 257
Cdd:cd18782 181 SYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLV-LWVGAYLVLrGELTLGQ 259
|
170
....*....|....*...
gi 15608759 258 GLTVLLLAPEVYWPLRRV 275
Cdd:cd18782 260 LIAFRILSGYVTGPILRL 277
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
337-488 |
8.29e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAW---WRQLSWLPQRPV--LVPgtvRHNL-- 409
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPYgsLNP---RKKVgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 410 VLLGPVD---DLERACAAAgfdAVLDELPRgldtvlgrggVGL------------SLGQRQRLGLARALGSPAAVLLLDE 474
Cdd:PRK11308 114 ILEEPLLintSLSAAERRE---KALAMMAK----------VGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADE 180
|
170
....*....|....
gi 15608759 475 PTAHLDARTEQHVL 488
Cdd:PRK11308 181 PVSALDVSVQAQVL 194
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
442-524 |
1.14e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 442 LGRGGVGLSLGQRQRLGLARALGSPA---AVLLLDEPTAHL---DARTEQHVLGAIVErarAGATVLVVAHRQQVAAAGD 515
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKLLEVLQRLVD---KGNTVVVIEHNLDVIKTAD 899
|
....*....
gi 15608759 516 RVVEVNSDG 524
Cdd:TIGR00630 900 YIIDLGPEG 908
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
449-520 |
1.53e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 449 LSLGQRQRLGLARALGSP--AAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAAAGDRVVEV 520
Cdd:PRK00635 477 LSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDI 550
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
437-506 |
2.30e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.15 E-value: 2.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608759 437 GLD-TVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAH 506
Cdd:PRK13651 153 GLDeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1-276 |
5.05e-04 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 42.02 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 1 MACGVGISGCAIGSAIVLASIVAGVIDPANPGMAglrrWLGPLsILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVL 80
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVEKDLEAL----LLVPL-AIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 81 TAVTARRPSQLAAQRdaAAVLITR---GLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMV 157
Cdd:cd18552 80 DKLLRLPLSFFDRNS--SGDLISRitnDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 158 LIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLELLATLGV 237
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15608759 238 ALVaVGIGLRLVFGEmSLTAG-----LTVLLLApevYWPLRRVG 276
Cdd:cd18552 238 ALV-LWYGGYQVISG-ELTPGefisfITALLLL---YQPIKRLS 276
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
45-264 |
5.46e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 42.09 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 45 ILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVtaRRPSQLAAQRDAAAVLITR---GLDGLRPYFTGYLPTLL 121
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHL--QRLSLDFHERETSGRIMTRmtsDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 122 LAAILTPATVAVIGLYDLKSMAIVVITLPLIPIFMVLIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPE 201
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNA 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15608759 202 QRIAELSADHRRSAMATLRIAFLSALVLELLATLGVALVaVGIGLRLVFGEmSLTAG-LTVLLL 264
Cdd:cd18546 202 ERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV-LLVGAWRVAAG-TLTVGvLVAFLL 263
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
333-485 |
9.10e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTApSSGRITVAGVDVTNLAPaawwRQLswLPQR--------------- 397
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNR----RQL--LPVRhriqvvfqdpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 398 PVL-VPGTVRHNLVLLGPvdDLERACAAAGFDAVLDELprGLDTVL-GRGGVGLSLGQRQRLGLARALGSPAAVLLLDEP 475
Cdd:PRK15134 377 PRLnVLQIIEEGLRVHQP--TLSAAQREQQVIAVMEEV--GLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170
....*....|
gi 15608759 476 TAHLDaRTEQ 485
Cdd:PRK15134 453 TSSLD-KTVQ 461
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
317-362 |
9.78e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 9.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15608759 317 RLERLSVRG----RDgrapydltADIEPGRVTVLTGRNGAGKSTTLQAIA 362
Cdd:COG4637 1 MITRIRIKNfkslRD--------LELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
333-503 |
1.16e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS---SGRITVAGVDVTNLAPaawwRQLS-WLPQRPVLVP------ 402
Cdd:PLN03140 183 DASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP----RKTSaYISQNDVHVGvmtvke 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 403 -----------GTvRHNLVL----------LGP---VDDLERACAAAGFDAVL--DELPR--GL----DTVLGRGGV-GL 449
Cdd:PLN03140 259 tldfsarcqgvGT-RYDLLSelarrekdagIFPeaeVDLFMKATAMEGVKSSLitDYTLKilGLdickDTIVGDEMIrGI 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15608759 450 SLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHV---LGAIVERARagATVLV 503
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkcLQQIVHLTE--ATVLM 392
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
342-362 |
1.18e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.52 E-value: 1.18e-03
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
338-403 |
1.42e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 338 IEPGRVTVLTGRNGAGKSTTLQAIAGLTAPS--SGRITVAGVDVTNLAPAAWWRQLSWLP-QRPVLVPG 403
Cdd:CHL00131 30 INKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGIFLAfQYPIEIPG 98
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
314-504 |
1.57e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 314 GVIRLERLSVRGRDGRAPYDLTAdiEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAGVDVTNLAPAAWWRQlsw 393
Cdd:PRK11288 254 GEVRLRLDGLKGPGLREPISFSV--RAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRA--- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 394 lpqRPVLVP------GTV--------------RHNLVLLGPVDDLERACAAAGFDAVLDELPRGLDTVLGRggvgLSLGQ 453
Cdd:PRK11288 329 ---GIMLCPedrkaeGIIpvhsvadninisarRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMN----LSGGN 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 454 RQRLGLARALGSPAAVLLLDEPTAHLD--ARTEqhVLGAIVERARAGATVLVV 504
Cdd:PRK11288 402 QQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAQGVAVLFV 452
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
335-369 |
1.65e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|....*
gi 15608759 335 TADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSS 369
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
333-361 |
2.39e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 2.39e-03
10 20
....*....|....*....|....*....
gi 15608759 333 DLTADIEPGrVTVLTGRNGAGKSTTLQAI 361
Cdd:pfam13476 11 DQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
317-371 |
2.65e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15608759 317 RLERLSVRGrdgrapY----DLTADIEPGrVTVLTGRNGAGKSTTLQAIAGLTAPSSGR 371
Cdd:COG3593 2 KLEKIKIKN------FrsikDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
440-518 |
2.79e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 440 TVLGRGGVGLSLGQRQRLGLARALGSPAAVLLLDEPTAHLDARTEQHVLGAI-VERARAGATVLVVAHRQQVAA-AGDRV 517
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRV 239
|
.
gi 15608759 518 V 518
Cdd:PRK10261 240 L 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-518 |
2.92e-03 |
|
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: 40.19 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGL-TAPSSGRITVAGVDVTNLAPAAWWRQ-LSWLPQ---RPVLVPGT-VR 406
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAgIAMVPEdrkRHGIVPILgVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 407 HNLVL--LGPVDDLERACAAAGFDAVLDELPR------GLDTVLGRggvgLSLGQRQRLGLARALGSPAAVLLLDEPTAH 478
Cdd:TIGR02633 358 KNITLsvLKSFCFKMRIDAAAELQIIGSAIQRlkvktaSPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15608759 479 LDARTEQHVLGAIVERARAGATVLVVAHR-QQVAAAGDRVV 518
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVL 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
450-480 |
3.74e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|.
gi 15608759 450 SLGQRQRLGLARALGSPAAVLLLDEPTAHLD 480
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
337-362 |
4.25e-03 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 38.43 E-value: 4.25e-03
10 20
....*....|....*....|....*.
gi 15608759 337 DIEPGRVTVLTGRNGAGKSTTLQAIA 362
Cdd:cd03283 21 DMEKKNGILITGSNMSGKSTFLRTIG 46
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
343-364 |
4.73e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 4.73e-03
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
45-246 |
4.92e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 39.12 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 45 ILLVLWGLRASIQWLQARLAQRGASAVIADLSGQVLTAVTAR----RPSQLAAQRdaaavliTRGLDGLRPYFTGYLPTL 120
Cdd:cd18586 47 GMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELplesRPSGYWQQL-------LRDLDTLRNFLTGPSLFA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 121 LLAAILTPATVAVIGLYdlkSMAIVVITLPLIPIFMVLIGL---ATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRA 197
Cdd:cd18586 120 FFDLPWAPLFLAVIFLI---HPPLGWVALVGAPVLVGLAWLnhrATRKPLGEANEAQAARDALAAETLRNAETIKALGML 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15608759 198 SGPEQRIAELsadHRRSAMATLRIAFLSALVLELLATL----GVALVAVGIGL 246
Cdd:cd18586 197 GNLRRRWEAR---HAETLELQIRASDLAGAISAIGKTLrmalQSLILGVGAYL 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
333-493 |
6.42e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.30 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 333 DLTADIEPGRVTVLTGRNGAGKSTTLQAIAGLTaPS------SGRITVAGVDVTNlAPAAWWR-----QLSWLPQRPvlv 401
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLH-ASEQTLRgvrgnKIAMIFQEP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 402 pgtvrhnLVLLGPVDDLERACA-------AAGFDAVLDELPRGLDTVLGRGGVG--------LSLGQRQRLGLARALGSP 466
Cdd:PRK15134 102 -------MVSLNPLHTLEKQLYevlslhrGMRREAARGEILNCLDRVGIRQAAKrltdyphqLSGGERQRVMIAMALLTR 174
|
170 180
....*....|....*....|....*..
gi 15608759 467 AAVLLLDEPTAHLDARTEQHVLGAIVE 493
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRE 201
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
11-273 |
6.48e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 38.64 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 11 AIGSAIVLASIVAGVIDP-----------ANPGMAGLRRWLGPL-SILLVLWGLRASIQWLQARLAQRGASAVIADLSGQ 78
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPyltkiliddvlIQLGPGGNTSLLLLLvLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 79 VLTAVTA--------RRPSQLAAQrdaaavlITRGLDGLRPYFTGYLPTLLLAAILTPATVAVIGLYDLKSMAIVVITLP 150
Cdd:cd18563 82 LYEHLQRlslsffdkRQTGSLMSR-------VTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 151 LIPIFMVLIGLATTNPSAAALAAMTAVQARLLDLIAGIPTLRALGRASGPEQRIAELSADHRRSAMATLRIAFLSALVLE 230
Cdd:cd18563 155 LVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLT 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15608759 231 LLATLGVALV-AVGiGLRLVFGEMSLTAGLTVLLLAPEVYWPLR 273
Cdd:cd18563 235 FLTSLGTLIVwYFG-GRQVLSGTMTLGTLVAFLSYLGMFYGPLQ 277
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
334-403 |
7.96e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 7.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 334 LTADIEPGRVTVLTGRNGAGKSTTLQAIAGLT--APSSGRITVAGVDVTNLAPAAWWRQLSWLP-QRPVLVPG 403
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfQYPVEIPG 92
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
317-376 |
8.74e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 8.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608759 317 RLERLSVRGRDGRAPYDL---TADIEPGRVTVLTGRNGAGKSTTLQAIAGLTAPSSGRITVAG 376
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
437-520 |
9.63e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608759 437 GLD--TvLGRGGVGLSLGQRQRLGLARALGSP-AAVL-LLDEPTAHLDARTEQHVLGAIVERARAGATVLVVAHRQQVAA 512
Cdd:COG0178 473 GLDylT-LDRSAGTLSGGEAQRIRLATQIGSGlVGVLyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIR 551
|
....*...
gi 15608759 513 AGDRVVEV 520
Cdd:COG0178 552 AADYIIDI 559
|
|
| |
