|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-498 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 567.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAG 82
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINdgVVGALDVASNLVLDRLngAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMA 162
Cdd:COG1129 81 IAIIHQELN--LVPNLSVAENIFLGRE--PRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAM 242
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 243 LGQNLG-LHSIDARAAGAPVFSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAY 321
Cdd:COG1129 237 VGRELEdLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 322 APRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLATLS 401
Cdd:COG1129 317 RIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 402 GGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLTELDEALETADRILVMSENTIVGEH 480
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
490
....*....|....*...
gi 1998276353 481 RNADVDMDRLLAEVAGQR 498
Cdd:COG1129 477 DREEATEEAIMAAATGGA 494
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-490 |
2.95e-132 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 392.85 E-value: 2.95e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMR 80
Cdd:COG3845 1 MMPPAL-ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNINdgVVGALDVASNLVLdrlnGA--GSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIA 158
Cdd:COG3845 80 LGIGMVHQHFM--LVPNLTVAENIVL----GLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGA 238
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 239 VNAMLGQNLGLH-SIDARAAGAPVFSARDLRIAPGA-----KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAG 312
Cdd:COG3845 234 AELMVGREVLLRvEKAPAEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 313 SMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSL--PFLPRFSNMSVTRRRAERQTAREQIADLKIVC 390
Cdd:COG3845 314 SIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 391 RSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLREsARDR--ATLVFLTELDEALETADRI 468
Cdd:COG3845 394 PGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAgaAVLLISEDLDEILALSDRI 472
|
490 500
....*....|....*....|..
gi 1998276353 469 LVMSENTIVGEHRNADVDMDRL 490
Cdd:COG3845 473 AVMYEGRIVGEVPAAEATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-491 |
1.30e-123 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 370.78 E-value: 1.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAF-GPNAvLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFpGVKA-LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNINdgVVGALDVASNLVLDRLNGAGSgfFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:PRK11288 80 GVAIIYQELH--LVPEMTVAENLYLGQLPHKGG--IVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKP-LDYEGAVN 240
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAqVDRDQLVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 241 AMLGQNLG-LHSIDARAAGAPVFSARDLRiAPG-AKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDG 318
Cdd:PRK11288 236 AMVGREIGdIYGYRPRPLGEVRLRLDGLK-GPGlREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 319 RAYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMS-VTRRRAERQTAREQIADLKIVCRSERDDL 397
Cdd:PRK11288 315 KPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 398 ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLTELDEALETADRILVMSENTI 476
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
490
....*....|....*
gi 1998276353 477 VGEHRNADVDMDRLL 491
Cdd:PRK11288 475 AGELAREQATERQAL 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-484 |
2.14e-103 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 319.04 E-value: 2.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGV 83
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINdgVVGALDVASNLVLDRLngAGSGFFFNP----RKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIAR 159
Cdd:PRK09700 83 GIIYQELS--VIDELTVLENLYIGRH--LTKKVCGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAV 239
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 240 NAMLGQNL-----GLHSIDARAAGAPVFSARDL--RIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAG 312
Cdd:PRK09700 239 RLMVGRELqnrfnAMKENVSNLAHETVFEVRNVtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 313 SMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSL-PFLP--RFSN-MSVTRRRAERQTAREQIADLKI 388
Cdd:PRK09700 319 EIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAIsRSLKdgGYKGaMGLFHEVDEQRTAENQRELLAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 389 VCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLTELDEALETADR 467
Cdd:PRK09700 399 KCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDR 478
|
490
....*....|....*..
gi 1998276353 468 ILVMSENTIVGEHRNAD 484
Cdd:PRK09700 479 IAVFCEGRLTQILTNRD 495
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-492 |
7.27e-96 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 299.54 E-value: 7.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGV--HRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQ 88
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 NINdgVVGALDVASNLVLDrlNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVM 168
Cdd:PRK13549 90 ELA--LVKELSVLENIFLG--NEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQNLG 248
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 249 -LHSIDARAAGAPVFSARDLR----IAPGAK---PLSMELGAGEVVAVTGLVGVGKTRLAETLFGI-HAPLAGSMQLDGR 319
Cdd:PRK13549 246 aLYPREPHTIGEVILEVRNLTawdpVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 320 AYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLAT 399
Cdd:PRK13549 326 PVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDR-ATLVFLTELDEALETADRILVMSENTIVG 478
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
490
....*....|....
gi 1998276353 479 EHRNADVDMDRLLA 492
Cdd:PRK13549 486 DLINHNLTQEQVME 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-496 |
3.87e-95 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 297.30 E-value: 3.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGV 83
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINdgVVGALDVASNLVLDR--LNGAGSgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:PRK10762 82 GIIHQELN--LIPQLTIAENIFLGRefVNRFGR---IDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNA 241
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 242 MLGQNLGLH--SIDaRAAGAPVFSARDLRiAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR 319
Cdd:PRK10762 237 MVGRKLEDQypRLD-KAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 320 AYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADL-KIVCRSERDDLA 398
Cdd:PRK10762 315 EVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfNIKTPSMEQAIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 399 TLSGGNQQKVTVARWL-TQPsRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFL-TELDEALETADRILVMSENTI 476
Cdd:PRK10762 395 LLSGGNQQKVAIARGLmTRP-KVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVsSEMPEVLGMSDRILVMHEGRI 473
|
490 500
....*....|....*....|
gi 1998276353 477 VGEHRNADVDMDRLLAEVAG 496
Cdd:PRK10762 474 SGEFTREQATQEKLMAAAVG 493
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-492 |
3.64e-94 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 295.04 E-value: 3.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQNI 90
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 NdgVVGALDVASNlVLDRLngagsgfffnPRKVRREAR--EVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVM 168
Cdd:PRK15439 96 L--LFPNLSVKEN-ILFGL----------PKRQASMQKmkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV--GQFDEKPLD------YEGAVN 240
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlsGKTADLSTDdiiqaiTPAARE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 241 AML--GQNLGLHSIDAR---AAGAPVFSARDLRiAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQ 315
Cdd:PRK15439 243 KSLsaSQKLWLELPGNRrqqAAGAPVLTVEDLT-GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 316 LDGRAYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENM-SLPflprFSNMSV-TRRRAERQTAREQIADLKIVCRSE 393
Cdd:PRK15439 322 LNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVcALT----HNRRGFwIKPARENAVLERYRRALNIKFNHA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 394 RDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFL-TELDEALETADRILVMS 472
Cdd:PRK15439 398 EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFIsSDLEEIEQMADRVLVMH 477
|
490 500
....*....|....*....|
gi 1998276353 473 ENTIVGEHRNADVDMDRLLA 492
Cdd:PRK15439 478 QGEISGALTGAAINVDTIMR 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-478 |
1.06e-89 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 283.16 E-value: 1.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQ 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 NINdgVVGALDVASNLVLDRLngAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVM 168
Cdd:PRK10982 81 ELN--LVLQRSVMDNMWLGRY--PTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQNLG 248
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 249 LHSID-ARAAGAPVFSARDLRIA--PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRT 325
Cdd:PRK10982 237 QRFPDkENKPGEVILEVRNLTSLrqPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 326 PASAIRDGVFLVAKDRASTGivpefnIYENMSLPFLPRFSNM----------SVTRRRAERQTAreqIADLKIVCRSERD 395
Cdd:PRK10982 317 ANEAINHGFALVTEERRSTG------IYAYLDIGFNSLISNIrnyknkvgllDNSRMKSDTQWV---IDSMRVKTPGHRT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 396 DLATLSGGNQQKVTVARW-LTQPsRLLILDEPFQGVDIAARHDIAAKLRESA-RDRATLVFLTELDEALETADRILVMSE 473
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWlLTQP-EILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITDRILVMSN 466
|
....*
gi 1998276353 474 NTIVG 478
Cdd:PRK10982 467 GLVAG 471
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-492 |
1.76e-83 |
|
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: 267.08 E-value: 1.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGV--HRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQ 88
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 NINdgVVGALDVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVM 168
Cdd:TIGR02633 86 ELT--LVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQNL- 247
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREIt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 248 GLHSIDARAAGAPVFSARDLR----IAPGAK---PLSMELGAGEVVAVTGLVGVGKTRLAETLFGIH-APLAGSMQLDGR 319
Cdd:TIGR02633 244 SLYPHEPHEIGDVILEARNLTcwdvINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 320 AYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLAT 399
Cdd:TIGR02633 324 PVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDR-ATLVFLTELDEALETADRILVMSENTIVG 478
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
490
....*....|....
gi 1998276353 479 EHRNADVDMDRLLA 492
Cdd:TIGR02633 484 DFVNHALTQEQVLA 497
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-491 |
7.47e-80 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 257.80 E-value: 7.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRA---DRGVMMLGD-RPFSPATPAEAmrA 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGEvCRFKDIRDSEA--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNIndGVVGALDVASNLVLDrlNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:NF040905 79 GIVIIHQEL--ALIPYLSIAENIFLG--NERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD--EKPLDYEGAV 239
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 240 NAMLGQNLglhsiDAR------AAGAPVFSARDLR----IAPGAKPL---SMELGAGEVVAVTGLVGVGKTRLAETLFG- 305
Cdd:NF040905 235 RGMVGRDL-----EDRypertpKIGEVVFEVKNWTvyhpLHPERKVVddvSLNVRRGEIVGIAGLMGAGRTELAMSVFGr 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 306 -----IhaplAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAR 380
Cdd:NF040905 310 sygrnI----SGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 381 EQIADLKIVCRSERDDLATLSGGNQQKVTVARWL-TQPSrLLILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLTEL 458
Cdd:NF040905 386 EYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLfTDPD-VLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSEL 464
|
490 500 510
....*....|....*....|....*....|...
gi 1998276353 459 DEALETADRILVMSENTIVGEHRNADVDMDRLL 491
Cdd:NF040905 465 PELLGMCDRIYVMNEGRITGELPREEASQERIM 497
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-227 |
8.73e-70 |
|
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: 219.99 E-value: 8.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTV 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQnindgvvgaldvasnlvldrlngagsgfffnprkvrrearevaermglgidlsaevtdLPLADRQMVAIARAMAHEPQ 166
Cdd:cd03216 81 YQ----------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
258-476 |
6.89e-65 |
|
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: 208.05 E-value: 6.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 258 GAPVFSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLV 337
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 338 AKDRASTGIVPEFNIYENMSLPFLprfsnmsvtrrraerqtareqiadlkivcrserddlatLSGGNQQKVTVARWLTQP 417
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 418 SRLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLTELDEALETADRILVMSENTI 476
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-477 |
2.11e-49 |
|
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: 177.02 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAF--GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRAD---RGVMMLGDRPFSPATPAEa 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRAGVVTVHQN----INDGVVGAlDVASNLVLDRLNgagsgfffnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQM 154
Cdd:COG1123 81 RGRRIGMVFQDpmtqLNPVTVGD-QIAEALENLGLS---------RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 155 VAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqfdekpl 233
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 234 dYEGAVNAMLGQNLGLHSI-----------DARAAGAPVFSARDLRIAPGAKP---------LSMELGAGEVVAVTGLVG 293
Cdd:COG1123 223 -EDGPPEEILAAPQALAAVprlgaargraaPAAAAAEPLLEVRNLSKRYPVRGkggvravddVSLTLRRGETLGLVGESG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 294 VGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAS--AIRDGVFLVAKDrASTGIVPEFNIYENMSLPFLprfsnmsvTR 371
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrELRRRVQMVFQD-PYSSLNPRMTVGDIIAEPLR--------LH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 372 RRAERQTAREQIADLKIVCRSERDDL----ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESAR 447
Cdd:COG1123 373 GLLSRAERRERVAELLERVGLPPDLAdrypHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQR 452
|
490 500 510
....*....|....*....|....*....|..
gi 1998276353 448 DR-ATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:COG1123 453 ELgLTYLFIShDLAVVRYIADRVAVMYDGRIV 484
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-230 |
3.07e-49 |
|
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: 169.15 E-value: 3.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVH 87
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNINdgVVGALDVASNLVLDRLNGAGSGFFFNP-----RKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMA 162
Cdd:cd03219 82 QIPR--LFPELTVLENVMVAAQARTGSGLLLARarreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV--GQFDE 230
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIaeGTPDE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-217 |
9.59e-48 |
|
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: 165.60 E-value: 9.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAG 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINdgVVGALDVASNLVLDRLNGAGSGFFFNP----------RKVRREAREVAERMGLGIDLSAEVTDLPLADR 152
Cdd:COG0411 81 IARTFQNPR--LFPELTVLENVLVAAHARLGRGLLAALlrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRA-RGVAILYISHRMSDIRRLADRIV 217
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIV 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-225 |
2.12e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGdrpFSPATPAEAMRA--GVV 84
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGeVRVLG---EDVARDPAEVRRriGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TvhQNinDGVVGALDVASNLVL-DRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAH 163
Cdd:COG1131 79 P--QE--PALYPDLTVRENLRFfARLYG------LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-227 |
1.07e-40 |
|
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: 145.94 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVGAL-- 98
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGLVFQNPDDQLFAPTve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 -DVA---SNLVLDRlngagsgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:COG1122 95 eDVAfgpENLGLPR------------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 175 SSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-222 |
8.14e-38 |
|
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: 137.60 E-value: 8.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVG 96
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGLVFQNPDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 AL---DVASNLvldRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEP 173
Cdd:cd03225 91 PTveeEVAFGL---ENLG------LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 174 TSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-232 |
8.36e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 8.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAF-GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRA 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNINdgVVGALDVASN-LV--LDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIA 158
Cdd:COG3638 81 RIGMIFQQFN--LVPRLSVLTNvLAgrLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqFDEKP 232
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVV--FDGPP 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-222 |
3.38e-37 |
|
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: 134.83 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGdrpFSPATPAEAMRAGVVTV 86
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGeIKVLG---KDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINdgvvgaldvasnlVLDRLNGagsgfffnprkvrreaREVaermglgIDLSaevtdlpLADRQMVAIARAMAHEPQ 166
Cdd:cd03230 79 PEEPS-------------LYENLTV----------------REN-------LKLS-------GGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-225 |
8.79e-36 |
|
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: 133.18 E-value: 8.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGV 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQniNDGVVGALDVASNLVLdrlnGAgsgfffnprKVRREAREVAERMglgidlsAEVTDL-P-LADR--------- 152
Cdd:COG0410 81 GYVPE--GRRIFPSLTVEENLLL----GA---------YARRDRAEVRADL-------ERVYELfPrLKERrrqragtls 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 153 ----QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG0410 139 ggeqQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-250 |
2.67e-35 |
|
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: 131.90 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfSPATPAEAMRA-GVVTV 86
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQiGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 hqniNDGVVGALDVASNLvldRLNGAGSGFFfnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQ 166
Cdd:COG4555 82 ----ERGLYDRLTVRENI---RYFAELYGLF--DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV-----GQFDEKPL--DYEGAV 239
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVaqgslDELREEIGeeNLEDAF 232
|
250
....*....|.
gi 1998276353 240 NAMLGQNLGLH 250
Cdd:COG4555 233 VALIGSEEGEA 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-225 |
4.47e-35 |
|
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: 130.63 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVH 87
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QniNDGVVGALDVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMG-LGIDLSAevtdlplADRQMVAIARAMAHEPQ 166
Cdd:cd03224 82 E--GRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKqLAGTLSG-------GEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
4.61e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 4.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaeamR 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNINDGV-VGALD-VASNLVldrlngAGSGFFFNPRKVRRE-AREVAERMGLgidlsaevtdLPLADRQM--- 154
Cdd:COG1121 77 IGYVPQRAEVDWDFpITVRDvVLMGRY------GRRGLFRRPSRADREaVDEALERVGL----------EDLADRPIgel 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 155 -------VAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:COG1121 141 sggqqqrVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-225 |
5.50e-35 |
|
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: 130.33 E-value: 5.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVV--- 84
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNIGMVfqd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 -------TVHQNIndgvvgaldvASNLVLDRLNGAgsgfffnprKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAI 157
Cdd:cd03259 81 yalfphlTVAENI----------AFGLKLRGVPKA---------EIRARVRELLELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-227 |
9.73e-35 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 130.55 E-value: 9.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVV 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQNINDGvvgaLDVASNLVLDRLngAGSGFFFNPRKV-RREAREVAERMGLgidlsaevtdLPLADR----------Q 153
Cdd:COG1120 81 PQEPPAPFG----LTVRELVALGRY--PHLGLFGRPSAEdREAVEEALERTGL----------EHLADRpvdelsggerQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 154 MVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-227 |
2.98e-34 |
|
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: 128.17 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAT-------PAEAmra 81
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 gvvtvhqnindGVVGALDVASNLV-LDRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARA 160
Cdd:cd03269 80 -----------GLYPKMKVIDQLVyLAQLKG------LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
3.53e-34 |
|
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: 128.94 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--A 78
Cdd:COG1127 1 MSEPMI-EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRA--GVV----------TVHQNindgvvgaldVAsnLVLDRLNGagsgffFNPRKVRREAREVAERMGLgidlsAEVTD 146
Cdd:COG1127 80 LRRriGMLfqggalfdslTVFEN----------VA--FPLREHTD------LSEAEIRELVLEKLELVGL-----PGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 LPLAD-----RQMVAIARAMAHEPQVMILDEPTSSL---SSNEaerLFALIDRLR-ARGVAILYISHRMSDIRRLADRIV 217
Cdd:COG1127 137 KMPSElsggmRKRVALARALALDPEILLYDEPTAGLdpiTSAV---IDELIRELRdELGLTSVVVTHDLDSAFAIADRVA 213
|
250
....*....|
gi 1998276353 218 SLRDGAIVGQ 227
Cdd:COG1127 214 VLADGKIIAE 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-227 |
4.49e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFG----PNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-- 77
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 78 AMRA---GVVtvHQNINdgVVGALDVASNLVL-DRLNGAgsgfffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADR 152
Cdd:COG1136 82 RLRRrhiGFV--FQFFN--LLPELTALENVALpLLLAGV-------SRKERRErARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMsDIRRLADRIVSLRDGAIVGQ 227
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-222 |
2.68e-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: 123.89 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAmRAGVVTVH 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QnindgvvgaldvasnlvldrlngagsgfffnprkvrrearevaermglgidLSAevtdlplADRQMVAIARAMAHEPQV 167
Cdd:cd00267 80 Q---------------------------------------------------LSG-------GQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 168 MILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-224 |
1.44e-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: 123.75 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNA----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRA 81
Cdd:cd03255 2 ELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 ---GVVtvHQNINdgVVGALDVASNLVL-DRLNGagsgfffNPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVA 156
Cdd:cd03255 82 rhiGFV--FQSFN--LLPDLTALENVELpLLLAG-------VPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 157 IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMsDIRRLADRIVSLRDGAI 224
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-233 |
2.54e-32 |
|
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: 123.76 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGP----NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGV 83
Cdd:COG1124 3 EVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK-AFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNindgvvgaldvasnlvldrlnGAGSgffFNPRK-----------------VRREAREVAERMGLGIDL----SA 142
Cdd:COG1124 82 QMVFQD---------------------PYAS---LHPRHtvdrilaeplrihglpdREERIAELLEQVGLPPSFldryPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 143 EVTDlplADRQMVAIARAMAHEPQVMILDEPTSSL-SSNEAERLfALIDRLRA-RGVAILYISHRMSDIRRLADRIVSLR 220
Cdd:COG1124 138 QLSG---GQRQRVAIARALILEPELLLLDEPTSALdVSVQAEIL-NLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQ 213
|
250
....*....|...
gi 1998276353 221 DGAIVGQFDEKPL 233
Cdd:COG1124 214 NGRIVEELTVADL 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-228 |
1.17e-31 |
|
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: 120.78 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGDRPFSPATPAEamRAGVVTV 86
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeITFDGKSYQKNIEALR--RIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQnindGVVGALDVASNLvldRLNGAGsgfffnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQ 166
Cdd:cd03268 80 AP----GFYPNLTARENL---RLLARL------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQF 228
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-225 |
1.50e-31 |
|
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: 127.33 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAF-----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE 77
Cdd:COG1123 257 AEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 78 --AMRAGVVTVHQNindgVVGALD--------VASNLvldRLNGAGSGfffnpRKVRREAREVAERMGlgidLSAEVTD- 146
Cdd:COG1123 337 lrELRRRVQMVFQD----PYSSLNprmtvgdiIAEPL---RLHGLLSR-----AERRERVAELLERVG----LPPDLADr 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 LPLA----DRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRD 221
Cdd:COG1123 401 YPHElsggQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYD 480
|
....
gi 1998276353 222 GAIV 225
Cdd:COG1123 481 GRIV 484
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-232 |
2.44e-31 |
|
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: 121.14 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRAGV 83
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINdgVVGALDVASNLV---LDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARA 160
Cdd:cd03256 81 GMIFQQFN--LIERLSVLENVLsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqFDEKP 232
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV--FDGPP 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-224 |
1.54e-30 |
|
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: 118.02 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRP-FSPATPAEAMRAGVVTVH 87
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKlTDDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNINdgVVGALDVASNLVLdrlngagsgfffNPRKVRREAREVAERmgLGIDLSAEVTDLPLAD----------RQMVAI 157
Cdd:cd03262 83 QQFN--LFPHLTVLENITL------------APIKVKGMSKAEAEE--RALELLEKVGLADKADaypaqlsggqQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-225 |
2.13e-30 |
|
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: 117.85 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNA----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAtPAEAMRA-G 82
Cdd:cd03266 3 TADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-PAEARRRlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVtvhqNINDGVVGALDVASNLV-LDRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:cd03266 82 FV----SDSTGLYDRLTARENLEyFAGLYG------LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-227 |
1.37e-29 |
|
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: 116.34 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG-VHRADRGVMMLGDRPFSPATPAEaMRA- 81
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWE-LRKr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 -GVVT--VHQNINDGVVgALDVasnlVLdrlngagSGFF---FNPRKV----RREAREVAERMGLGIDLSAEVTDLPLAD 151
Cdd:COG1119 80 iGLVSpaLQLRFPRDET-VLDV----VL-------SGFFdsiGLYREPtdeqRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 152 RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARG-VAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-227 |
3.65e-29 |
|
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: 114.91 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRAGVVT 85
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNindgvvGAL----DVASNLvldrlngagsGFF------FNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMV 155
Cdd:cd03261 82 LFQS------GALfdslTVFENV----------AFPlrehtrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-225 |
3.83e-29 |
|
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: 114.59 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG------VMMLGDRPFSPATPAEAMR 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegeVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNINdgvVGALDVASNLVL-DRLNGagsgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLAD------RQ 153
Cdd:cd03260 81 RRVGMVFQKPN---PFPGSIYDNVAYgLRLHG---------IKLKEELDERVEEALRKAALWDEVKDRLHALglsggqQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 154 MVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARgVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-225 |
9.07e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.59 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAT-------PAE---- 77
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEErgly 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 78 -AMRAGvvtvHQnindgvvgaldvasnLV-LDRLNGAgsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMV 155
Cdd:COG4152 84 pKMKVG----EQ---------------LVyLARLKGL------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-225 |
9.75e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 113.55 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFS-PATPAEAMRAGVV 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQNINdgvvgaL----DVASNLVLDrlngagsgfffnPRKVRR----EAREVA----ERMGLgidlsaevtdlplADR 152
Cdd:COG1126 81 MVFQQFN------LfphlTVLENVTLA------------PIKVKKmskaEAEERAmellERVGL-------------ADK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 -------------QMVAIARAMAHEPQVMILDEPTSSLS-SNEAERLfALIDRLRARGVAILYISHRMSDIRRLADRIVS 218
Cdd:COG1126 130 adaypaqlsggqqQRVAIARALAMEPKVMLFDEPTSALDpELVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVF 208
|
....*..
gi 1998276353 219 LRDGAIV 225
Cdd:COG1126 209 MDGGRIV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-219 |
2.04e-28 |
|
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: 112.24 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfspatpAEAMRAGVVTVH 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNIN---DGVVGALDVasnlVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGidlsaEVTDLPLAD-----RQMVAIAR 159
Cdd:cd03235 75 QRRSidrDFPISVRDV----VLMGLYGHKGLFRRLSKADKAKVDEALERVGLS-----ELADRQIGElsggqQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSL 219
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-223 |
2.34e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.80 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfsPATPAEAMRAGVV 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TV-HQninDGVVGALDVASNLVLDRLngagsgfFFNPRKVRREAREVAERMGLgidlsAEVTDLPLAD-----RQMVAIA 158
Cdd:COG4133 79 YLgHA---DGLKPELTVRENLRFWAA-------LYGLRADREAIDEALEAVGL-----AGLADLPVRQlsagqKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHrmSDIRRLADRIVSLRDGA 223
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-227 |
2.58e-28 |
|
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: 110.60 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAgVVTVH 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QnindgvvgaldvasnlVLDRLNgagsgfffnprkvrreAREVAERmglgidlsaEVTDLPLADRQMVAIARAMAHEPQV 167
Cdd:cd03214 80 Q----------------ALELLG----------------LAHLADR---------PFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 168 MILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-222 |
2.88e-28 |
|
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: 110.74 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPF-SPATPAEAMRAGVVT 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNINdgVVGALDVASNLVLdRLNGAgsgfffnprkvrrearevaermglgidlsaevtdlplaDRQMVAIARAMAHEP 165
Cdd:cd03229 81 VFQDFA--LFPHLTVLENIAL-GLSGG--------------------------------------QQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 166 QVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-274 |
2.19e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.88 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEamR 80
Cdd:COG3842 1 MAMPAL-ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNindgvvGAL----DVASN----LVLDRLngagsgfffnPRKVRRE-AREVAERMGLGidlsaevtdlPLAD 151
Cdd:COG3842 77 RNVGMVFQD------YALfphlTVAENvafgLRMRGV----------PKAEIRArVAELLELVGLE----------GLAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 152 R----------QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLR 220
Cdd:COG3842 131 RyphqlsggqqQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMN 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 221 DGAIVgQFDEkPLD-YE-----------GAVNAMLGQNLGLHSIDARAAGAPVFSARDLRIAPGAK 274
Cdd:COG3842 211 DGRIE-QVGT-PEEiYErpatrfvadfiGEANLLPGTVLGDEGGGVRTGGRTLEVPADAGLAAGGP 274
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-230 |
2.33e-27 |
|
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: 116.09 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 20 AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNIN--DGvvga 97
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIGVVLQDVFlfSG---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 lDVASNLVLDRLNgagsgffFNPRKVRREAR-----EVAERMGLGID--LSAEVTDLPLADRQMVAIARAMAHEPQVMIL 170
Cdd:COG2274 564 -TIRENITLGDPD-------ATDEEIIEAARlaglhDFIEALPMGYDtvVGEGGSNLSGGQRQRLAIARALLRNPRILIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 171 DEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIrRLADRIVSLRDGAIV--GQFDE 230
Cdd:COG2274 636 DEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVedGTHEE 695
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-224 |
2.85e-27 |
|
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: 107.90 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAfgpnAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVV 84
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQN-INDGVVGALDVASNLVLDRLngagsgfffnprkvrrearevaermglgidLSAevtdlplADRQMVAIARAMAH 163
Cdd:cd03215 79 YVPEDrKREGLVLDLSVAENIALSSL------------------------------LSG-------GNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-222 |
3.48e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.08 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVT 85
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNI----NDGVVGALDVASNLVLDrlNGAGSGFFFNP--RKVRREAREVA----ERMGLGIDLSAEVTDLPLADRQMV 155
Cdd:PRK11300 85 TFQHVrlfrEMTVIENLLVAQHQQLK--TGLFSGLLKTPafRRAESEALDRAatwlERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-222 |
6.51e-27 |
|
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: 107.98 E-value: 6.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFG--PNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfspatpaeaMRAGVVT 85
Cdd:cd03263 2 QIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS---------IRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNI-----NDGVVGALDVASNLVL-DRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIAR 159
Cdd:cd03263 73 ARQSLgycpqFDALFDELTVREHLRFyARLKG------LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-225 |
6.58e-27 |
|
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: 108.06 E-value: 6.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 18 PNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQ--------- 88
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQdvtlfygtl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 --NINdgvVGALDVASNLVLDRLNGAGSGFFFNpRKVRREAREVAERmglGIDLSAevtdlplADRQMVAIARAMAHEPQ 166
Cdd:cd03245 95 rdNIT---LGAPLADDERILRAAELAGVTDFVN-KHPNGLDLQIGER---GRGLSG-------GQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 167 VMILDEPTSSLSSNEAERlfaLIDRLRA--RGVAILYISHRMSdIRRLADRIVSLRDGAIV 225
Cdd:cd03245 161 ILLLDEPTSAMDMNSEER---LKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-225 |
7.14e-27 |
|
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: 107.73 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGV---- 83
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVfqny 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 -----VTVHQNIndgvvgaldvASNLVLDRlngagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIA 158
Cdd:cd03301 82 alyphMTVYDNI----------AFGLKLRK---------VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-225 |
1.20e-26 |
|
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: 106.96 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNA-VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAtpaeaMRAGVVT- 85
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK-----ERRKSIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNINDGVVGAlDVASNLVLdrlnGAGsgfffNPRKVRREAREVAERMglgiDLSAEVTDLPLA----DRQMVAIARAM 161
Cdd:cd03226 76 VMQDVDYQLFTD-SVREELLL----GLK-----ELDAGNEQAETVLKDL----DLYALKERHPLSlsggQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-477 |
1.42e-26 |
|
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: 107.13 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRastGIVPEFNIYEN 355
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPflprfsnmSVTRRRAERQTAREQIADLKIVCRSERDDLA-TLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAA 434
Cdd:cd03224 96 LLLG--------AYARRRAKRKARLERVYELFPRLKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1998276353 435 RHDIAAKLREsARDRATLVFLTE--LDEALETADRILVMSENTIV 477
Cdd:cd03224 168 VEEIFEAIRE-LRDEGVTILLVEqnARFALEIADRAYVLERGRVV 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-175 |
1.53e-26 |
|
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: 105.04 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPaTPAEAMRAGVVTVHQniNDGVVGALDVA 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQ--DPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 102 SNLVLdrlngAGSGFFFNPRKVRREAREVAERMGLGiDLSAEVTDLPLAD-----RQMVAIARAMAHEPQVMILDEPTS 175
Cdd:pfam00005 78 ENLRL-----GLLLKGLSKREKDARAEEALEKLGLG-DLADRPVGERPGTlsggqRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-225 |
2.02e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMR--AG 82
Cdd:COG2884 3 RFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipYLRrrIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VV----------TVHQNindgvvgaldVAsnLVLdRLNGAgsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADR 152
Cdd:COG2884 83 VVfqdfrllpdrTVYEN----------VA--LPL-RVTGK------SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-227 |
4.33e-26 |
|
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: 111.77 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 20 AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGVVTVHQNindGVVGALD 99
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA-SWRRQIAWVPQN---PYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASNLVLdrlngagsgffFNPRKVRREAREVAERMGLgidlSAEVTDLP------LAD---------RQMVAIARAMAHE 164
Cdd:COG4988 427 IRENLRL-----------GRPDASDEELEAALEAAGL----DEFVAALPdgldtpLGEggrglsggqAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-265 |
4.48e-26 |
|
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: 109.03 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRP-FSPAT----PAEAMRAGVV----------TVHQN 89
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARgiflPPHRRRIGYVfqearlfphlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 90 INDGVvgaldvasnlvldrlngagsgfFFNPRKVRREAR-EVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVM 168
Cdd:COG4148 98 LLYGR----------------------KRAPRAERRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQfdekpldyeGAVNAMLGQNL 247
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS---------GPLAEVLSRPD 226
|
250
....*....|....*...
gi 1998276353 248 GLHSIDARAAGApVFSAR 265
Cdd:COG4148 227 LLPLAGGEEAGS-VLEAT 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-222 |
5.69e-26 |
|
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: 104.00 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNIndgvvg 96
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES-LRKNIAYVPQDP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 aldvasnlvldrlngagsgFFFNprkvrreaREVAERMglgidLSA-EvtdlpladRQMVAIARAMAHEPQVMILDEPTS 175
Cdd:cd03228 86 -------------------FLFS--------GTIRENI-----LSGgQ--------RQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 176 SLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDG 222
Cdd:cd03228 126 ALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-225 |
6.40e-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: 105.67 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPA--EAM 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGVVTVHQNINdgvvGALD----VASnLVLDRLNGAGSgfffNPRKVRREAREVAERMGLGidLSAEVTD-----LPLA 150
Cdd:cd03257 81 RKEIQMVFQDPM----SSLNprmtIGE-QIAEPLRIHGK----LSKKEARKEAVLLLLVGVG--LPEEVLNrypheLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 151 DRQMVAIARAMAHEPQVMILDEPTSSL-SSNEAERLfALIDRLRA-RGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALdVSVQAQIL-DLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-227 |
1.97e-25 |
|
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: 103.91 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 32 GEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPF-----SPATPAEAMRAGVvtVHQNIndGVVGALDVASNLVL 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkKINLPPQQRKIGL--VFQQY--ALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 107 drlngagsGFFFNPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERL 185
Cdd:cd03297 99 --------GLKRKRNREDRIsVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1998276353 186 FALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-229 |
2.50e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 106.70 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE---AMragvV 84
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniAM----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ----------TVHQNIndgvvgaldvASNLvldRLNGagsgffFNPRKVRREAREVAERMGLGidlsaevtdlPLADR-- 152
Cdd:COG3839 81 fqsyalyphmTVYENI----------AFPL---KLRK------VPKAEIDRRVREAAELLGLE----------DLLDRkp 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 --------QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGA 223
Cdd:COG3839 132 kqlsggqrQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
....*.
gi 1998276353 224 IVgQFD 229
Cdd:COG3839 212 IQ-QVG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
259-500 |
2.62e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 259 APVFSARDLRIA-PGAKPL---SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGV 334
Cdd:COG1129 2 EPLLEMRGISKSfGGVKALdgvSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 335 FLVAKDRAstgIVPEFNIYENMSLPFLPRfsNMSVTRRRAERQTAREQIADLKIVCrSERDDLATLSGGNQQKVTVARWL 414
Cdd:COG1129 82 AIIHQELN---LVPNLSVAENIFLGREPR--RGGLIDWRAMRRRARELLARLGLDI-DPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 415 TQPSRLLILDEP---FQGVDIAARHDIAAKLREsarDRATLVFLT-ELDEALETADRILVMSENTIVGEHRNADVDMDRL 490
Cdd:COG1129 156 SRDARVLILDEPtasLTEREVERLFRIIRRLKA---QGVAIIYIShRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDEL 232
|
250
....*....|
gi 1998276353 491 LAEVAGQRLE 500
Cdd:COG1129 233 VRLMVGRELE 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-227 |
2.80e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVV-- 84
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAVLpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 --------TVHQnindgVVGaldvasnlvLDRLNGAGSgfffnPRKVRREAREVAERMGLgidlsaevtdLPLADR---- 152
Cdd:COG4559 83 hsslafpfTVEE-----VVA---------LGRAPHGSS-----AAQDRQIVREALALVGL----------AHLAGRsyqt 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 ------QMVAIARAMA-------HEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHrmsDI---RRLADRI 216
Cdd:COG4559 134 lsggeqQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH---DLnlaAQYADRI 210
|
250
....*....|.
gi 1998276353 217 VSLRDGAIVGQ 227
Cdd:COG4559 211 LLLHQGRLVAQ 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
8.05e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 103.25 E-value: 8.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIF-RIAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATP 75
Cdd:COG1116 1 MSAAAPAlELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 76 aeamRAGVV----------TVHQNIndgvvgALDVasnlvldRLNGAgsgfffnPRKVRRE-AREVAERMGLGidlsaev 144
Cdd:COG1116 81 ----DRGVVfqepallpwlTVLDNV------ALGL-------ELRGV-------PKAERRErARELLELVGLA------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 145 tdlPLAD----------RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHrmsDIR--- 210
Cdd:COG1116 130 ---GFEDayphqlsggmRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTH---DVDeav 203
|
250 260
....*....|....*....|.
gi 1998276353 211 RLADRIV--SLRDGAIVGQFD 229
Cdd:COG1116 204 FLADRVVvlSARPGRIVEEID 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-225 |
8.38e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.60 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVH 87
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNinDGVVGALDVASNL--VLDRLNGAGsgfffnpRKVRREA-------REVAERMGlGiDLSAevtdlplADRQMVAIA 158
Cdd:TIGR03410 82 QG--REIFPRLTVEENLltGLAALPRRS-------RKIPDEIyelfpvlKEMLGRRG-G-DLSG-------GQQQQLAIA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-229 |
3.45e-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: 100.62 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNA----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaeamRAGV 83
Cdd:cd03293 2 EVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 V----------TVHQNIndgvvgALDVasnlvldRLNGAGsgfffnPRKVRREAREVAERMGLG-------IDLSAEVtd 146
Cdd:cd03293 78 VfqqdallpwlTVLDNV------ALGL-------ELQGVP------KAEARERAEELLELVGLSgfenaypHQLSGGM-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 lpladRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSL--RDGA 223
Cdd:cd03293 137 -----RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGR 211
|
....*.
gi 1998276353 224 IVGQFD 229
Cdd:cd03293 212 IVAEVE 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
261-500 |
4.21e-24 |
|
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: 101.27 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 261 VFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASAIRdgvfl 336
Cdd:COG1120 1 MLEAENLSVGYGGRPvlddVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR------DLASLS----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 337 vAKDRAST-GIVP-EFNIYENMS---------LPFLPRFSNMSVT-RRRAERQTAREQIADLKivcrsERDdLATLSGGN 404
Cdd:COG1120 70 -RRELARRiAYVPqEPPAPFGLTvrelvalgrYPHLGLFGRPSAEdREAVEEALERTGLEHLA-----DRP-VDELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 405 QQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT--ELDEALETADRILVMSENTIVGEHRN 482
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVlhDLNLAARYADRLVLLKDGRIVAQGPP 222
|
250
....*....|....*...
gi 1998276353 483 ADVDMDRLLAEVAGQRLE 500
Cdd:COG1120 223 EEVLTPELLEEVYGVEAR 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-225 |
4.33e-24 |
|
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: 100.49 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGpNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMRAGVV---- 84
Cdd:cd03299 3 VENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDISYVpqny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ------TVHQNINDGVvgaldvaSNLVLDRLNgagsgfffnprkVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIA 158
Cdd:cd03299 81 alfphmTVYKNIAYGL-------KKRKVDKKE------------IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-229 |
5.18e-24 |
|
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: 100.35 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNA----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AM 79
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGVVTVHQNINdgVVGALDVASNLVLDrLNGAGSgfffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIA 158
Cdd:cd03258 81 RRRIGMIFQHFN--LLSSRTVFENVALP-LEIAGV-----PKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD 229
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-223 |
6.01e-24 |
|
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: 100.20 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFG---------PnaVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLgDRPFSP-- 72
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqggkrlP--VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-RHDGGWvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 73 ---ATPAE--AMRAGVVT-VHQNINdgV---VGALDVASNLVLDRlnGAGsgfffnprkvRREAREVAERMGLGIDLSAE 143
Cdd:COG4778 79 laqASPREilALRRRTIGyVSQFLR--ViprVSALDVVAEPLLER--GVD----------REEARARARELLARLNLPER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 144 VTDLPLA-----DRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVS 218
Cdd:COG4778 145 LWDLPPAtfsggEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVD 224
|
....*
gi 1998276353 219 LRDGA 223
Cdd:COG4778 225 VTPFS 229
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
9-227 |
7.88e-24 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 100.06 E-value: 7.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVtVHQ 88
Cdd:TIGR03864 4 VAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV-FQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 NINDGvvgALDVASNLVLDR-LNGAGSgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQV 167
Cdd:TIGR03864 83 PTLDL---DLSVRQNLRYHAaLHGLSR------AEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 168 MILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:TIGR03864 154 LLLDEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLAD 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
257-500 |
3.67e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.24 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 257 AGAPVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasaird 332
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPvledVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 333 gvflVAKDRASTGIVP-EFNIyeNMSLPF-------LPRFSNMSVTRR--RAERQTAREQIADLKIvcrserDDLA---- 398
Cdd:COG1121 70 ----PRRARRRIGYVPqRAEV--DWDFPItvrdvvlMGRYGRRGLFRRpsRADREAVDEALERVGL------EDLAdrpi 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 399 -TLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSeNTI 476
Cdd:COG1121 138 gELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVThDLGAVREYFDRVLLLN-RGL 216
|
250 260
....*....|....*....|....
gi 1998276353 477 VGEHRNADVDMDRLLAEVAGQRLE 500
Cdd:COG1121 217 VAHGPPEEVLTPENLSRAYGGPVA 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-227 |
3.88e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVV-- 84
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAVLpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 --------TVHQnindgVVGaldvasnlvLDRLNGAGSgfffnPRKVRREAREVAERMGLgidlsaevtdLPLADR---- 152
Cdd:PRK13548 84 hsslsfpfTVEE-----VVA---------MGRAPHGLS-----RAEDDALVAAALAQVDL----------AHLAGRdypq 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 ------QMVAIARAMA------HEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSL 219
Cdd:PRK13548 135 lsggeqQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLL 214
|
....*...
gi 1998276353 220 RDGAIVGQ 227
Cdd:PRK13548 215 HQGRLVAD 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-225 |
7.65e-23 |
|
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: 97.02 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGDRPFSpATPAEAMRAGVVTVHQNindgvvgalD 99
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGeVRVAGLVPWK-RRKKFLRRIGVVFGQKT---------Q 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASNL-VLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLS 178
Cdd:cd03267 106 LWWDLpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 179 SNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03267 186 VVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-231 |
1.44e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.68 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVV--- 84
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVfqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 -------TVHQNINDGvvgaLDVASNlvldrlngagsgfffNPRKVRREAREVAERMGLGidlsaevtdlPLADR----- 152
Cdd:COG1118 84 yalfphmTVAENIAFG----LRVRPP---------------SKAEIRARVEELLELVQLE----------GLADRypsql 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 -----QMVAIARAMAHEPQVMILDEPTSSLSS---NEAER-LFALIDRLrarGVAILYISHRMSDIRRLADRIVSLRDGA 223
Cdd:COG1118 135 sggqrQRVALARALAVEPEVLLLDEPFGALDAkvrKELRRwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGR 211
|
....*...
gi 1998276353 224 IVgQFDEK 231
Cdd:COG1118 212 IE-QVGTP 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-227 |
2.76e-22 |
|
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: 100.23 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQN--INDGv 94
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDEDDLRRRIAVVPQRphLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 95 vgalDVASNLVLdrlngagsgffFNPRKVRREAREVAERMGLGiDLSAEVT---DLPLAD---------RQMVAIARAMA 162
Cdd:COG4987 424 ----TLRENLRL-----------ARPDATDEELWAALERVGLG-DWLAALPdglDTWLGEggrrlsggeRRRLALARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQ 550
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-227 |
3.41e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 99.85 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMRAGVVTVHQninDGVVGALDV 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL-ESLRRQIGVVPQ---DTFLFSGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNgagsgffFNPRKVRREAR-----EVAERM--GL-------GIDLSA-EvtdlpladRQMVAIARAMAHEP 165
Cdd:COG1132 431 RENIRYGRPD-------ATDEEVEEAAKaaqahEFIEALpdGYdtvvgerGVNLSGgQ--------RQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 166 QVMILDEPTSSL-SSNEAeRLFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:COG1132 496 PILILDEATSALdTETEA-LIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
274-494 |
3.75e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.13 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGraYAPRTPASAIRdgvflvakdrASTGIVPE-FNI 352
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG--EDVARDPAEVR----------RRIGYVPQePAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMS----LPFLPRFSNMS--VTRRRAERQTAREQIADLkivcrseRDDLA-TLSGGNQQKVTVAR-WLTQPsRLLILD 424
Cdd:COG1131 85 YPDLTvrenLRFFARLYGLPrkEARERIDELLELFGLTDA-------ADRKVgTLSGGMKQRLGLALaLLHDP-ELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRATlVFLT--ELDEALETADRILVMSENTIVgehrnADVDMDRLLAEV 494
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKT-VLLSthYLEEAERLCDRVAIIDKGRIV-----ADGTPDELKARL 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
276-479 |
5.06e-22 |
|
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: 94.66 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRastGIVPEFNIYEN 355
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPFLPRfsnmsvtRRRAERQTAREQIADLKIVCRSERDDLA-TLSGGNQQKVTVARWL-TQPsRLLILDEPFQGVDIA 433
Cdd:COG0410 99 LLLGAYAR-------RDRAEVRADLERVYELFPRLKERRRQRAgTLSGGEQQMLAIGRALmSRP-KLLLLDEPSLGLAPL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 434 ARHDIAAKLREsARDRATLVFLTE--LDEALETADRILVMSENTIVGE 479
Cdd:COG0410 171 IVEEIFEIIRR-LNREGVTILLVEqnARFALEIADRAYVLERGRIVLE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-248 |
1.09e-21 |
|
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: 93.94 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfspATPAEAMRAGVVTVH 87
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED---ATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNIndGVVGALDVASNLVLdrlngagsGFFFNPRKVRREAREVAERM----------GLGIDLSAEvtdLPLADRQMVAI 157
Cdd:cd03296 81 QHY--ALFRHMTVFDNVAF--------GLRVKPRSERPPEAEIRAKVhellklvqldWLADRYPAQ---LSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAI--VGQFDEKpld 234
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIeqVGTPDEV--- 224
|
250
....*....|....
gi 1998276353 235 YEGAVNAMLGQNLG 248
Cdd:cd03296 225 YDHPASPFVYSFLG 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-248 |
2.24e-21 |
|
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: 92.69 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeamRAGVVTVH 87
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNIndGVVGALDVASNLvldrlngagsGFFFNPRKVRRE--AREVAERMGLgIDLSA----EVTDLPLADRQMVAIARAM 161
Cdd:cd03300 79 QNY--ALFPHLTVFENI----------AFGLRLKKLPKAeiKERVAEALDL-VQLEGyanrKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVgQFDeKPLD-YEGAV 239
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ-QIG-TPEEiYEEPA 223
|
....*....
gi 1998276353 240 NAMLGQNLG 248
Cdd:cd03300 224 NRFVADFIG 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-230 |
2.59e-21 |
|
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: 92.67 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQninDGVVGALDV 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQ---DTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNGagsgfffNPRKVRREAREVA-----ERMGLGID--LSAEVTDLPLADRQMVAIARAMAHEPQVMILDEP 173
Cdd:cd03254 94 MENIRLGRPNA-------TDEEVIEAAKEAGahdfiMKLPNGYDtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 174 TSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIV--GQFDE 230
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIeeGTHDE 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-227 |
2.63e-21 |
|
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: 92.17 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 31 AGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEamrAGVVTVHQNINdgVVGALDVASNLVLdrln 110
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENN--LFAHLTVEQNVGL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 111 GAGSGFFFNPrkVRREAREVA-ERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALI 189
Cdd:cd03298 94 GLSPGLKLTA--EDRQAIEVAlARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1998276353 190 DRLRA-RGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:cd03298 172 LDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-225 |
3.33e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGP-----NAVLRGVGLDLRAGE-VTVLmGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpaTPAEAMRA 81
Cdd:COG1101 3 ELKNLSKTFNPgtvneKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVV-TVHQNINDGVVGALDVASNLVLDRLNGAGSGFFF-NPRKVRREAREVAERMGLGID--LSAEVTDLPLADRQmvAI 157
Cdd:COG1101 80 KYIgRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRgLTKKRRELFRELLATLGLGLEnrLDTKVGLLSGGQRQ--AL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 158 ARAMA--HEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG1101 158 SLLMAtlTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-225 |
5.47e-21 |
|
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: 95.97 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMR------------AGvv 84
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigylpqdvelfDG-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQNIndgvvgaldvAsnlvldRLNGAgsgfffNPRKVRREAR-----EVAERMGLGID---------LSAevtdlplA 150
Cdd:COG4618 421 TIAENI----------A------RFGDA------DPEKVVAAAKlagvhEMILRLPDGYDtrigeggarLSG-------G 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 151 DRQMVAIARAMAHEPQVMILDEPTSSLSSnEAER-LFALIDRLRARGVAILYISHRMSdIRRLADRIVSLRDGAIV 225
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-224 |
7.20e-21 |
|
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: 89.58 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTkafgpNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTV 86
Cdd:cd03246 8 FRYPGAE-----PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE-LGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNIN--DGvvgalDVASNLVldrlngagSGfffnprkvrrearevaermglgidlsaevtdlplADRQMVAIARAMAHE 164
Cdd:cd03246 82 PQDDElfSG-----SIAENIL--------SG----------------------------------GQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRlADRIVSLRDGAI 224
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-233 |
9.69e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGD------RPFSPATPA-EAMRA 81
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKGLiRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNINdgVVGALDVASNLVLdrlngagsgfffNPRKVRREAREVAE--------RMGLGIDLSAEVTDLPLADRQ 153
Cdd:PRK11264 86 HVGFVFQNFN--LFPHRTVLENIIE------------GPVIVKGEPKEEATararellaKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 154 MVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPL 233
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-224 |
9.83e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.31 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 13 TKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDrpFSPATPAEAMR-----AGVVTVH 87
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERlirqeAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNINDGVVGALDVAsnlvldrlngagsgffFNPRKVRREAREVAERMGLgiDLSAEVTdlpLADR-------------QM 154
Cdd:PRK09493 86 FYLFPHLTALENVM----------------FGPLRVRGASKEEAEKQAR--ELLAKVG---LAERahhypselsggqqQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 155 VAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-225 |
1.56e-20 |
|
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: 89.94 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGeVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRpfSPATPAEAMRAGV----- 83
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIgylpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 -VTVHQNINdgVVGALDVASnlvldRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMA 162
Cdd:cd03264 80 eFGVYPNFT--VREFLDYIA-----WLKG------IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYiSHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
274-473 |
1.73e-20 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 89.83 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsAIRDGVFLVAKDrastgivPE---F 350
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK-ELRRKVGLVFQN-------PDdqfF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 N--IYENMSlpFLPRfsNMSVTRRRAERqTAREQIADLKIVCRSERDdLATLSGGNQQKVTVARWLTQPSRLLILDEPFQ 428
Cdd:cd03225 90 GptVEEEVA--FGLE--NLGLPEEEIEE-RVEEALELVGLEGLRDRS-PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 429 GVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSE 473
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVThDLDLLLELADRVIVLED 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-225 |
1.74e-20 |
|
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: 90.12 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDrpFSPATPAEAMRAGVVTVHQNI 90
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 NdgVVGALDVASNLVLD-RLNGAgsgfffnPRKVRRE-AREVAERMGLGidlsaEVTDLPLAD-----RQMVAIARAMAH 163
Cdd:cd03265 83 S--VDDELTGWENLYIHaRLYGV-------PGAERRErIDELLDFVGLL-----EAADRLVKTysggmRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-219 |
1.78e-20 |
|
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: 94.28 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAF-GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGVVTV 86
Cdd:TIGR02857 323 EFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNindGVVGALDVASNLVLDRLNGAGSgfffnprkvrrEAREVAERMGLGIDLSA--EVTDLPLAD---------RQMV 155
Cdd:TIGR02857 402 PQH---PFLFAGTIAENIRLARPDASDA-----------EIREALERAGLDEFVAAlpQGLDTPIGEggaglsggqAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRlADRIVSL 219
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
274-477 |
1.90e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 89.50 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsaiRDGVFLVAKDRAstgIVPEFNIY 353
Cdd:cd03259 17 DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMVFQDYA---LFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLPRFSNMSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVRELLELVGLEGL------LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 434 ARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03259 165 LREELREELKELQRElGITTIYVThDQEEALALADRIAVMNEGRIV 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-225 |
2.81e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 91.68 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRA-- 81
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE-LRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 ---GVV----------TVHQNIndgvvgaldvASNLvldRLNGAgsgfffnPRKVRRE-AREVAERMGLgidlsaevtdl 147
Cdd:COG1135 82 rkiGMIfqhfnllssrTVAENV----------ALPL---EIAGV-------PKAEIRKrVAELLELVGL----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 148 plADR-------------QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLA 213
Cdd:COG1135 131 --SDKadaypsqlsggqkQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRIC 208
|
250
....*....|..
gi 1998276353 214 DRIVSLRDGAIV 225
Cdd:COG1135 209 DRVAVLENGRIV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-248 |
4.91e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.76 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQN-INDGVVGALDV 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNgagsgfFFNPRKVRreAREVAERMGLG--IDL------SAE--VTDLPLADRQMVAIARAMAHEPQVMIL 170
Cdd:PRK10762 348 KENMSLTALR------YFSRAGGS--LKHADEQQAVSdfIRLfniktpSMEqaIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 171 DEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQNLG 248
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAVGKLNR 497
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
5.82e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVM---MLGDRPFSPATPAE 77
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 78 A-----MRAGVVTVHQNINDGVVGALDVASNlVLDRLNGAGSGFFFNprkVRREAREVAERMglGIDLsAEVTDLPLA-- 150
Cdd:PRK11701 81 AerrrlLRTEWGFVHQHPRDGLRMQVSAGGN-IGERLMAVGARHYGD---IRATAGDWLERV--EIDA-ARIDDLPTTfs 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 151 --DRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK11701 154 ggMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-229 |
6.66e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFS-PATPAE----AMRAG 82
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEkairLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINdgVVGALDVASNLVLDRLNGAGsgffFNPRKVRREAREVAERmgLGIDLSAEVTDLPLA--DRQMVAIARA 160
Cdd:COG4161 84 VGMVFQQYN--LWPHLTVMENLIEAPCKVLG----LSKEQAREKAMKLLAR--LRLTDKADRFPLHLSggQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD 229
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
274-476 |
6.73e-20 |
|
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: 87.07 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASairdgvflvakdRASTGIVPE-FNI 352
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV------------KRRIGYLPEePSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMslpflprfsnmsvtrrraerqTAREQIadlkivcrserddlaTLSGGNQQKVTVARWL-TQPsRLLILDEPFQGVD 431
Cdd:cd03230 85 YENL---------------------TVRENL---------------KLSGGMKQRLALAQALlHDP-ELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 432 IAARHDIAAKLRESARDRATlVFLT--ELDEALETADRILVMSENTI 476
Cdd:cd03230 128 PESRREFWELLRELKKEGKT-ILLSshILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
266-471 |
7.30e-20 |
|
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: 87.97 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 266 DLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasairdgvflVAKDR 341
Cdd:cd03235 4 DLTVSYGGHPvledVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP----------------LEKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 342 ASTGIVP-------EFNI--YENMSLPFLPRfSNMSVTRRRAERQTAREQIADLKIVCRSERDdLATLSGGNQQKVTVAR 412
Cdd:cd03235 68 KRIGYVPqrrsidrDFPIsvRDVVLMGLYGH-KGLFRRLSKADKAKVDEALERVGLSELADRQ-IGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 413 WLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVM 471
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVThDLGLVLEYFDRVLLL 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
9.83e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMR 80
Cdd:PRK13536 37 MSTVAI-DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNINDgvvgALDVASNLVLdrlngAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARA 160
Cdd:PRK13536 116 IGVVPQFDNLDL----EFTVRENLLV-----FGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-225 |
1.31e-19 |
|
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: 87.87 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNA----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAT--PAE 77
Cdd:COG4181 6 APIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 78 AMRAGVVtvhqnindGVV----------GALD-VASNLVLDRLNGAgsgfffnprkvRREAREVAERMGLGIDLSAEVTD 146
Cdd:COG4181 86 RLRARHV--------GFVfqsfqllptlTALEnVMLPLELAGRRDA-----------RARARALLERVGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
274-473 |
1.46e-19 |
|
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: 85.37 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPaSAIRDGVflvakdrastGIVPEfniy 353
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRI----------GYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 enmslpflprfsnmsvtrrraerqtareqiadlkivcrserddlatLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 434 ARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSE 473
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVThDPELAELAADRVIVLKD 155
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-224 |
1.52e-19 |
|
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: 87.53 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFsPATPAEAMRAGVVTVHQ-------NINDG 93
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLHSKVSLVGQepvlfarSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 94 VV-GALDVASNLVLDRLNGAGSGFFFnPRKVRREAREVAERmglGIDLSAevtdlplADRQMVAIARAMAHEPQVMILDE 172
Cdd:cd03248 108 IAyGLQSCSFECVKEAAQKAHAHSFI-SELASGYDTEVGEK---GSQLSG-------GQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 173 PTSSLSSNEAERLF-ALIDRLRARGVaiLYISHRMSDIRRlADRIVSLRDGAI 224
Cdd:cd03248 177 ATSALDAESEQQVQqALYDWPERRTV--LVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-227 |
2.01e-19 |
|
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: 87.29 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 18 PNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA-GVV---------TVH 87
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQiGLVsqdvflfndTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNINDGVVGALDVAsnlVLDRLNGAgsgfffnprkvrrEAREVAERMGLGIDLSAEVTDLPLA--DRQMVAIARAMAHEP 165
Cdd:cd03251 94 ENIAYGRPGATREE---VEEAARAA-------------NAHEFIMELPEGYDTVIGERGVKLSggQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 166 QVMILDEPTSSLsSNEAERLF-ALIDRLRARGVAILyISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:cd03251 158 PILILDEATSAL-DTESERLVqAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVER 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-225 |
2.07e-19 |
|
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: 91.32 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 20 AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNI---NDgvvg 96
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQVALVSQDVvlfND---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 alDVASNLVLDRLNGAGSGfffnprKVRREAR-----EVAERMGLGIDLSAEVTDLPLA--DRQMVAIARAMAHEPQVMI 169
Cdd:TIGR02203 421 --TIANNIAYGRTEQADRA------EIERALAaayaqDFVDKLPLGLDTPIGENGVLLSggQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 170 LDEPTSSLsSNEAERLF-ALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:TIGR02203 493 LDEATSAL-DNESERLVqAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-225 |
2.19e-19 |
|
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: 88.08 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 14 KAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRA------GVV--- 84
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRElrrkkiSMVfqs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ---TVHQNINDGVVGALDVASNlvldrlngagsgfffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARA 160
Cdd:cd03294 111 falLPHRTVLENVAFGLEVQGV----------------PRAEREErAAEALELVGLEGWEHKYPDELSGGMQQRVGLARA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 161 MAHEPQVMILDEPTSSLS----SNEAERLFALIDRLRArgvAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03294 175 LAVDPDILLMDEAFSALDplirREMQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
263-477 |
2.28e-19 |
|
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: 85.56 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 263 SARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPasairdgvflva 338
Cdd:cd03214 1 EVENLSVGYGGRTvlddLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 339 KDRAST-GIVPEfniyenmslpflprfsNMSVTrrraerqtareQIADLKivcrsERDdLATLSGGNQQKVTVARWLTQP 417
Cdd:cd03214 69 KELARKiAYVPQ----------------ALELL-----------GLAHLA-----DRP-FNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 418 SRLLILDEPFQGVDIAARHDIAAKLRESARDR--ATLVFLTELDEALETADRILVMSENTIV 477
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
2.50e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 2 GDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA 81
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNINDGvvgaLDVASNLVLdrlngAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:PRK13537 83 GVVPQFDNLDPD----FTVRENLLV-----FGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
274-502 |
3.10e-19 |
|
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: 86.84 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRASTGIVP-EFNI 352
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE------------DVRKEPREARRQIGVLPdERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMS----LPFLPRFSNMSvtrRRAERQTAREQIADLKIvcRSERDD-LATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:COG4555 86 YDRLTvrenIRYFAELYGLF---DEELKKRIEELIELLGL--EEFLDRrVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVgehrnADVDMDRLLAEVAGQRLEPA 502
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSShIMQEVEALCDRVVILHKGKVV-----AQGSLDELREEIGEENLEDA 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-241 |
3.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.48 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 19 NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVGAL 98
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGLVFQDPDDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 ---DVAsnlvldrlngagsgffFNPRKVRREAREVAERMGLGIDLSA--EVTD-----LPLADRQMVAIARAMAHEPQVM 168
Cdd:PRK13647 97 vwdDVA----------------FGPVNMGLDKDEVERRVEEALKAVRmwDFRDkppyhLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNA 241
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-235 |
3.82e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG----VMMLGD---RPFSPATPAEA 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshIELLGRtvqREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRAGVVTVHQNINdgVVGALDVASNLVLDRLngaGSGFFFN------PRKVRREAREVAERMGLGIDLSAEVTDLPLADR 152
Cdd:PRK09984 84 SRANTGYIFQQFN--LVNRLSVLENVLIGAL---GSTPFWRtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLF-ALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV-----G 226
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMdTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFydgssQ 238
|
....*....
gi 1998276353 227 QFDEKPLDY 235
Cdd:PRK09984 239 QFDNERFDH 247
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
260-468 |
4.71e-19 |
|
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: 85.61 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaPRTPASAIRDGVF 335
Cdd:COG4133 1 MMLEAENLSCRRGERLlfsgLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 336 LVAkdrASTGIVPEFNIYENMSlpFLPRFSNMSVTRRRAERQTAR---EQIADLKIvcrserddlATLSGGNQQKVTVAR 412
Cdd:COG4133 79 YLG---HADGLKPELTVRENLR--FWAALYGLRADREAIDEALEAvglAGLADLPV---------RQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 413 WLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRI 468
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
274-477 |
5.31e-19 |
|
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: 85.85 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAirdgvflvakdRASTGIV---PE- 349
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-----------RRKVGLVfqnPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 --FN--IYENMSlpFLPRfsNMSVTRRRAERQtAREQIADLKIvcrserDDLA-----TLSGGNQQKVTVARWL-TQPsR 419
Cdd:COG1122 87 qlFAptVEEDVA--FGPE--NLGLPREEIRER-VEEALELVGL------EHLAdrpphELSGGQKQRVAIAGVLaMEP-E 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 420 LLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVThDLDLVAELADRVIVLDDGRIV 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-244 |
5.86e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 16 FGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQNINdgVV 95
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR--VF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 96 GALDVASNLVLdrlngagSGFFFNPRKVRREAREVAERMGLGIDLSAE-VTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:PRK11614 93 SRMTVEENLAM-------GGFFAERDQFQERIKWVYELFPRLHERRIQrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 175 SSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAV-NAMLG 244
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVrSAYLG 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
276-472 |
6.10e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 85.63 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGraYAPRTPASAIRDGVflvakdrastGIVPEFNI-YE 354
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSL----------GYCPQFDAlFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMS----LPFLPRFsnmsvtrRRAERQTAREQIADLKIVCRSE--RDDLA-TLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:cd03263 89 ELTvrehLRFYARL-------KGLPKSEIKEEVELLLRVLGLTdkANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRAtlVFLT--ELDEALETADRILVMS 472
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRS--IILTthSMDEAEALCDRIAIMS 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-224 |
6.54e-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: 85.15 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 13 TKAFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFS----PATPAEAMRAGVV--- 84
Cdd:cd03292 7 TKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIGVVfqd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ---TVHQNINDGVVGALDVAsnlvldrlnGAGsgfffnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM 161
Cdd:cd03292 87 frlLPDRNVYENVAFALEVT---------GVP------PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
274-471 |
6.89e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 85.85 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayAPRTPASAIRDGVFLVAKDRAstgIVPEFNIY 353
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNLPPEKRDISYVPQNYA---LFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSlpflprFSNMSVTRRRAERQTAREQIA-DLKIVCRSERDDlATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDI 432
Cdd:cd03299 90 KNIA------YGLKKRKVDKKEIERKVLEIAeMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 433 AARHDIAAKLRESARDRATLVF-LT-ELDEALETADRILVM 471
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLhVThDFEEAWALADKVAIM 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-426 |
6.89e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVmmlgdrpfspATPAEAMRAGVV---- 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE----------VSIPKGLRIGYLpqep 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ------TVHQNINDGVVGALDVASNlvLDRLNGAGSGFFFNPRKV---------------RREAREVAERMGLG-IDLSA 142
Cdd:COG0488 71 pldddlTVLDTVLDGDAELRALEAE--LEELEAKLAEPDEDLERLaelqeefealggweaEARAEEILSGLGFPeEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 143 EVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLssnEAERLFALIDRLRARGVAILYISHrmsD---IRRLADRIVSL 219
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL---DLESIEWLEEFLKNYPGTVLVVSH---DryfLDRVATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 220 RDGAIVgqfdekplDYEG----------------------------------------------------AVNAMLGQ-- 245
Cdd:COG0488 223 DRGKLT--------LYPGnysayleqraerleqeaaayakqqkkiakeeefirrfrakarkakqaqsrikALEKLEREep 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 246 -----NLGLHSIDARAAGAPVFSARDLRIAPGAKPL----SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQL 316
Cdd:COG0488 295 prrdkTVEIRFPPPERLGKKVLELEGLSKSYGDKTLlddlSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 317 dgrayaprtpASAIRDGVFlvAKDRAStgIVPEFNIYENMSlPFLPRFSNMSVtRRRAER-----QTAREQIADlkivcr 391
Cdd:COG0488 375 ----------GETVKIGYF--DQHQEE--LDPDKTVLDELR-DGAPGGTEQEV-RGYLGRflfsgDDAFKPVGV------ 432
|
490 500 510
....*....|....*....|....*....|....*
gi 1998276353 392 serddlatLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:COG0488 433 --------LSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-275 |
7.14e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.28 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRAGV 83
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNindgVVGAldvasnlvldrlngagsgffFNPRK------------------VRREARevAERMGLGIDLSAEVT 145
Cdd:PRK10419 92 QMVFQD----SISA--------------------VNPRKtvreiireplrhllsldkAERLAR--ASEMLRAVDLDDSVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 146 D-----LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSL 219
Cdd:PRK10419 146 DkrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVM 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 220 RDGAIVgqfDEKPldyegavnamLGQNLGLHSIDARAAGAPVFSARDLRIAPGAKP 275
Cdd:PRK10419 226 DNGQIV---ETQP----------VGDKLTFSSPAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-229 |
8.76e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 8.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPF--SPATPAEAMRAgvvt 85
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfSKTPSDKAIRE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNindgvVGALDVASNL-----VLDRLNGAgsgfffnPRKV----RREAREVAERMGLGIDLSAEVTDLPL----ADR 152
Cdd:PRK11124 80 LRRN-----VGMVFQQYNLwphltVQQNLIEA-------PCRVlglsKDQALARAEKLLERLRLKPYADRFPLhlsgGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD 229
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-477 |
1.24e-18 |
|
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: 88.71 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGV--HRADRGVMMLG----------DRPFSPATP 75
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 76 ----AEAMRAGVV-------TVHQNIND----------GVVGALDVASNlVLDRLNGAGsgffFNPRKVRREAREVAERM 134
Cdd:TIGR03269 82 cpvcGGTLEPEEVdfwnlsdKLRRRIRKriaimlqrtfALYGDDTVLDN-VLEALEEIG----YEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 135 GLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLF-ALIDRLRARGVAILYISHRMSDIRRLA 213
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 214 DRIVSLRDGAIV--GQFDEkpldyegAVNAMLGQNLGLHSIDARAAGAPVFSARDLR---------IAPGAKPLSMELGA 282
Cdd:TIGR03269 237 DKAIWLENGEIKeeGTPDE-------VVAVFMEGVSEVEKECEVEVGEPIIKVRNVSkryisvdrgVVKAVDNVSLEVKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLD-GRAYAPRTpasaiRDGVFLVAKDRASTGIV-------PEFNIYE 354
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMT-----KPGPDGRGRAKRYIGILhqeydlyPHRTVLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMS------LPFlprfsnmSVTRRRAerqtareqIADLKIVCRSERDDLA-------TLSGGNQQKVTVARWLTQPSRLL 421
Cdd:TIGR03269 385 NLTeaigleLPD-------ELARMKA--------VITLKMVGFDEEKAEEildkypdELSEGERHRVALAQVLIKEPRIV 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLREsARDRATLVFLT---ELDEALETADRILVMSENTIV 477
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILK-AREEMEQTFIIvshDMDFVLDVCDRAALMRDGKIV 507
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-301 |
1.28e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAgVVTVHQ 88
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 N----INDGVVGALDVASNLVLDRLNGAGSgfffnprKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHE 164
Cdd:PRK09536 85 DtslsFEFDVRQVVEMGRTPHRSRFDTWTE-------TDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIvgqfdekpldyegavnamlg 244
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV-------------------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 245 qnlglhsidaRAAGAP--VFSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAE 301
Cdd:PRK09536 218 ----------RAAGPPadVLTADTLRAAFDARTAVGTDPATGAPTVTPLPDPDRTEAAA 266
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-234 |
4.04e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEamrAGVVTVHQNI 90
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 ndGVVGALDVASNLVLD-RLNGAgsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMI 169
Cdd:PRK11000 85 --ALYPHLSVAENMSFGlKLAGA------KKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 170 LDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAI--VGqfdeKPLD 234
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVaqVG----KPLE 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-225 |
5.65e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.88 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 27 LDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEamRaGV------------VTVHQNIndgv 94
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--R-PVsmlfqennlfphLTVAQNI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 95 vgALDVASNLvldRLNGAgsgfffnprkVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:COG3840 93 --GLGLRPGL---KLTAE----------QRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 175 SSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:COG3840 158 SALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-227 |
6.25e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.91 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVGAL--- 98
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDNQFVGATvqd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLvldRLNGAgsgfffnPRK--VRReAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSS 176
Cdd:PRK13635 102 DVAFGL---ENIGV-------PREemVER-VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 177 LSSNEAERLFALIDRLRA-RGVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
254-477 |
9.03e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 86.36 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 254 ARAAGAPVFSARDLRIA-PGA-----KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPA 327
Cdd:COG4987 326 APAPGGPSLELEDVSFRyPGAgrpvlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 328 SAirdgvflvakdRASTGIVPE----FN--IYENMslpflpRFSNMSVTRRRAERQTAREQIADLkivCRSERDDLAT-- 399
Cdd:COG4987 406 DL-----------RRRIAVVPQrphlFDttLRENL------RLARPDATDEELWAALERVGLGDW---LAALPDGLDTwl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 ------LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSE 473
Cdd:COG4987 466 geggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAGLERMDRILVLED 544
|
....
gi 1998276353 474 NTIV 477
Cdd:COG4987 545 GRIV 548
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-482 |
1.13e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 81.75 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAI---RDGVFlvakdrastgivPEFNI 352
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYvfqQDALL------------PWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMSLPflPRFSNMSVTRRRAErqtAREQIA--DLKivcRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:cd03293 91 LDNVALG--LELQGVPKAEARER---AEELLElvGLS---GFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 431 DIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSEN--TIVGEHRN 482
Cdd:cd03293 163 DALTREQLQEELLDiWRETGKTVLLVThDIDEAVFLADRVVVLSARpgRIVAEVEV 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-224 |
1.28e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 84.61 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMR 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVV----------TVHQNINDGV----VGALDVASnLVLDRLngagsgfffnpRKVRREarEVAERmglgidlsaEVTD 146
Cdd:PRK09452 88 VNTVfqsyalfphmTVFENVAFGLrmqkTPAAEITP-RVMEAL-----------RMVQLE--EFAQR---------KPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 LPLADRQMVAIARAMAHEPQVMILDEPTSSLS-------SNEAERLfalidrLRARGVAILYISHRMSDIRRLADRIVSL 219
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqmQNELKAL------QRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
....*
gi 1998276353 220 RDGAI 224
Cdd:PRK09452 219 RDGRI 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-241 |
1.96e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAtpaeAMRAGVV---TVHQNIndgvvga 97
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL----ELGAGFHpelTGRENI------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 ldvasnlvldRLNGAGSGffFNPRKVRREAREVAERMGLGidlsaEVTDLPLadRQ----MV---AIARAMAHEPQVMIL 170
Cdd:COG1134 110 ----------YLNGRLLG--LSRKEIDEKFDEIVEFAELG-----DFIDQPV--KTyssgMRarlAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 171 DEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqFDEKPLD----YEGAVNA 241
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV--MDGDPEEviaaYEALLAG 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-490 |
2.42e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 81.46 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPaSAIRdgvflvaKDRASTG-------IVPE 349
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG-KALR-------QLRRQIGmifqqfnLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FNIYENMSLPFLPRFSNMSVTRRR---AERQTAREQIADLKIvcrserDDLA-----TLSGGNQQKVTVARWLTQPSRLL 421
Cdd:cd03256 93 LSVLENVLSGRLGRRSTWRSLFGLfpkEEKQRALAALERVGL------LDKAyqradQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLRESARDR--ATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRL 490
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
283-478 |
2.80e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 80.42 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRtpasaiRDGVFLVAKDRAsTGIV-------PEFNIYEN 355
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDS------RKKINLPPQQRK-IGLVfqqyalfPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 msLPFLPRFSNMSVTRRRAERQTAREQIADLKivcrseRDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAAR 435
Cdd:cd03297 96 --LAFGLKRKRNREDRISVDELLDLLGLDHLL------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1998276353 436 HDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTIVG 478
Cdd:cd03297 168 LQLLPELKQiKKNLNIPVIFVThDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
274-427 |
3.13e-17 |
|
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: 78.46 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAiRDGVFLVAKDrasTGIVPEFNIY 353
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQD---PQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 354 ENMSLPflPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:pfam00005 78 ENLRLG--LLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-245 |
3.56e-17 |
|
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: 80.99 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGVVTVHQninDGVVGALDV 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA-WLRRQVGVVLQ---ENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDrlngagsgfffNPRKVRREAREVAE-----------RMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMI 169
Cdd:cd03252 93 RDNIALA-----------DPGMSMERVIEAAKlagahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 170 LDEPTSSLSSnEAERlfALIDRLRA--RGVAILYISHRMSDIRRlADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQ 245
Cdd:cd03252 162 FDEATSALDY-ESEH--AIMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
276-477 |
4.72e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPAsairdgvflvakDRASTGIVPE-FNIYE 354
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIA------------ARNRIGYLPEeRGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMS----LPFLPRFSNMSVT--RRRAERQTAREQIADLkivcRSERddLATLSGGNQQKVT-VARWLTQPsRLLILDEPF 427
Cdd:cd03269 84 KMKvidqLVYLAQLKGLKKEeaRRRIDEWLERLELSEY----ANKR--VEELSKGNQQKVQfIAAVIHDP-ELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSThQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-226 |
4.77e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAF-GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEA--MRAG 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINdgVVGALDVASNLVLDRLNGAGSGfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMA 162
Cdd:PRK10908 81 IGMIFQDHH--LLMDRTVYDNVAIPLIIAGASG-----DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVG 226
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-227 |
4.89e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVVTVHQNiNDGVVGALD 99
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQD-PEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASNLVldrlngagsgffFNPRKVRREAREVAERMGLGIDL-------SAEVTDLPLADRQMVAIARAMAHEPQVMILDE 172
Cdd:PRK13638 95 IDSDIA------------FSLRNLGVPEAEITRRVDEALTLvdaqhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 173 PTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-234 |
5.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAI-FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGV---HRADRGVMMLGDRPFSPATPA 76
Cdd:PRK13640 1 MKDNIVeFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 77 EaMRAGVVTVHQNINDGVVGAL---DVAsnlvldrlngagsgFFFNPRKVRRE-----AREVAERMGLGIDLSAEVTDLP 148
Cdd:PRK13640 81 D-IREKVGIVFQNPDNQFVGATvgdDVA--------------FGLENRAVPRPemikiVRDVLADVGMLDYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 149 LADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRA-RGVAILYISHRMsDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDI-DEANMADQVLVLDDGKLLAQ 224
|
....*..
gi 1998276353 228 fdEKPLD 234
Cdd:PRK13640 225 --GSPVE 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-243 |
5.75e-17 |
|
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: 83.34 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHR-ADRGVMMLGDRPFSPATPAEAMRAGVVTVHQN-INDGVVGALDVAS 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 103 NLVLDRLNGagsgfFFNPRKVRREAREVAERMGLG-IDLSAEVTDLPLA-----DRQMVAIARAMAHEPQVMILDEPTSS 176
Cdd:TIGR02633 359 NITLSVLKS-----FCFKMRIDAAAELQIIGSAIQrLKVKTASPFLPIGrlsggNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 177 LSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAML 243
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAAAL 500
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
260-500 |
6.00e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.59 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKPL----SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsairdgvf 335
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLlddvSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 336 LVAKDRAstgIVPEFNiyeNMSLPFL----------PRfsnmsVTRRRAERQTAREQIADLKIVCRSERdDLATLSGGNQ 405
Cdd:PRK13548 73 ELARRRA---VLPQHS---SLSFPFTveevvamgraPH-----GLSRAEDDALVAAALAQVDLAHLAGR-DYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 406 QKVTVARWLTQ------PSRLLILDEPFQGVDIAARHDIAAKLRESARDR--ATLVFLTELDEALETADRILVMSENTIV 477
Cdd:PRK13548 141 QRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
250 260
....*....|....*....|...
gi 1998276353 478 GEHRNADVDMDRLLAEVAGQRLE 500
Cdd:PRK13548 221 ADGTPAEVLTPETLRRVYGADVL 243
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-224 |
6.63e-17 |
|
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: 79.89 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTV 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINdgVVGALDVASNL--VLDrlngagsgFFFNPRKVRREARE--VAE------RMGLGIDLSAevtdlplADRQMVA 156
Cdd:cd03218 81 PQEAS--IFRKLTVEENIlaVLE--------IRGLSKKEREEKLEelLEEfhithlRKSKASSLSG-------GERRRVE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 157 IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-230 |
7.60e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRpfspatpaeaMRAGVVT 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----------VKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNindgvvgALDVASNlVLDRLNGAGsgfffnPRKVRREAREVAERMGL-GIDLSAEVTDLPLADRQMVAIARAMAHE 164
Cdd:COG0488 385 QHQE-------ELDPDKT-VLDELRDGA------PGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 165 PQVMILDEPT-----SSLSsneaerlfALIDRLRA-RGVAILyISHrmsD---IRRLADRIVSLRDGAIV---GQFDE 230
Cdd:COG0488 451 PNVLLLDEPTnhldiETLE--------ALEEALDDfPGTVLL-VSH---DryfLDRVATRILEFEDGGVReypGGYDD 516
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
274-477 |
7.70e-17 |
|
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: 79.22 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayapRTPASAIRDGVFLVAKDrastgivPEFNIY 353
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK----PIKAKERRKSIGYVMQD-------VDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLpRFSNMSVTrrrAERQTAREQIADLKIVCRSERDDLaTLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:cd03226 86 TDSVREEL-LLGLKELD---AGNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1998276353 434 ARHDIAAKLRE-SARDRATLVFLTELDEALETADRILVMSENTIV 477
Cdd:cd03226 161 NMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-476 |
8.65e-17 |
|
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: 79.07 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayaprTPASAIRDGvFLVAKDRASTGIV-------PE 349
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG------TDISKLSEK-ELAAFRRRHIGFVfqsfnllPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FNIYENMSLPFLPRfsnmSVTRRRAERQtAREQIADLKIVCRSERDdLATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:cd03255 97 LTALENVELPLLLA----GVPKKERRER-AEELLERVGLGDRLNHY-PSELSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 430 VDIAARHDIAAKLRESARDR-ATLVFLTELDEALETADRILVMSENTI 476
Cdd:cd03255 171 LDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
262-476 |
9.25e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 78.70 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 262 FSARDLRIAPGAK----PLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPrTPASAIRDGVFLV 337
Cdd:COG4619 1 LELEGLSFRVGGKpilsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA-MPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 338 AkdrASTGIVPEfNIYENMSLPFlpRFSNMSVTRRRAERqtareqiaDLKIVCRSERD---DLATLSGGNQQKVTVAR-W 413
Cdd:COG4619 80 P---QEPALWGG-TVRDNLPFPF--QLRERKFDRERALE--------LLERLGLPPDIldkPVERLSGGERQRLALIRaL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 414 LTQPsRLLILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:COG4619 146 LLQP-DVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVShDPEQIERVADRVLTLEAGRL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-217 |
9.31e-17 |
|
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: 81.25 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRA---DRGVMMLGDRPFSPATPAEaMR 80
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE-LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 A----GVVTVHQN----------INDGVVGALdvasnlvldRLNGAGSGfffnpRKVRREAREVAERMGlgIDLSAEVtd 146
Cdd:COG0444 82 KirgrEIQMIFQDpmtslnpvmtVGDQIAEPL---------RIHGGLSK-----AEARERAIELLERVG--LPDPERR-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 lplAD----------RQMVAIARAMAHEPQVMILDEPTSSL-SSNEAERLfALIDRLRA-RGVAILYISHRMSDIRRLAD 214
Cdd:COG0444 144 ---LDryphelsggmRQRVMIARALALEPKLLIADEPTTALdVTIQAQIL-NLLKDLQReLGLAILFITHDLGVVAEIAD 219
|
...
gi 1998276353 215 RIV 217
Cdd:COG0444 220 RVA 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
254-479 |
9.78e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 82.88 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 254 ARAAGAPVFSARDLRIA-----PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAS 328
Cdd:COG4988 329 LPAAGPPSIELEDVSFSypggrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 329 aIRDGVFLVAKDrastgivPE-FN--IYENMslpflpRFSNMSVTRrrAERQTAREQiADLKIVCRSERDDLAT------ 399
Cdd:COG4988 409 -WRRQIAWVPQN-------PYlFAgtIRENL------RLGRPDASD--EELEAALEA-AGLDEFVAALPDGLDTplgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 --LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSENTIV 477
Cdd:COG4988 472 rgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR-TVILITHRLALLAQADRILVLDDGRIV 550
|
..
gi 1998276353 478 GE 479
Cdd:COG4988 551 EQ 552
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-231 |
1.10e-16 |
|
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: 79.65 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAF-GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTV 86
Cdd:cd03295 2 EFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNIndGVVGALDVASNLVL-DRLNGagsgffFNPRKVRREAREVAERMGLGIDLSAE--VTDLPLADRQMVAIARAMAH 163
Cdd:cd03295 81 IQQI--GLFPHMTVEENIALvPKLLK------WPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVgQFDEK 231
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV-QVGTP 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-251 |
1.17e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.24 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 27 LDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeamRAGV------------VTVHQNIndgv 94
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVsmlfqennlfshLTVAQNI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 95 vgALDVASNLvldRLNGAGsgfffnprkvRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:PRK10771 93 --GLGLNPGL---KLNAAQ----------REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 175 SSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqfdekpldYEGAVNAMLGQN------L 247
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA---------WDGPTDELLSGKasasalL 228
|
....
gi 1998276353 248 GLHS 251
Cdd:PRK10771 229 GIKS 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
274-477 |
1.18e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.20 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPASAIRDGVFLVAKDRAstgIVPEFNIY 353
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK---DITNLPPHKRPVNTVFQNYA---LFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLPRFSNMSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:cd03300 91 ENIAFGLRLKKLPKAEIKERVAEALDLVQLEGY------ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 434 ARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03300 165 LRKDMQLELKRLQKELGiTFVFVThDQEEALTMSDRIAVMNKGKIQ 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-229 |
1.20e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.91 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpaTPAeAMRAgvvTVHQNinDGVVG 96
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPG-ADRG---VVFQK--DALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 ALDVASNLVLD-RLNGAgsgfffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:COG4525 90 WLNVLDNVAFGlRLRGV-------PKAERRArAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 175 SSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIV--SLRDGAIVGQFD 229
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVvmSPGPGRIVERLE 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-224 |
1.23e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.63 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEA------------M 79
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrlL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGVVTVHQNINdgVVGALDVASNLVLDRLNGAGSGfffnprkvRREAREVAERM--GLGIDLSAEV---TDLPLADRQM 154
Cdd:PRK10619 91 RTRLTMVFQHFN--LWSHMTVLENVMEAPIQVLGLS--------KQEARERAVKYlaKVGIDERAQGkypVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 155 VAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-227 |
1.63e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFS-PATPAEAMRAGVVTVHQNINDGVVgALD 99
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPDDQLF-APT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASNLVLDRLNgagsgFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSS 179
Cdd:PRK13639 96 VEEDVAFGPLN-----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 180 NEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-479 |
2.06e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 76.70 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKdrastgivpefniyenm 356
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 357 slpflprfsnmsvtrrraerqtareqiadlkivcrserddlatLSGGNQQKVTVARWLTQPSRLLILDEP---FQGVDIA 433
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPtaaLTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 434 ARHDIAAKLRESARdraTLVFLT-ELDEALETADRILVMSENTIVGE 479
Cdd:cd03216 120 RLFKVIRRLRAQGV---AVIFIShRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-224 |
2.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.02 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVGAL--- 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPDNQFVGSIvky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLvldrlngagSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLS 178
Cdd:PRK13648 104 DVAFGL---------ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 179 SNEAERLFALIDRLRA-RGVAILYISHRMSDIRRlADRIVSLRDGAI 224
Cdd:PRK13648 175 PDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-479 |
2.93e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 78.25 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTrlaeTLF----GIHAPLAGSMQLDGRAYAPRTPASAIRDGV---FLVakdrasTGIVP 348
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKT----TLFnlisGFLRPTSGSVLFDGEDITGLPPHEIARLGIgrtFQI------PRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPFLPR-FSNMSVTRRRAERQTAREQIAD-LKIV-CRSERDDLA-TLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:cd03219 89 ELTVLENVMVAAQARtGSGLLLARARREEREARERAEElLERVgLADLADRPAgELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRATLVfLTE--LDEALETADRILVMSENTIVGE 479
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVL-LVEhdMDVVMSLADRVTVLDQGRVIAE 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
3.03e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.88 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAFGP--NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAmR 80
Cdd:PRK13632 4 KSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVVTVHQNINDGVVGAL---DVASNLVLDRLNgagsgfffnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAI 157
Cdd:PRK13632 83 KKIGIIFQNPDNQFIGATvedDIAFGLENKKVP---------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGV-AILYISHRMSDIrRLADRIVSLRDGAIVGQfdEKPLD 234
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQ--GKPKE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-225 |
3.41e-16 |
|
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: 81.27 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAfgpnavLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRAdRGVMMLGDRPFSPATPAE--AMRAGVV 84
Cdd:COG4172 293 RRTVGHVKA------VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrPLRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQNINdgvvgaldvasnlvldrlngaGSgffFNPR-----------KVRREAREVAERMGLGIDLSAEVtDLPLAD-- 151
Cdd:COG4172 366 VVFQDPF---------------------GS---LSPRmtvgqiiaeglRVHGPGLSAAERRARVAEALEEV-GLDPAArh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 152 ----------RQMVAIARAMAHEPQVMILDEPTSSLS-SNEAERLfALIDRL-RARGVAILYISHRMSDIRRLADRIVSL 219
Cdd:COG4172 421 ryphefsggqRQRIAIARALILEPKLLVLDEPTSALDvSVQAQIL-DLLRDLqREHGLAYLFISHDLAVVRALAHRVMVM 499
|
....*.
gi 1998276353 220 RDGAIV 225
Cdd:COG4172 500 KDGKVV 505
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-477 |
3.50e-16 |
|
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: 81.27 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIFRIAGLTKAFG----PNAVLRGVGLDLRAGEVTVLMGANGAGKS----TLVKVMSGVHRADRGVMMLGDRPFSP 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 73 ATPAE--AMRAGVVTV-----------HQNINDGVVGALdvasnlvldRLNGAGSGfffnpRKVRREAREVAERMGlgID 139
Cdd:COG4172 81 LSERElrRIRGNRIAMifqepmtslnpLHTIGKQIAEVL---------RLHRGLSG-----AAARARALELLERVG--IP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 140 LSAEvtdlPLAD---------RQMVAIARAMAHEPQVMILDEPTSSLS-SNEAERLfALIDRLRAR-GVAILYISHRMSD 208
Cdd:COG4172 145 DPER----RLDAyphqlsggqRQRVMIAMALANEPDLLIADEPTTALDvTVQAQIL-DLLKDLQRElGMALLLITHDLGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 209 IRRLADRIVSLRDGAIVGQfdekpldyeGAVNAMLG-------QNL-----GLHSIDARAAGAPVFSARDLRIA-PGAKP 275
Cdd:COG4172 220 VRRFADRVAVMRQGEIVEQ---------GPTAELFAapqhpytRKLlaaepRGDPRPVPPDAPPLLEARDLKVWfPIKRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 L--------------SMELGAGEVVAVTGLVGVGKTRLAETLFGIHaPLAGSMQLDGRAYAPRTPAS--AIRDGVFLVAK 339
Cdd:COG4172 291 LfrrtvghvkavdgvSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 340 DrastgivpefniyenmslPF--L-PRfsnMSVTR-------------RRAERqtaREQIAD-LKIVcrseRDDLATL-- 400
Cdd:COG4172 370 D------------------PFgsLsPR---MTVGQiiaeglrvhgpglSAAER---RARVAEaLEEV----GLDPAARhr 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 401 -----SGGNQQKVTVARWL-TQPsRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELD--EALetADRILV 470
Cdd:COG4172 422 yphefSGGQRQRIAIARALiLEP-KLLVLDEPTSALDVSVQAQILDLLRDLQREHGlAYLFIShDLAvvRAL--AHRVMV 498
|
....*..
gi 1998276353 471 MSENTIV 477
Cdd:COG4172 499 MKDGKVV 505
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-225 |
3.83e-16 |
|
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: 77.57 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 7 FRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGvVTV 86
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPE-LTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNIndgvvgaldvasnlvldRLNGAGSGffFNPRKVRREAREVAERMGLGidlsaEVTDLPL-------ADRQMVAIAR 159
Cdd:cd03220 102 RENI-----------------YLNGRLLG--LSRKEIDEKIDEIIEFSELG-----DFIDLPVktyssgmKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 160 AMahEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:cd03220 158 AL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
274-472 |
3.92e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 77.51 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPASAIRDGVFlvakdrASTGIVPEFNIY 353
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGPDRMVVF------QNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFlprfSNMSVTRRRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:TIGR01184 73 ENIALAV----DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 434 ARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMS 472
Cdd:TIGR01184 149 TRGNLQEELMQIWEEhRVTVLMVThDVDEALLLSDRVVMLT 189
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-225 |
6.00e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVM-------SGVHR-ADRGVMMLGDRPFs 71
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRvAGQDVATLDADAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 72 patpAEAMRAGVVTVHQNINdgVVGALDVASNLVLDRLNgAGSGfffnpRKVRRE-AREVAERMGLGIDLSAEVTDLPLA 150
Cdd:PRK10535 81 ----AQLRREHFGFIFQRYH--LLSHLTAAQNVEVPAVY-AGLE-----RKQRLLrAQELLQRLGLEDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 151 DRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRmSDIRRLADRIVSLRDGAIV 225
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-225 |
8.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQNINDGVVGaldva 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQFVG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 102 sNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNE 181
Cdd:PRK13644 93 -RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276353 182 AERLFALIDRLRARGVAILYISHRMSDIrRLADRIVSLRDGAIV 225
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIV 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
257-471 |
8.99e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 257 AGAPVFSARDLRIAPGAkplsmelgageVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR---AYAPRTpaSAIRDG 333
Cdd:NF040873 3 GGRPVLHGVDLTIPAGS-----------LTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarvAYVPQR--SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 334 VFLVAKDRASTGIVPEFNIYENMSlpflprfsnmSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARW 413
Cdd:NF040873 70 LPLTVRDLVAMGRWARRGLWRRLT----------RDDRAAVDDALERVGLADL------AGRQLGELSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 414 LTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVM 471
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
259-485 |
9.56e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 79.56 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 259 APVFSARDLRIA------PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAP---LAGSMQLDGRAYAPRTPASA 329
Cdd:COG1123 2 TPLLEVRDLSVRypggdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 330 IRDgVFLVAKDrASTGIVP---EFNIYENMSLPFLPRfsnmSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQ 406
Cdd:COG1123 82 GRR-IGMVFQD-PMTQLNPvtvGDQIAEALENLGLSR----AEARARVLELLEAVGLERR------LDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 407 KVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTE--LDEALETADRILVMSENTIVGEHRNAD 484
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLIThdLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
.
gi 1998276353 485 V 485
Cdd:COG1123 230 I 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
276-477 |
1.06e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 75.99 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFlvakdrASTGIVPEFNIYEN 355
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF------QENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPFLPRFSNMSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAAR 435
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGL------EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276353 436 HDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03298 165 AEMLDLVLDLHAETKmTVLMVThQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-225 |
1.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 16 FGPNAVLRGVGLD-----LRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAM---RAGVVTVH 87
Cdd:PRK13641 12 YSPGTPMEKKGLDnisfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QnindgvVGALDVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLsAEVTDLPLADRQM--VAIARAMAHEP 165
Cdd:PRK13641 92 Q------FPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDL-ISKSPFELSGGQMrrVAIAGVMAYEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 166 QVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-227 |
1.28e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.59 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVV 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQNINDGVvgaldvasnlVLDRLNGAGSGFFFN--PRKVRREAREVAERMG-LGIDLSAE--VTDLPLADRQMVAIAR 159
Cdd:PRK11231 82 PQHHLTPEGI----------TVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEqTRINHLADrrLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-246 |
1.68e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHR-ADRGVMMLGDRPFSPATPAEAMRAGVVTVHQN-INDGVVGALDVAS 102
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDrKRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 103 NL---VLDRLNGAGSgffFNPRKVRREAREVAERMGLGI-DLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLS 178
Cdd:PRK13549 361 NItlaALDRFTGGSR---IDDAAELKTILESIQRLKVKTaSPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 179 SNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVNAMLGQN 246
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALRSE 505
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-224 |
2.01e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATP------AEAMRAG 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrlmfQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINDGVVGaldvasnlvldrlngagsgfffnprKVRREAREVAERMGLgidlSAEVTDLPLA----DRQMVAIA 158
Cdd:PRK11247 95 WKKVIDNVGLGLKG-------------------------QWRDAALQALAAVGL----ADRANEWPAAlsggQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAI 224
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
274-473 |
2.36e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 74.15 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasaIRDGVFLVAKDRASTGIVpefniY 353
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED---------LTDLEDELPPLRRRIGMV-----F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLpflprFSNMSVtrrraerqtaREQIADLkivcrserddlatLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:cd03229 83 QDFAL-----FPHLTV----------LENIALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1998276353 434 ARHDIAAKLRES-ARDRATLVFLT-ELDEALETADRILVMSE 473
Cdd:cd03229 135 TRREVRALLKSLqAQLGITVVLVThDLDEAARLADRVVVLRD 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-225 |
2.92e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 16 FGPNA-----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAgvvtVHQNI 90
Cdd:PRK13643 11 YQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP----VRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 ndGVVGAL---DVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLsAEVTDLPLADRQM--VAIARAMAHEP 165
Cdd:PRK13643 87 --GVVFQFpesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEF-WEKSPFELSGGQMrrVAIAGILAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 166 QVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-222 |
3.06e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSP-ATPAEAM----RAGVV-TVHQNINDgv 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAElrnqKLGFIyQFHHLLPD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 95 VGALDvasNLVLDRLNGAGsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:PRK11629 102 FTALE---NVAMPLLIGKK-----KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 175 SSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLaDRIVSLRDG 222
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-204 |
3.59e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMR-AGvvtvHQNindGVV 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG----HRN---AMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 96 GALDVASNLVL-DRLNGAGsgfffnprkvRREAREVAERMGLgidlsAEVTDLPLAD-----RQMVAIARAMAHEPQVMI 169
Cdd:PRK13539 86 PALTVAENLEFwAAFLGGE----------ELDIAAALEAVGL-----APLAHLPFGYlsagqKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1998276353 170 LDEPTSSLSSNeAERLFA-LIDRLRARGVAILYISH 204
Cdd:PRK13539 151 LDEPTAALDAA-AVALFAeLIRAHLAQGGIVIAATH 185
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-472 |
3.66e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.28 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPASAIRDGVFlvAKDrastGIVPEFNIY 353
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADRGVVF--QKD----ALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLPRFSNMSVTRRRAERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:COG4525 95 DNVAFGLRLRGVPKAERRARAEELLALVGLADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 434 ARHDIAAK-LRESARDRATLVFLT-ELDEALETADRILVMS 472
Cdd:COG4525 169 TREQMQELlLDVWQRTGKGVFLIThSVEEALFLATRLVVMS 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-476 |
5.01e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 74.68 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsaiRDGVFLVAKDRAstgIVPEFNIYEN 355
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERNVGFVFQHYA---LFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MS--LPFLPRfsnmsvtRRRAERQTAREQIADL-KIVCRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:cd03296 95 VAfgLRVKPR-------SERPPEAEIRAKVHELlKLVQLDWLADRypAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 431 DIAARHDIAAKLREsARDR--ATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:cd03296 168 DAKVRKELRRWLRR-LHDElhVTTVFVThDQEEALEVADRVVVMNKGRI 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-204 |
5.42e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 15 AFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMmlgDRPfspatpaEAMRAGVVTvhQNINdgv 94
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRN-------GKLRIGYVP--QKLY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 95 vgaLDVASNLVLDRLngagsgFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:PRK09544 78 ---LDTTLPLTVNRF------LRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|.
gi 1998276353 175 SSLSSNEAERLFALIDRLRAR-GVAILYISH 204
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
274-489 |
5.94e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.74 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTrlaeTLF----GIHAPLAGSMQLDGRAyaprtpasairdgvflVAKDRASTGIV-- 347
Cdd:COG1116 28 DDVSLTVAAGEFVALVGPSGCGKS----TLLrliaGLEKPTSGEVLVDGKP----------------VTGPGPDRGVVfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 -----PEFNIYENMSLPflPRFSNMSVTRRRAErqtAREQIADLKIvcrSERDDL--ATLSGGNQQKVTVARWLTQPSRL 420
Cdd:COG1116 88 epallPWLTVLDNVALG--LELRGVPKAERRER---ARELLELVGL---AGFEDAypHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 421 LILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSEN--TIVGEHrnaDVDMDR 489
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVThDVDEAVFLADRVVVLSARpgRIVEEI---DVDLPR 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
6.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA-----GVV---TVHQNINDG 93
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPlrkkvGIVfqfPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 94 VvgALDVAsnlvldrlngagsgffFNP-------RKVRREAREVAERMGLGIDLSAEvTDLPLADRQM--VAIARAMAHE 164
Cdd:PRK13634 103 V--EKDIC----------------FGPmnfgvseEDAKQKAREMIELVGLPEELLAR-SPFELSGGQMrrVAIAGVLAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
6.27e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.69 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVH------RADRGVMMLGDRPFSPATPA 76
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgaRVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 77 EAMRAGVVTVHQN-------INDGVVGALdvasnlvldRLNGagsgfffnpRKVRREAREVAERMGLGIDLSAEV----- 144
Cdd:COG1117 88 VELRRRVGMVFQKpnpfpksIYDNVAYGL---------RLHG---------IKSKSELDEIVEESLRKAALWDEVkdrlk 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 145 ---TDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARgVAILYISHRMSDIRRLADR 215
Cdd:COG1117 150 ksaLGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDY 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-225 |
6.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.56 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGV------HRADRGVMMLGDRPFSpaTPAEAMRAG 82
Cdd:PRK14247 6 IRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypeARVSGEVYLDGQDIFK--MDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNINDGVVGAL--DVASNLVLDRLNGAGSGFFFNPRKVRREAR---EVAERMGlgidlsAEVTDLPLADRQMVAI 157
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIfeNVALGLKLNRLVKSKKELQERVRWALEKAQlwdEVKDRLD------APAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-225 |
6.62e-15 |
|
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: 73.84 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGvhRADRGVMMLGD-----RPFSPATpaeaMRAGVVTVHQniNDGVV 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQilfngQPRKPDQ----FQKCVAYVRQ--DDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 96 GALDV------ASNLVLDRLNGagsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMI 169
Cdd:cd03234 94 PGLTVretltyTAILRLPRKSS-------DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 170 LDEPTSSLSSNEAERLFALIDRLRARGVAILYISHR-MSDIRRLADRIVSLRDGAIV 225
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
265-479 |
8.44e-15 |
|
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: 73.69 E-value: 8.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPASAIRDGVFlvakd 340
Cdd:cd03261 4 RGLTKSFGGRTvlkgVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE---DISGLSEAELYRL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 341 RASTGIVPEFN-------IYENMSLPfLPRFSNMSvtrrraeRQTAREQIAD-LKIVCRSERDDL--ATLSGGNQQKVTV 410
Cdd:cd03261 76 RRRMGMLFQSGalfdsltVFENVAFP-LREHTRLS-------EEEIREIVLEkLEAVGLRGAEDLypAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 411 ARWLTQPSRLLILDEPFQGVD-IAAR--HDIAAKLRESArdRATLVFLT-ELDEALETADRILVMSENTIVGE 479
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDpIASGviDDLIRSLKKEL--GLTSIMVThDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-204 |
1.02e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAmRAGVVTVHQNi 90
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-RGLLYLGHAP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 ndGVVGALDVASNLVldrlngagsgfFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMIL 170
Cdd:cd03231 83 --GIKTTLSVLENLR-----------FWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 1998276353 171 DEPTSSLSSNEAERLFALIDRLRARGVAILYISH 204
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-248 |
1.24e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVV---- 84
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFVfqhy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 ------TVHQNINDGVVgaldvasnlVLdrlngagsgfffnPRKVRREAREVAER-MGLgidlsAEVTDLP-LADR---- 152
Cdd:PRK10851 84 alfrhmTVFDNIAFGLT---------VL-------------PRRERPNAAAIKAKvTQL-----LEMVQLAhLADRypaq 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 ------QMVAIARAMAHEPQVMILDEPTSSLSSN---EAER-LFALIDRLRARGVailYISHRMSDIRRLADRIVSLRDG 222
Cdd:PRK10851 137 lsggqkQRVALARALAVEPQILLLDEPFGALDAQvrkELRRwLRQLHEELKFTSV---FVTHDQEEAMEVADRVVVMSQG 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 1998276353 223 AI--VGQFDE---KP-----LDYEGAVNAMLGQNLG 248
Cdd:PRK10851 214 NIeqAGTPDQvwrEPatrfvLEFMGEVNRLQGTIRG 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
265-492 |
1.25e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.25 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGAKPL--SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsairdgvflvakDRA 342
Cdd:COG3840 5 DDLTYRYGDFPLrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------------ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 343 STGIVPEFN------IYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKivcrserDDL-ATLSGGNQQKVTVARWLT 415
Cdd:COG3840 73 VSMLFQENNlfphltVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLL-------DRLpGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 416 QPSRLLILDEPFQGVDIAARHDIAAKLRESARDR-ATLVFLT-ELDEALETADRILVMSENTIVgehrnADVDMDRLLA 492
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERgLTVLMVThDPEDAARIADRVLLVADGRIA-----ADGPTAALLD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-229 |
1.27e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKST----LVKVMsgvhrADRGVMMLGDRPFSPATPAEAM--RAGVVT 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLpvRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQNINDGVVGALDV----ASNLVLDR--LNGAgsgfffnprkvRREAREVAERMGLGIDLSAE---VTDLPLADRQMVA 156
Cdd:PRK15134 367 VFQDPNSSLNPRLNVlqiiEEGLRVHQptLSAA-----------QREQQVIAVMEEVGLDPETRhryPAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 157 IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD 229
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
268-471 |
1.49e-14 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 71.65 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 268 RIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayaprTPASAIRDGVFlvakdRASTGIV 347
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG------VDLRDLDLESL-----RKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFniyenmslPFLprFsNMSVtrrraerqtaREQIadlkivcrserddlatLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:cd03228 82 PQD--------PFL--F-SGTI----------RENI----------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVM 471
Cdd:cd03228 125 SALDPETEALILEALRALAKGK-TVIVIAHRLSTIRDADRIIVL 167
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-216 |
1.67e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.38 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIFRIAGLTKAF--------GPNAVLR---GVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRP 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 70 FSPATPAE--AMRAGVVTVHQN----------INDGVVGALDVasnlvldrlNGAGSGfffnpRKVRREAREVAERMGLg 137
Cdd:COG4608 82 ITGLSGRElrPLRRRMQMVFQDpyaslnprmtVGDIIAEPLRI---------HGLASK-----AERRERVAELLELVGL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 138 idlSAEVtdlplADR----------QMVAIARAMAHEPQVMILDEPTSSLS-SNEAERLFALIDrLRAR-GVAILYISHR 205
Cdd:COG4608 147 ---RPEH-----ADRyphefsggqrQRIGIARALALNPKLIVCDEPVSALDvSIQAQVLNLLED-LQDElGLTYLFISHD 217
|
250
....*....|.
gi 1998276353 206 MSDIRRLADRI 216
Cdd:COG4608 218 LSVVRHISDRV 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
271-477 |
2.39e-14 |
|
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: 73.06 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRDgvflVAKDRAST-----G 345
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRE----LRRKKISMvfqsfA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 346 IVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSErddlatLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 426 PFQGVDIAARHDIAAK-LRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03294 187 AFSALDPLIRREMQDElLRLQAELQKTIVFIThDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-227 |
3.06e-14 |
|
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: 70.80 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfsPATPAEAMRAGVVTVHQNIndgvvgaldv 100
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLISVLNQRP---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 asnlvldrlngagsgFFFNprkvrreareVAERMGLGIDLSAevtdlplADRQMVAIARAMAHEPQVMILDEPTSSLSS- 179
Cdd:cd03247 85 ---------------YLFD----------TTLRNNLGRRFSG-------GERQRLALARILLQDAPIVLLDEPTVGLDPi 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 180 NEAERLFALIDRLRARgvAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:cd03247 133 TERQLLSLIFEVLKDK--TLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
274-500 |
3.32e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRAstgIVPEFNIY 353
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELS---VIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDL-ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDI 432
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 433 AARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQRLE 500
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYIShKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQ 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-234 |
3.54e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 71.73 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMragVV----------TVHQNIn 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRM---VVfqnysllpwlTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 92 dgvvgALDVasNLVLDRLngagsgfffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMIL 170
Cdd:TIGR01184 76 -----ALAV--DRVLPDL----------SKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 171 DEPTSSLS----SNEAERLFALIDRlraRGVAILYISHRMSDIRRLADRIVSLRDG--AIVGQFDEKPLD 234
Cdd:TIGR01184 139 DEPFGALDaltrGNLQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNGpaANIGQILEVPFP 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-230 |
3.71e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 19 NAVlRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGDRPFsPATPAEAMRAGVVTVHQnindgvvga 97
Cdd:COG4586 36 EAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGeVRVLGYVPF-KRRKEFARRIGVVFGQR--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 ldvaSNL-----VLD--RLNGAGSGFffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRqMVA-IARAMAHEPQVMI 169
Cdd:COG4586 105 ----SQLwwdlpAIDsfRLLKAIYRI--PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQR-MRCeLAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 170 LDEPTSSLSSNEAERLFALIDRLRA-RGVAILYISHRMSDIRRLADRIVSLRDGAIV--GQFDE 230
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIydGSLEE 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
276-476 |
3.80e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRaSTGIVPE------ 349
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT------------DVSRLHARDR-KVGFVFQhyalfr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 -FNIYENMS--LPFLPRFS--NMSVTRRRAERQTAREQIADLkivcrSERDDlATLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:PRK10851 88 hMTVFDNIAfgLTVLPRRErpNAAAIKAKVTQLLEMVQLAHL-----ADRYP-AQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEElKFTSVFVThDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
271-477 |
3.88e-14 |
|
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: 71.95 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRDGVFLVAKdraSTGIVPEF 350
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDPVELRRKIGYVIQ---QIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 NIYENMSLpfLPRFSNMSVTRRRAErqtAREQIADLKIVCRSERDDL-ATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:cd03295 91 TVEENIAL--VPKLLKWPKEKIRER---ADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1998276353 430 VDIAARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElGKTIVFVThDIDEAFRLADRIAIMKNGEIV 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-204 |
4.01e-14 |
|
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: 70.85 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMRAGVVTVHQni 90
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 nDGVVGALDVASNLVldrlngagsgfFFNP--RKVRREAREVAERMGLgidlsAEVTDLPLA-----DRQMVAIARAMAH 163
Cdd:TIGR01189 82 -PGLKPELSALENLH-----------FWAAihGGAQRTIEDALAAVGL-----TGFEDLPAAqlsagQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISH 204
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-238 |
4.02e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMRAGVVTVHQNindGVVG 96
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQT---PTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 ALDVASNLVLdrlngagsgfffnPRKVRREAREVA------ERMGLGID-LSAEVTDLPLADRQMVAIARAMAHEPQVMI 169
Cdd:PRK10247 94 GDTVYDNLIF-------------PWQIRNQQPDPAiflddlERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 170 LDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRlADRIVSLRDGAivGQFDEKplDYEGA 238
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLQPHA--GEMQEA--RYELA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-227 |
5.09e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPAT-----PAEAMRAGVV----------TVHQN 89
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclPPEKRRIGYVfqdarlfphyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 90 IN-----------DGVVGALDVASnlVLDRLNGAGSGfffnprkvrrearevaermglgidlsaevtdlplADRQMVAIA 158
Cdd:PRK11144 97 LRygmaksmvaqfDKIVALLGIEP--LLDRYPGSLSG----------------------------------GEKQRVAIG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 159 RAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLrARGV--AILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK11144 141 RALLTAPELLLMDEPLASLDLPRKRELLPYLERL-AREIniPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-479 |
5.14e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDrastgIVPEFNIYEN 355
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDN-----LDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 msLPFLPRFSNMSVTRRRAERQT----AR-EQIADLKIvcrserddlATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:PRK13537 101 --LLVFGRYFGLSAAAARALVPPllefAKlENKADAKV---------GELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1998276353 431 DIAARHDIAAKLRE-SARDRATLVFLTELDEALETADRILVMSENTIVGE 479
Cdd:PRK13537 170 DPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
5.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFspatpaEAMRAGVVTVHQNIN------DGVV 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLMKLRESVGmvfqdpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 96 GALDVASNLVLDRLNgagsgFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTS 175
Cdd:PRK13636 96 FSASVYQDVSFGAVN-----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 176 SLSS-NEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13636 171 GLDPmGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-481 |
6.36e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrAYAPRTPASAirdgvflvakdRASTGIVPEFniyEN 355
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-VPVPARARLA-----------RARIGVVPQF---DN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPFLPRfSNMSVTRR--RAERQTAREQIADLKIVCRSERD---DLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:PRK13536 125 LDLEFTVR-ENLLVFGRyfGMSTREIEAVIPSLLEFARLESKadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 431 DIAARHDIAAKLRE-SARDRATLVFLTELDEALETADRILVMSENTIVGEHR 481
Cdd:PRK13536 204 DPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-233 |
7.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.12 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRagvvTVHQNIndGVVGALDvA 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR----PVRKRI--GMVFQFP-E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 102 SNLVLDRLNgagSGFFFNPRKVRREAREVAER-MGLGIDLSAEVTDLPLADRQM-------VAIARAMAHEPQVMILDEP 173
Cdd:PRK13646 96 SQLFEDTVE---REIIFGPKNFKMNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMsggqmrkIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 174 TSSLSSNEAERLFALIDRLRA-RGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPL 233
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-230 |
1.10e-13 |
|
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: 70.65 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKvmsgvhradrgvmmLGDRPFSPatpaeamRAGVVTV-HQNIND------- 92
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVS--------------LLERFYDP-------TSGEILLdGVDIRDlnlrwlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 93 ---GVVG------ALDVASNLVLDRlngagsgfffNPRKVRrEAREVAER-------MGLGIDLSAEV----TDLPLADR 152
Cdd:cd03249 77 sqiGLVSqepvlfDGTIAENIRYGK----------PDATDE-EVEEAAKKanihdfiMSLPDGYDTLVgergSQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIV--GQFDE 230
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVeqGTHDE 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-261 |
1.19e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGDRPFSPATPAEAMRAG 82
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTvhQNindgVVGALDVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTD-LPLADRQMVAIARAM 161
Cdd:PRK10253 85 LLA--QN----ATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLDYEGAVN 240
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
|
250 260
....*....|....*....|.
gi 1998276353 241 AMLGqnLGLHSIDARAAGAPV 261
Cdd:PRK10253 239 RIYG--LRCMIIDDPVAGTPL 257
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
276-479 |
1.28e-13 |
|
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: 70.09 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpaSAIRDGvflvAKDRASTGIVPEFNIYEN 355
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH--------DVVREP----REVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MslpfLPRFSNMSVTRRRA--ERQTAREQIAD-LKIVCRSERDD--LATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:cd03265 87 E----LTGWENLYIHARLYgvPGAERRERIDElLDFVGLLEAADrlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 431 DIAARHDIAAKLRESARDRATLVFLTE--LDEALETADRILVMSENTIVGE 479
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTThyMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
273-498 |
1.55e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 273 AKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDG---RAYAPRTPASAIRdgvfLVAKDRASTGIVPE 349
Cdd:PRK10253 23 AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASKEVARRIG----LLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FNIYENMSLPFLPRFsnmsvTRRRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:PRK10253 99 QELVARGRYPHQPLF-----TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 430 VDIAARHDIAAKLRESARDRA-TL-VFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQR 498
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGyTLaAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLR 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-225 |
1.61e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPF------SPATPAEA 78
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYnghniySPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRAGVVTVHQNIN-------DGVVGALdvasnlvldRLNGAgsgfffnprKVRREAREVAERMGLGIDLSAEVTD----- 146
Cdd:PRK14239 84 LRKEIGMVFQQPNpfpmsiyENVVYGL---------RLKGI---------KDKQVLDEAVEKSLKGASIWDEVKDrlhds 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 ---LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEA----ERLFALIDRLrargvAILYISHRMSDIRRLADRIVSL 219
Cdd:PRK14239 146 algLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAgkieETLLGLKDDY-----TMLLVTRSMQQASRISDRTGFF 220
|
....*.
gi 1998276353 220 RDGAIV 225
Cdd:PRK14239 221 LDGDLI 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-225 |
2.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.46 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNA-----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDrpFSPATPAEAM--- 79
Cdd:PRK13637 4 KIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 --RAGVV-----------TVHQNINDGvvgaldvASNLVLdrlngagsgfffNPRKVRREAREVAERMGLGIDLSAEVT- 145
Cdd:PRK13637 82 rkKVGLVfqypeyqlfeeTIEKDIAFG-------PINLGL------------SEEEIENRVKRAMNIVGLDYEDYKDKSp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 146 -DLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGA 223
Cdd:PRK13637 143 fELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
..
gi 1998276353 224 IV 225
Cdd:PRK13637 223 CE 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
37-227 |
2.29e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.22 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 37 LMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEaMRAGVVTVHQNINDGVVGAL---DVA---SNLVLDRln 110
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPDDQIFSPTveqDIAfgpINLGLDE-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 111 gagsgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALID 190
Cdd:PRK13652 112 ----------ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1998276353 191 RLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13652 182 DLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
274-477 |
2.32e-13 |
|
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: 69.46 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsairdgvfLVAKDRASTGIVPEfNIY 353
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR--------LRKIRRKEIQMVFQ-DPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 EnmSLPflPRfsnMSV---------TRRRAERQTAREQIADLKIVCRSERDDLAT-----LSGGNQQKVTVARWL-TQPs 418
Cdd:cd03257 93 S--SLN--PR---MTIgeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALaLNP- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 419 RLLILDEPFQGVDIAARHDIAAKLRESARDR-ATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFIThDLGVVAKIADRVAVMYAGKIV 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-261 |
2.58e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 3 DTAIFRIAGLTkafgpnaVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAG 82
Cdd:PRK10575 15 RNVSFRVPGRT-------LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE-SWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 83 VVTVHQNindgvvgaLDVASNLVLDRLNGAGS-------GFFfnPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMV 155
Cdd:PRK10575 87 VAYLPQQ--------LPAAEGMTVRELVAIGRypwhgalGRF--GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDEKPLD 234
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
250 260
....*....|....*....|....*..
gi 1998276353 235 YEGAVNAMLGQNLGLhsIDARAAGAPV 261
Cdd:PRK10575 237 RGETLEQIYGIPMGI--LPHPAGAAPV 261
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-222 |
2.79e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 20 AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG--------VHR-ADRGVMMLGDRPFSPatpaeamragvvtvhqni 90
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgrIARpAGARVLFLPQRPYLP------------------ 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 ndgvVGALdvASNLVLDRLNGAGSgfffnprkvRREAREVAERMGLG--IDLSAEVTD----LPLADRQMVAIARAMAHE 164
Cdd:COG4178 439 ----LGTL--REALLYPATAEAFS---------DAELREALEAVGLGhlAERLDEEADwdqvLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIdRLRARGVAILYISHRmSDIRRLADRIVSLRDG 222
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLL-REELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
263-456 |
3.39e-13 |
|
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: 68.15 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 263 SARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPasaIRDGVFLVA 338
Cdd:TIGR01189 2 AARNLACSRGERMlfegLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD---EPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 339 KDRAstGIVPEFNIYENmsLPFLPRFSnmsvtrrRAERQTAREQIADLKIVCRSERdDLATLSGGNQQKVTVARWLTQPS 418
Cdd:TIGR01189 79 GHLP--GLKPELSALEN--LHFWAAIH-------GGAQRTIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1998276353 419 RLLILDEPFQGVDIAARHDIAAKLRESARdRATLVFLT 456
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLA-RGGIVLLT 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
247-474 |
3.65e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 247 LGLHSIDARAAGAPVFSArdlriapgakpLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTP 326
Cdd:PRK11248 2 LQISHLYADYGGKPALED-----------INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 327 ASAIRDGVFlvakdrASTGIVPEFNIYENMSlpFLPRFSNMSVTRRRaerQTAREQIADLKIVCRSERDdLATLSGGNQQ 406
Cdd:PRK11248 68 PGAERGVVF------QNEGLLPWRNVQDNVA--FGLQLAGVEKMQRL---EIAHQMLKKVGLEGAEKRY-IWQLSGGQRQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 407 KVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT--ELDEALETADRILVMSEN 474
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIthDIEEAVFMATELVLLSPG 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
259-485 |
3.73e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 259 APVFSARDLRIAPGAKPL----SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRdgv 334
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVldgvDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 335 fLVAKDRASTGIVPEFN---IYENMSLPFLPRFSNMSVTRRRAERQtAREQIADLKIVCRserdDLATLSGGNQQKVTVA 411
Cdd:PRK09536 78 -RVASVPQDTSLSFEFDvrqVVEMGRTPHRSRFDTWTETDRAAVER-AMERTGVAQFADR----PVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 412 RWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLTELDEALETADRILVMSENTIVGEHRNADV 485
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-258 |
4.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.39 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPF---SPATPAEAMRAGVVTVHQNINDgvvgal 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVFQFPES------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLVLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLsAEVTDLPLADRQM--VAIARAMAHEPQVMILDEPTSS 176
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESL-FEKNPFELSGGQMrrVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 177 LSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVgqFDEKPLDYEGAVNAMLGQNLGLHSIDARA 256
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV--LSGKPKDIFQDVDFLEEKQLGVPKITKFA 253
|
..
gi 1998276353 257 AG 258
Cdd:PRK13649 254 QR 255
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
253-471 |
4.76e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 71.16 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 253 DARAAGAPVFSARDLRIA-----PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPA 327
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAypgrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 328 SaIRDGVFLVAKdrasTGIVPEFNIYENMSLpFLPRFSNMSVtRRRAERQTAREQIADLKIVCRSERDDLAT-LSGGNQQ 406
Cdd:TIGR02857 393 S-WRDQIAWVPQ----HPFLFAGTIAENIRL-ARPDASDAEI-REALERAGLDEFVAALPQGLDTPIGEGGAgLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 407 KVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVM 471
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR-TVLLVTHRLALAALADRIVVL 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-225 |
4.84e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE-AMRAGVVTV 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINdgvvgaldvaSNLVLDRLNGAGsgfffnpR------KVRREAREVaermglgIDLSAEVTDL-PLAD-------- 151
Cdd:COG4604 83 ENHIN----------SRLTVRELVAFG-------RfpyskgRLTAEDREI-------IDEAIAYLDLeDLADryldelsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 152 --RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHrmsDIR---RLADRIVSLRDGAIV 225
Cdd:COG4604 139 gqRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH---DINfasCYADHIVAMKDGRVV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-225 |
5.19e-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: 67.94 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVH--RADRGVMMLGDRPFSPATPAEAMRAGVVTV 86
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQN---InDGVVgaldvasnlVLDRLNGAGSGFFFNPRKvRREarevaermglgidlsaevtdlpladrqmvaIARAMAH 163
Cdd:cd03217 83 FQYppeI-PGVK---------NADFLRYVNEGFSGGEKK-RNE------------------------------ILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRmsdiRRLADRIVS-----LRDGAIV 225
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLLDYIKPdrvhvLYDGRIV 184
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
276-480 |
5.96e-13 |
|
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: 68.28 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAirdgvflvakdRASTGIVPEFNIYEN 355
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL-----------RRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPFLPRFSNMSVTRRR----AERQTAREQIADL-----KIVcrSERDdlATLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:cd03252 90 RSIRDNIALADPGMSMERvieaAKLAGAHDFISELpegydTIV--GEQG--AGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 427 FQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV--GEH 480
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVeqGSH 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-227 |
6.11e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGP-NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGVVTVH 87
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QninDGVVGALDVASNLVLDRlngagsgfFFNPRKVRR--EAREVAERM-----GLGIDLSAEVTDLPLADRQMVAIARA 160
Cdd:PRK10790 422 Q---DPVVLADTFLANVTLGR--------DISEEQVWQalETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILyISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV-IAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-230 |
6.25e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA-GVV---------TVHQNIN 91
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNiAVVfqdaglfnrSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 92 DGVVGALDVASNLVLDRlnGAGSGFFFnpRKVRREAREVAERmglGIDLSAevtdlplADRQMVAIARAMAHEPQVMILD 171
Cdd:PRK13657 431 VGRPDATDEEMRAAAER--AQAHDFIE--RKPDGYDTVVGER---GRQLSG-------GERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 172 EPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIV--GQFDE 230
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVesGSFDE 555
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-225 |
7.24e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVH-------RADRGVMMLGDRPFSpaTPAEA 78
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQ--IDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRAGVVTVHQNINDgvVGALDVASNLVLDrLNGAGsgfFFNPRKVRREAREVAERMGLGID----LSAEVTDLPLADRQM 154
Cdd:PRK14246 88 LRKEVGMVFQQPNP--FPHLSIYDNIAYP-LKSHG---IKEKREIKKIVEECLRKVGLWKEvydrLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 155 VAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
276-477 |
7.27e-13 |
|
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: 68.00 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASaIRDGVFLVAKDrastgiVPEFN--IY 353
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQD------VTLFYgtLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLpflprfSNMSVTRRR----AERQTAREQIA------DLKIvcrSERDDLatLSGGNQQKVTVARWLTQPSRLLIL 423
Cdd:cd03245 96 DNITL------GAPLADDERilraAELAGVTDFVNkhpnglDLQI---GERGRG--LSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 424 DEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSENTIV 477
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-225 |
7.52e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGV-----MMLGDRPFSPATPAEAMRAGVVTV 86
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINDGVVGALDvasnlvlDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPL----ADRQMVAIARAMA 162
Cdd:PRK14271 107 FQRPNPFPMSIMD-------NVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFrlsgGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 163 HEPQVMILDEPTSSLSSNEAERLFALIDRLRARgVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
270-476 |
7.76e-13 |
|
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: 66.47 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 270 APGAKP-----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPaSAIRDGVFLVAKDrast 344
Cdd:cd03246 10 YPGAEPpvlrnVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYLPQD---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 givpefniyenMSLpflprFSNmsvtrrraerqTAREQIadlkivcrserddlatLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:cd03246 85 -----------DEL-----FSG-----------SIAENI----------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTI 476
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
260-500 |
8.98e-13 |
|
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: 68.19 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAG-SMQLDGRayapRTPASAIRDgv 334
Cdd:COG1119 2 PLLELRNVTVRRGGKTilddISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE----RRGGEDVWE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 335 fLvakdRASTGIV-PEfniyenMSLPFLPRFS--NM-------SVTRRR----AERQTAREQIADLKIVCRSERDdLATL 400
Cdd:COG1119 76 -L----RKRIGLVsPA------LQLRFPRDETvlDVvlsgffdSIGLYReptdEQRERARELLELLGLAHLADRP-FGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 401 SGGNQQKVTVARWL-TQPsRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:COG1119 144 SQGEQRRVLIARALvKDP-ELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVThHVEEIPPGITHVLLLKDGRVV 222
|
250 260
....*....|....*....|...
gi 1998276353 478 GEHRNADVDMDRLLAEVAGQRLE 500
Cdd:COG1119 223 AAGPKEEVLTSENLSEAFGLPVE 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
276-477 |
9.93e-13 |
|
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: 70.63 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAirdgvflvakdRASTGIVPE----FN 351
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-----------RRQIGVVLQdvflFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 --IYENMSLpFLPRFSNMSVtrRRAERQT-AREQIA------DLKIvcrSERDdlATLSGGNQQKVTVAR-WLTQPsRLL 421
Cdd:COG2274 563 gtIRENITL-GDPDATDEEI--IEAARLAgLHDFIEalpmgyDTVV---GEGG--SNLSGGQRQRLAIARaLLRNP-RIL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSENTIV 477
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGR-TVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
262-477 |
1.07e-12 |
|
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: 67.59 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 262 FSARDLRIAPGA----KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIH-----APLAGSMQLDGRAyaprtpasaIRD 332
Cdd:cd03260 1 IELRDLNVYYGDkhalKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKD---------IYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 333 GVFLVAKDRASTGIV----PEFN--IYENMSLPflPRFSNMSVTRRRAERQTAREQIADLKivcRSERDDLA--TLSGGN 404
Cdd:cd03260 72 LDVDVLELRRRVGMVfqkpNPFPgsIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALW---DEVKDRLHalGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 405 QQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLREsARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVThNMQQAARVADRTAFLLNGRLV 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-236 |
1.29e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE----AM 79
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGV-----VTVHQNIndgvvgaldvASNLVLDRLNGAgsgfffnprkvrrearEVAERMGLGIDL-------SAEVTDL 147
Cdd:PRK11607 97 FQSYalfphMTVEQNI----------AFGLKQDKLPKA----------------EIASRVNEMLGLvhmqefaKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 148 PLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERL-FALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVg 226
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV- 229
|
250
....*....|
gi 1998276353 227 QFDEKPLDYE 236
Cdd:PRK11607 230 QIGEPEEIYE 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-225 |
1.39e-12 |
|
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: 67.26 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATpAEAMRA--GVV---------TVHQN 89
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRaiGVVpqdtvlfndTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 90 I--------NDGVVGALDVASnlVLDRLNGAGSGFffnprkvrreAREVAERmglGIDLSAevtdlplADRQMVAIARAM 161
Cdd:cd03253 95 IrygrpdatDEEVIEAAKAAQ--IHDKIMRFPDGY----------DTIVGER---GLKLSG-------GEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
274-480 |
1.46e-12 |
|
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: 67.26 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasaIRDgvflVAKD--RASTGIVPE-- 349
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---------IRE----VTLDslRRAIGVVPQdt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 --FN--IYENMslpflpRFSNMSVTRRRAERQTAREQIADlKIVcrSERDDLAT--------LSGGNQQKVTVARWLTQP 417
Cdd:cd03253 85 vlFNdtIGYNI------RYGRPDATDEEVIEAAKAAQIHD-KIM--RFPDGYDTivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 418 SRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALeTADRILVMSENTIV--GEH 480
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIV-NADKIIVLKDGRIVerGTH 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-225 |
1.54e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG--VHRADRGVMMLGDRPFSPATPAEAMRAGV------------VTV 86
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAGIflafqypveipgVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 hqnindgvvgaldvaSNLvLDRLNGAGSGFFFNPRKVRREAREVAERMGLGIDLsaevtdlplADRQMVA---------- 156
Cdd:COG0396 95 ---------------SNF-LRTALNARRGEELSAREFLKLLKEKMKELGLDEDF---------LDRYVNEgfsggekkrn 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 157 -IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRmsdiRRL-----ADRIVSLRDGAIV 225
Cdd:COG0396 150 eILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY----QRIldyikPDFVHVLVDGRIV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-225 |
1.69e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.66 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRAGVVTVHQNI---NDgvvgal 98
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA-SLRNQVALVSQNVhlfND------ 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLVLDRLNgagsgfffnprKVRREAREVAERM------------GL-------GIDLSAevtdlplADRQMVAIAR 159
Cdd:PRK11176 432 TIANNIAYARTE-----------QYSREQIEEAARMayamdfinkmdnGLdtvigenGVLLSG-------GQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSnEAER-LFALIDRLRaRGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:PRK11176 494 ALLRDSPILILDEATSALDT-ESERaIQAALDELQ-KNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-227 |
1.98e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSGVHRADrGVMMLGDRPFSPATPAE-AMRAGVVTVHQNindgVVGALDVASNLVLD 107
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAElARHRAYLSQQQT----PPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 108 RLNGAgsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIA-------RAMAHEPQVMILDEPTSSLSSN 180
Cdd:PRK03695 94 QPDKT------RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 181 EAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-222 |
2.05e-12 |
|
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: 64.78 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADrgvmmlgdrpfspatpaeamrAGVVTVH 87
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD---------------------EGIVTWG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 88 QNINDGVVGALdvasnlvldrlngagSGfffnprkvrrearevAERMglgidlsaevtdlpladRqmVAIARAMAHEPQV 167
Cdd:cd03221 61 STVKIGYFEQL---------------SG---------------GEKM-----------------R--LALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 168 MILDEPTSSLSsneAERLFALIDRLRARGVAILYISHrmsD---IRRLADRIVSLRDG 222
Cdd:cd03221 92 LLLDEPTNHLD---LESIEALEEALKEYPGTVILVSH---DryfLDQVATKIIELEDG 143
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-227 |
2.14e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAF--GPNAV--LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRA-- 81
Cdd:PRK11153 3 ELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 --GVVTVHQNIndgvVGALDVASNLVLD-RLNGAgsgfffNPRKVRREAREVAERMGLgidlsaevTDLplADR------ 152
Cdd:PRK11153 83 qiGMIFQHFNL----LSSRTVFDNVALPlELAGT------PKAEIKARVTELLELVGL--------SDK--ADRypaqls 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 153 ----QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK11153 143 ggqkQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
276-481 |
2.29e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 66.49 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasaIRDgvFLVAKDRASTGIVPE----FN 351
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---------VRD--YTLASLRRQIGLVSQdvflFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 --IYENMslpflpRFSNMSVTRRRAERqtAREQIADLKIVCRSER-------DDLATLSGGNQQKVTVARWLTQPSRLLI 422
Cdd:cd03251 90 dtVAENI------AYGRPGATREEVEE--AARAANAHEFIMELPEgydtvigERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 423 LDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV--GEHR 481
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRL-STIENADRIVVLEDGKIVerGTHE 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-225 |
2.31e-12 |
|
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: 65.65 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 20 AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHR--ADRGVMMLGDRPFSPATPAEAMraGVVTVHqninDGVVGA 97
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKII--GYVPQD----DILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 LDVasnlvldrlngagsgfffnprkvrREArevaermglgIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSL 177
Cdd:cd03213 97 LTV------------------------RET----------LMFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 178 SSNEAERLFALIDRLRARGVAILYISHRMS-DIRRLADRIVSLRDGAIV 225
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-224 |
2.42e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGV- 83
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 -----------VTVHQNIndgvvgaLDVASNLVLDRlngagsgfffnpRKVRREAREVAERMGL-------GIDLS-AEv 144
Cdd:COG1137 82 ylpqeasifrkLTVEDNI-------LAVLELRKLSK------------KEREERLEELLEEFGIthlrkskAYSLSgGE- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 145 tdlpladRQMVAIARAMAHEPQVMILDEPtsslssneaerlFALID------------RLRARGVAILYISHRMSDIRRL 212
Cdd:COG1137 142 -------RRRVEIARALATNPKFILLDEP------------FAGVDpiavadiqkiirHLKERGIGVLITDHNVRETLGI 202
|
250
....*....|..
gi 1998276353 213 ADRIVSLRDGAI 224
Cdd:COG1137 203 CDRAYIISEGKV 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
267-494 |
2.46e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 267 LRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRA 342
Cdd:PRK11231 8 LTVGYGTKRilndLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 343 STGI-VPEFNIYENMslPFLPRFSNMSVT-RRRAERQTAREQIADLkivcrSERDdLATLSGGNQQKVTVARWLTQPSRL 420
Cdd:PRK11231 88 PEGItVRELVAYGRS--PWLSLWGRLSAEdNARVNQAMEQTRINHL-----ADRR-LTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 421 LILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEV 494
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTV 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-235 |
2.85e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAmraGVVTVHq 88
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAER---GVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 ninDGVVGALDVASNLVLD-RLNGAGsgfffnprkvRREAREVAERMGLGIDLS-AE---VTDLPLADRQMVAIARAMAH 163
Cdd:PRK11248 79 ---EGLLPWRNVQDNVAFGlQLAGVE----------KMQRLEIAHQMLKKVGLEgAEkryIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAivGQFDEK-PLDY 235
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGP--GRVVERlPLNF 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-205 |
3.00e-12 |
|
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: 68.93 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQNINdgvVG 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQDAH---LF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 ALDVASNLVLDRLNGAGSgfffnprkvrrEAREVAERMGLGIDLSA--EVTDLPL---------ADRQMVAIARAMAHEP 165
Cdd:TIGR02868 422 DTTVRENLRLARPDATDE-----------ELWAALERVGLADWLRAlpDGLDTVLgeggarlsgGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 166 QVMILDEPTSSLSSNEAERLFA-LIDRLRARGVaiLYISHR 205
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEdLLAALSGRTV--VLITHH 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-225 |
3.18e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSgvHRADRGVMMLGDRPFSpATPAEA--MRAGVVTVHQNinDGVVGALD 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA--FRSPKGVKGSGSVLLN-GMPIDAkeMRAISAYVQQD--DLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASNLV------LDRLNgagsgfffnPRKVRREA-REVAERMGLG------IDLSAEVTDLPLADRQMVAIARAMAHEPQ 166
Cdd:TIGR00955 116 VREHLMfqahlrMPRRV---------TKKEKRERvDEVLQALGLRkcantrIGVPGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARG-VAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-225 |
4.59e-12 |
|
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: 65.13 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPN--AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTV 86
Cdd:cd03369 9 VENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQninDGVVGALDVASNLvlDRLNGagsgffFNPRKVRrEAREVAERmglGIDLSAevtdlplADRQMVAIARAMAHEPQ 166
Cdd:cd03369 88 PQ---DPTLFSGTIRSNL--DPFDE------YSDEEIY-GALRVSEG---GLNLSQ-------GQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 167 VMILDEPTSSLSSnEAERLFALIDRLRARGVAILYISHRMSDIRRLaDRIVSLRDGAIV 225
Cdd:cd03369 146 VLVLDEATASIDY-ATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
276-486 |
4.70e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 66.37 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAS--AIRDGVFLVAKDRASTgIVPEFNIY 353
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrAFRRDVQLVFQDSPSA-VNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPfLPRFSNMSVTRRRAERQTAREQIaDLkivcRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVD 431
Cdd:TIGR02769 109 QIIGEP-LRHLTSLDESEQKARIAELLDMV-GL----RSEDADKlpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 432 IAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTIVGEHRNADVD 486
Cdd:TIGR02769 183 MVLQAVILELLRKlQQAFGTAYLFIThDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-227 |
4.73e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.02 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRAdRGVMMLGDRPFSPATPAEA--MRA---------GVVTVHQNI 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELarHRAylsqqqsppFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 ndgvvgALDVASNLVLDrlngagsgfffnprKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAH------- 163
Cdd:COG4138 91 ------ALHQPAGASSE--------------AVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 164 EPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAS 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
265-473 |
5.16e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.20 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGAKPL----SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAP---LAGSMQLDGRAYAPrtpasairdgvfLV 337
Cdd:COG4136 5 ENLTITLGGRPLlaplSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA------------LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 338 AKDRAsTGIV-------PEFNIYENmsLPF-LPRfsnmsvTRRRAERQTAREQ-IADLKIVCRSERDdLATLSGGNQQKV 408
Cdd:COG4136 73 AEQRR-IGILfqddllfPHLSVGEN--LAFaLPP------TIGRAQRRARVEQaLEEAGLAGFADRD-PATLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 409 TVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEA-LETADRILVMSE 473
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEdAPAAGRVLDLGN 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
274-479 |
5.35e-12 |
|
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: 64.26 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayaprTPASAIRDGVflvakdRASTGIVPE---- 349
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG------VPVSDLEKAL------SSLISVLNQrpyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FN--IYENMSLPFlprfsnmsvtrrraerqtareqiadlkivcrserddlatlSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:cd03247 87 FDttLRNNLGRRF----------------------------------------SGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSENTIVGE 479
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLKDK-TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
261-485 |
6.25e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 65.30 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 261 VFSARDlRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRdgvflvaKD 340
Cdd:cd03258 10 VFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-LLSGKELR-------KA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 341 RASTGIV-PEFN------IYENMSLPFLPRFSNMSVTRRRAERQtareqiadLKIVCRSERDDL--ATLSGGNQQKVTVA 411
Cdd:cd03258 81 RRRIGMIfQHFNllssrtVFENVALPLEIAGVPKAEIEERVLEL--------LELVGLEDKADAypAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 412 RWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIVGEHRNADV 485
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLIThEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-225 |
6.34e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLG----------DRPfspat 74
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 75 paeamRAGVVTVHQNINDGV--VGAL---------DVA-----SNL--------VLDRLNGAgsgfffnprkvRREAR-- 128
Cdd:PRK11147 77 -----RNVEGTVYDFVAEGIeeQAEYlkryhdishLVEtdpseKNLnelaklqeQLDHHNLW-----------QLENRin 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 129 EVAERMGLgiDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIdrLRARGvAILYISHRMSD 208
Cdd:PRK11147 141 EVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISHDRSF 215
|
250
....*....|....*..
gi 1998276353 209 IRRLADRIVSLRDGAIV 225
Cdd:PRK11147 216 IRNMATRIVDLDRGKLV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-214 |
6.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEA------MRA 81
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERrvnlnrLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVHQNINdgvVGALDVASNLVLD-RLNGagsgffFNPRkvrREAREVAERMGLGIDLSAEVT--------DLPLADR 152
Cdd:PRK14258 89 QVSMVHPKPN---LFPMSVYDNVAYGvKIVG------WRPK---LEIDDIVESALKDADLWDEIKhkihksalDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARG-VAILYISHRMSDIRRLAD 214
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
272-471 |
6.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 272 GAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRdgvflvaKDRASTGIV---P 348
Cdd:PRK13641 22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVSLVfqfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLP---FLPRfsNMSVTRRRAERQTareqIADLKIVCRSErdDLAT-----LSGGNQQKVTVARWLTQPSRL 420
Cdd:PRK13641 95 EAQLFENTVLKdveFGPK--NFGFSEDEAKEKA----LKWLKKVGLSE--DLISkspfeLSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 421 LILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTE-LDEALETADRILVM 471
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHnMDDVAEYADDVLVL 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-222 |
7.27e-12 |
|
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: 64.19 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSGvhRADRGV----MMLGDRPFSPATPAEAmragvvtvhqnindGVVGALDVasnl 104
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVitgeILINGRPLDKNFQRST--------------GYVEQQDV---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 105 vldrlngagsgffFNPRKVRREArevaermglgIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAER 184
Cdd:cd03232 90 -------------HSPNLTVREA----------LRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1998276353 185 LFALIDRLRARGVAILYISHRMS-DIRRLADRIVSLRDG 222
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
274-471 |
7.96e-12 |
|
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: 64.58 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASaiRDgVFLVAKDRAstgIVPEFNIY 353
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RD-IAMVFQNYA---LYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPFLPRFSNMSVTRRRAeRQTAR----EQIADLKIvcrserddlATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:cd03301 91 DNIAFGLKLRKVPKDEIDERV-REVAEllqiEHLLDRKP---------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 430 VDiaarhdiaAKLRESARDR---------ATLVFLT-ELDEALETADRILVM 471
Cdd:cd03301 161 LD--------AKLRVQMRAElkrlqqrlgTTTIYVThDQVEAMTMADRIAVM 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-470 |
8.18e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSGVHRADrgvmmLGDrPFSPATPAEAMRA----------------GVVTVH--QNI 90
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGD-YEEEPSWDEVLKRfrgtelqnyfkklyngEIKVVHkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 N------DGVVGALdvasnlvLDRLNGAGsgfffnprkvrrEAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHE 164
Cdd:PRK13409 170 DlipkvfKGKVREL-------LKKVDERG------------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRLADR------------IVSLRDGAIVG------ 226
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNvhiaygepgaygVVSKPKGVRVGineylk 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 227 --------QFDEKPLDYEgavnamlgqnlgLHSIDARAAGAPVFSARDLRIAPGAKPLSMELG---AGEVVAVTGLVGVG 295
Cdd:PRK13409 310 gylpeenmRIRPEPIEFE------------ERPPRDESERETLVEYPDLTKKLGDFSLEVEGGeiyEGEVIGIVGPNGIG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 296 KTRLAETLFGIHAPLAGSMQLDGR-AYAPR--TPASAIRDGVFL--VAKDRASTGIVPEfnIYENMSLpflprfsnmsvt 370
Cdd:PRK13409 378 KTTFAKLLAGVLKPDEGEVDPELKiSYKPQyiKPDYDGTVEDLLrsITDDLGSSYYKSE--IIKPLQL------------ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 371 rrraerqtarEQIADLKivcrserddLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRA 450
Cdd:PRK13409 444 ----------ERLLDKN---------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEERE 504
|
490 500
....*....|....*....|..
gi 1998276353 451 TLVFLTELDEALE--TADRILV 470
Cdd:PRK13409 505 ATALVVDHDIYMIdyISDRLMV 526
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
276-499 |
8.82e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYapRTPASAIRDgvflvakDRASTGIV-PEFNIYE 354
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERL-------IRQEAGMVfQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMS----LPFLPRfsnmsvTRRRAERQTAREQIADL-KIVCRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:PRK09493 91 HLTalenVMFGPL------RVRGASKEEAEKQARELlAKVGLAERAHHypSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVgehrnADVDMDRLLAEVAGQRL 499
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVThEIGFAEKVASRLIFIDKGRIA-----EDGDPQVLIKNPPSQRL 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
271-500 |
1.10e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLS---MELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDrasTGIV 347
Cdd:PRK10762 15 PGVKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQE---LNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFNIYENMSL--PFLPRFSNMSVTRRRAErqtAREQIADLKiVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK10762 92 PQLTIAENIFLgrEFVNRFGRIDWKKMYAE---ADKLLARLN-LRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 426 P---FQGVDIAARHDIAAKLRESARDratLVFLTE-LDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQRLE 500
Cdd:PRK10762 168 PtdaLTDTETESLFRVIRELKSQGRG---IVYISHrLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLE 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-230 |
1.14e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSGVhRADRGVMMLGDRPFSPATPAEAMR------------AGvvTVHQNINDGVVG 96
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKhlswvgqnpqlpHG--TLRDNVLLGNPD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 ALDVASNLVLDRLNgagsgfffnprkvrreAREVAERMGLGIDLsaevtdlPLADR---------QMVAIARAMAHEPQV 167
Cdd:PRK11174 450 ASDEQLQQALENAW----------------VSEFLPLLPQGLDT-------PIGDQaaglsvgqaQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 168 MILDEPTSSLSSNEAERLFALIDRLrARGVAILYISHRMSDIRRLaDRIVSLRDGAIV--GQFDE 230
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVqqGDYAE 569
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
276-485 |
1.17e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 66.29 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRtpasaiRDGVFLVAKDRAsTGIVpefniYEN 355
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDS------RKGIFLPPEKRR-IGYV-----FQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSL-PFLPRFSNMSVTRRRA---ERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVD 431
Cdd:TIGR02142 84 ARLfPHLSVRGNLRYGMKRArpsERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 432 IAARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMSENTIVGEHRNADV 485
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVShSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
274-477 |
1.18e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.89 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAiRDgvflvakdrasTGIVpefniY 353
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEK-RN-----------VGMV-----F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLpflprFSNMSV--------TRRRAERQTAREQIAD-LKIVcrsERDDLA-----TLSGGNQQKVTVARWL-TQPs 418
Cdd:COG3842 84 QDYAL-----FPHLTVaenvafglRMRGVPKAEIRARVAElLELV---GLEGLAdryphQLSGGQQQRVALARALaPEP- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 419 RLLILDEPFQGVDiaarhdiaAKLRESARD---------RATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:COG3842 155 RVLLLDEPLSALD--------AKLREEMREelrrlqrelGITFIYVThDQEEALALADRIAVMNDGRIE 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
264-481 |
1.28e-11 |
|
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: 66.77 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 264 ARDLRIAPGA-----------------KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtp 326
Cdd:COG5265 348 APPLVVGGGEvrfenvsfgydperpilKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 327 asaIRDgvflVAKD--RASTGIVPE----FN--IYENMslpflpRFSNMSVTRRRAERQTAREQIADLkIvcRSERDDLA 398
Cdd:COG5265 422 ---IRD----VTQAslRAAIGIVPQdtvlFNdtIAYNI------AYGRPDASEEEVEAAARAAQIHDF-I--ESLPDGYD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 399 T--------LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFlteldeA--LET---A 465
Cdd:COG5265 486 TrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI------AhrLSTivdA 559
|
250
....*....|....*...
gi 1998276353 466 DRILVMSENTIV--GEHR 481
Cdd:COG5265 560 DEILVLEAGRIVerGTHA 577
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
276-471 |
1.30e-11 |
|
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: 63.64 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR-AYAPRTP----ASaIRDgvflvakdrastgivpef 350
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVSQEPwiqnGT-IRE------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 NIYenMSLPFLPRFSNMSVtrrraeRQTAREQiaDLKIVcrsERDDL-------ATLSGGNQQKVTVARWLTQPSRLLIL 423
Cdd:cd03250 85 NIL--FGKPFDEERYEKVI------KACALEP--DLEIL---PDGDLteigekgINLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 424 DEPFQGVDIAARHDIAAK-LRESARDRATLVFLTELDEALETADRILVM 471
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
263-477 |
1.37e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 263 SARDLRI-----APGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIhAPLAGSMQLDG------------RAYA--- 322
Cdd:PRK11174 351 EAEDLEIlspdgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGielreldpeswrKHLSwvg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 323 --PRTPASAIRDGVfLVAKDRAStgivpEFNIYENMSLPFLPRFSNMSvtrrraerqtarEQIADLKIvcrseRDDLATL 400
Cdd:PRK11174 430 qnPQLPHGTLRDNV-LLGNPDAS-----DEQLQQALENAWVSEFLPLL------------PQGLDTPI-----GDQAAGL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 401 SGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLvFLTELDEALETADRILVMSENTIV 477
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTL-MVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-225 |
1.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQNINDGVVGAL-- 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATIve 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 -DVA---SNLVLDrlngagsgfffnPRKVRREAREVAERMGLgidlsAEVTD-----LPLADRQMVAIARAMAHEPQVMI 169
Cdd:PRK13633 105 eDVAfgpENLGIP------------PEEIRERVDESLKKVGM-----YEYRRhaphlLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 170 LDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
276-479 |
1.52e-11 |
|
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: 63.93 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyAPRTPASAIRDGVFLvakdRASTGIVPEFNIYEN 355
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARRRLGFV----SDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 msLPFLPRFSNMsvtrRRAERQTAREQIAD-LKIVCRSERDdLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAA 434
Cdd:cd03266 99 --LEYFAGLYGL----KGDELTARLEELADrLGMEELLDRR-VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 435 RHDIAAKLRESARDRATLVFLTE-LDEALETADRILVMSENTIVGE 479
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHiMQEVERLCDRVVVLHRGRVVYE 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-243 |
1.55e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATpAEAMRAGVVTVHQninDGVVGALDV 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQ---EPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLvldrlngaGSGFFFNP----RKVRREAREVAERMGLGIDLSAEV----TDLPLADRQMVAIARAMAHEPQVMILDE 172
Cdd:TIGR00958 572 RENI--------AYGLTDTPdeeiMAAAKAANAHDFIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 173 PTSSLssnEAERLFALIDRLRARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQFDEKPLDYEGAVNAML 243
Cdd:TIGR00958 644 ATSAL---DAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
277-477 |
2.21e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsaiRDGVFLVAKDrasTGIVPEFNIYENM 356
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQE---NNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 357 SLPFLPRFsnmsvtRRRAERQTAREQIADlkivcRSERDDL-----ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVD 431
Cdd:PRK10771 93 GLGLNPGL------KLNAAQREKLHAIAR-----QMGIEDLlarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 432 IAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERQlTLLMVShSLEDAARIAPRSLVVADGRIA 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
276-479 |
2.38e-11 |
|
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: 63.72 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRASTGIVpefniyen 355
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ------------DITKLPMHKRARLGIG-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 mslpFLPR----FSNMSV-----------TRRRAERQTAREQ-IADLKIvcRSERDDLA-TLSGGNQQKVTVARWLTQPS 418
Cdd:cd03218 79 ----YLPQeasiFRKLTVeenilavleirGLSKKEREEKLEElLEEFHI--THLRKSKAsSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 419 RLLILDEPFQGVDIAARHDIAAKLREsARDRATLVFLTE--LDEALETADRILVMSENTIVGE 479
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDhnVRETLSITDRAYIIYEGKVLAE 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
276-479 |
2.59e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRastgivpefNIYEN 355
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGR---------RVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPflprfSNMSVTRRRAERQTAREQIA---DLKIVCRSERDDLA-TLSGGNQQKVTVARWLTQPSRLLILDEPFQG-- 429
Cdd:PRK11614 95 MTVE-----ENLAMGGFFAERDQFQERIKwvyELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGla 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 430 -VDIAARHDIAAKLREsardRATLVFLTE--LDEALETADRILVMSENTIVGE 479
Cdd:PRK11614 170 pIIIQQIFDTIEQLRE----QGMTIFLVEqnANQALKLADRGYVLENGHVVLE 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-431 |
2.73e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 27 LDLRAGEVTVLMGANGAGKSTLVKVMSGvhradRGVMMLGDRPFSPATPA----EAMRAGVVTVHQ-NINDGVVGALD-- 99
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAG-----ELPLLSGERQSQFSHITrlsfEQLQKLVSDEWQrNNTDMLSPGEDdt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 --VASNLVLDrlngagsgfffnprKVRREAR--EVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTS 175
Cdd:PRK10938 99 grTTAEIIQD--------------EVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 176 SLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRD--------------GAIVGQfdekpLDY-EGAVN 240
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADctlaetgereeilqQALVAQ-----LAHsEQLEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 241 AMLGQNLGLHSIDARAAGAPVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAE--------------T 302
Cdd:PRK10938 240 VQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPilhnLSWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndlT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 303 LFG-----------I--H-APLAGSMQLDGRAyaprtpASAIRDgVFLvakdrasTGIVPEFNIYENMSlpflprfsnms 368
Cdd:PRK10938 320 LFGrrrgsgetiwdIkkHiGYVSSSLHLDYRV------STSVRN-VIL-------SGFFDSIGIYQAVS----------- 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 369 vtrrRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVD 431
Cdd:PRK10938 375 ----DRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
274-503 |
2.95e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.10 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASAIRDGVFlvaKDRASTGIV---PE- 349
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKGLM---KLRESVGMVfqdPDn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 ----FNIYENMSLPFLprfsNMSV----TRRRAERQTAREQIADLKivcrseRDDLATLSGGNQQKVTVARWLTQPSRLL 421
Cdd:PRK13636 94 qlfsASVYQDVSFGAV----NLKLpedeVRKRVDNALKRTGIEHLK------DKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQRL 499
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGlTIIIAThDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRL 243
|
....
gi 1998276353 500 EPAG 503
Cdd:PRK13636 244 PRIG 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-221 |
3.17e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.88 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRAD---RGVMMLGDRPFSpATPAEAMRAGVV--TVHQNINdgvvg 96
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT-ALPAEQRRIGILfqDDLLFPH----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 aLDVASNLVldrlngagsgfFFNPRKVRREAR-----EVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILD 171
Cdd:COG4136 91 -LSVGENLA-----------FALPPTIGRAQRrarveQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 172 EPTSSLSSNEAERLFALI-DRLRARGVAILYISHRMSDIrRLADRIVSLRD 221
Cdd:COG4136 159 EPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
151-443 |
3.42e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 151 DRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQFD 229
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 230 EKPLdYEGAVNAMLGQNLglhsiDARAAGAPV---------FSARDLRIA-PGA--------------KPLSMELGAGEV 285
Cdd:PRK15134 241 AATL-FSAPTHPYTQKLL-----NSEPSGDPVplpepasplLDVEQLQVAfPIRkgilkrtvdhnvvvKNISFTLRPGET 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 286 VAVTGLVGVGKTRLAETLFGIHAPlAGSMQLDGRAYAPRTPAS--AIRDGVFLVAKDRASTgIVPEFNIYENMSLPFLPR 363
Cdd:PRK15134 315 LGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDPNSS-LNPRLNVLQIIEEGLRVH 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 364 FSNMSVTRRRAERQTAREQIAdLKIVCRSERDdlATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLR 443
Cdd:PRK15134 393 QPTLSAAQREQQVIAVMEEVG-LDPETRHRYP--AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-477 |
3.78e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.97 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVvavTGLVG---VGKTrlaeTLF----GIHAPLAGSMQLDGRAYAPrtpasairdgvflvaKDRASTGIVP 348
Cdd:COG4152 20 VSFTVPKGEI---FGLLGpngAGKT----TTIriilGILAPDSGEVLWDGEPLDP---------------EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 E-FNIYENMS----LPFLPRFSNMS--VTRRRAERQTAREQIADLKivcrseRDDLATLSGGNQQKV----TVARwltQP 417
Cdd:COG4152 78 EeRGLYPKMKvgeqLVYLARLKGLSkaEAKRRADEWLERLGLGDRA------NKKVEELSKGNQQKVqliaALLH---DP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 418 sRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT---ELDEALetADRILVMSENTIV 477
Cdd:COG4152 149 -ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSShqmELVEEL--CDRIVIINKGRKV 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-222 |
3.86e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPN----AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGdRPFSPATPAE--A 78
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGeVSLVG-QPLHQMDEEAraK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRAGVVT-VHQNINdgVVGALDVASNLVLDRL-NGAgsgfffNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVA 156
Cdd:PRK10584 85 LRAKHVGfVFQSFM--LIPTLNALENVELPALlRGE------SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 157 IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRlADRIVSLRDG 222
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAAR-CDRRLRLVNG 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
274-476 |
4.13e-11 |
|
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: 62.55 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsairdgvflVAKDRASTGIV-PEFNI 352
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN---------INELRQKVGMVfQQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMSLpflprFSNMS---VTRRRAERQTAREQIAD-LKIVCRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:cd03262 88 FPHLTV-----LENITlapIKVKGMSKAEAEERALElLEKVGLADKADAypAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 427 FQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVThEMGFAREVADRVIFMDDGRI 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-219 |
4.17e-11 |
|
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: 61.40 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 27 LDLRAGEVTVLMGANGAGKSTLVKVMSG--------VHR-ADRGVMMLGDRPFSPAtpaeamragvvtvhqnindgvvGA 97
Cdd:cd03223 22 FEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsgrIGMpEGEDLLFLPQRPYLPL----------------------GT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 LdvasnlvldrlngagsgfffnprkvrreaREV-----AERMGLGidlsaevtdlplaDRQMVAIARAMAHEPQVMILDE 172
Cdd:cd03223 80 L-----------------------------REQliypwDDVLSGG-------------EQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1998276353 173 PTSSLSSNEAERLFALidrLRARGVAILYISHRmSDIRRLADRIVSL 219
Cdd:cd03223 118 ATSALDEESEDRLYQL---LKELGITVISVGHR-PSLWKFHDRVLDL 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
276-480 |
4.30e-11 |
|
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: 62.43 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIrdgvflvAKDRASTGIV-------P 348
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAI-------PYLRRKIGVVfqdfrllP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPflprfsnMSVTRrrAERQTAREQIAD-LKIVCRS--ERDDLATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:cd03292 92 DRNVYENVAFA-------LEVTG--VPPREIRKRVPAaLELVGLShkHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETadrilvMSENTIVGEH 480
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT------TRHRVIALER 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
275-477 |
6.25e-11 |
|
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: 61.83 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 275 PLSMELGAGevvaVTGLVG---VGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRASTGIVP-EF 350
Cdd:cd03264 18 GVSLTLGPG----MYGLLGpngAGKTTLMRILATLTPPSSGTIRIDGQ------------DVLKQPQKLRRRIGYLPqEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 NIYENMS----LPFLPRFSNMSVTRRRAERQTAreqiadLKIVCRSERDD--LATLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:cd03264 82 GVYPNFTvrefLDYIAWLKGIPSKEVKARVDEV------LELVNLGDRAKkkIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALE-TADRILVMSENTIV 477
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR-IVILSTHIVEDVEsLCNQVAVLNKGKLV 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-218 |
8.06e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVV 84
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 85 TVHQ--------NINDGVVGALDVASNLVLDRlngagsgfffnpRKVRreAREVAE-------RMGLGIDLSAevtdlpl 149
Cdd:PRK10895 82 YLPQeasifrrlSVYDNLMAVLQIRDDLSAEQ------------REDR--ANELMEefhiehlRDSMGQSLSG------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 150 ADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADR--IVS 218
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERayIVS 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-227 |
8.40e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQNIndgvvg 96
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRV------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 alDVASNLVLDRLNGAgsgfffNPRKVRREAREVAERMGLGIDL-SAEVTDLPLAD--RQM-------VAIARAMAHEPQ 166
Cdd:PRK11160 424 --HLFSATLRDNLLLA------APNASDEALIEVLQQVGLEKLLeDDKGLNAWLGEggRQLsggeqrrLGIARALLHDAP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIdRLRARGVAILYISHRMSDIRRLaDRIVSLRDGAIVGQ 227
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELL-AEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
271-479 |
8.54e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.70 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRAS--TGIVP 348
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIY---ENMSLPFLPrfsnmsvTRRRAERQTAreQIADLKIVCRSERddlaTLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK13644 96 EEDLAfgpENLCLPPIE-------IRKRVDRALA--EIGLEKYRHRSPK----TLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTIVGE 479
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-225 |
9.22e-11 |
|
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: 64.07 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAeAMRA--GVV---------TVHQN 89
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA-SLRAaiGIVpqdtvlfndTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 90 INDGVVGAldvasnlvldrlngagsgfffNPRKVRREAR-----------------EVAERmglGIDLSAevtdlplADR 152
Cdd:COG5265 452 IAYGRPDA---------------------SEEEVEAAARaaqihdfieslpdgydtRVGER---GLKLSG-------GEK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSL-SSNEAERLFALidRLRARGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALdSRTERAIQAAL--REVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
283-478 |
1.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDgvflvakDRASTGIV---PEFNIYENMSLP 359
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKP-------LRKKVGIVfqfPEHQLFEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 360 ---FLPrfSNMSVTRRRAErQTAREQIA----DLKIVCRSERDdlatLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDI 432
Cdd:PRK13634 106 dicFGP--MNFGVSEEDAK-QKAREMIElvglPEELLARSPFE----LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 433 AARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTIVG 478
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGlTTVLVThSMEDAARYADQIVVMHKGTVFL 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
255-481 |
1.14e-10 |
|
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: 63.97 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 255 RAAGAPVFSARDLRIAPGakplsmelgagEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASaIRDGV 334
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPG-----------ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 335 FLVAKDrastgiVPEFN--IYENMSLPFLPRFSNMSVtRRRAERQTAREQIADLKIVCRSE-RDDLATLSGGNQQKVTVA 411
Cdd:TIGR02203 409 ALVSQD------VVLFNdtIANNIAYGRTEQADRAEI-ERALAAAYAQDFVDKLPLGLDTPiGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 412 RWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV--GEHR 481
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL-STIEKADRIVVMDDGRIVerGTHN 552
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-217 |
1.28e-10 |
|
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: 63.65 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGpNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDR-PFSPatpaeamragvvtvhQNI 90
Cdd:COG1245 347 LTKSYG-GFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKiSYKP---------------QYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 N---DGVVGALdvasnlvLDRLNGA--GSGFFFNprkvrrearEVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEP 165
Cdd:COG1245 411 SpdyDGTVEEF-------LRSANTDdfGSSYYKT---------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 166 QVMILDEPTSSLSSNeaERLFA--LIDRL-RARGVAILYISHRMSDIRRLADRIV 217
Cdd:COG1245 475 DLYLLDEPSAHLDVE--QRLAVakAIRRFaENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-219 |
1.33e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 2 GDTAIfrIA-GLTKAFGP-NAVlRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAM 79
Cdd:NF033858 263 DEPAI--EArGLTMRFGDfTAV-DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGV----------VTVHQnindgvvgaldvasNLVLD-RLngagsgffFNPRKVRREAR--EVAERMGLGIDLSAEVTD 146
Cdd:NF033858 340 RVGYmsqafslygeLTVRQ--------------NLELHaRL--------FHLPAAEIAARvaEMLERFDLADVADALPDS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 147 LPLADRQMVAIARAMAHEPQVMILDEPTSS---LSSNEAERLfaLIDRLRARGVAIlYIS-HRMSDIRRlADRIvSL 219
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGvdpVARDMFWRL--LIELSREDGVTI-FIStHFMNEAER-CDRI-SL 469
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
276-490 |
1.37e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGI---------HAPLAG-SMQLDGRAyaprtpASAIRdgvflvaKDRASTG 345
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagsHIELLGrTVQREGRL------ARDIR-------KSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 346 -IVPEFN------IYENM------SLPF----LPRFSnmSVTRRRAERQTAREQIADLKivcrseRDDLATLSGGNQQKV 408
Cdd:PRK09984 90 yIFQQFNlvnrlsVLENVligalgSTPFwrtcFSWFT--REQKQRALQALTRVGMVHFA------HQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 409 TVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT--ELDEALETADRILVMSENTIVGEHRNADVD 486
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlhQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
....
gi 1998276353 487 MDRL 490
Cdd:PRK09984 242 NERF 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
256-453 |
1.38e-10 |
|
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: 63.53 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 256 AAGAPVFSARDLRIA-PGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrAYAPRTPASAI 330
Cdd:TIGR02868 329 GLGKPTLELRDLSAGyPGAPPvldgVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 331 RDGVFLVAKDR---ASTgivpefnIYENMslpflpRFSNMSVTRRRAERQTAREQIADLkivCRSERDDL--------AT 399
Cdd:TIGR02868 408 RRRVSVCAQDAhlfDTT-------VRENL------RLARPDATDEELWAALERVGLADW---LRALPDGLdtvlgeggAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLV 453
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVL 525
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
260-476 |
1.54e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAiRD--G 333
Cdd:PRK09452 13 PLVELRGISKSFDGKEvisnLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAEN-RHvnT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 334 VFlvakdrASTGIVPEFNIYENMSLPF-LPRFSNMSVTRRRAE--RQTAREQIADLKIvcrserddlATLSGGNQQKVTV 410
Cdd:PRK09452 91 VF------QSYALFPHMTVFENVAFGLrMQKTPAAEITPRVMEalRMVQLEEFAQRKP---------HQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 411 ARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVMSENTI 476
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGiTFVFVThDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-479 |
1.57e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 270 APGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTpASAIRDGVFLVAK--DRASTGIV 347
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-VWDVRRQVGMVFQnpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFNI---YENMSLPflpRfSNMsVTR-RRAERQTAREQIADlkivcrserDDLATLSGGNQQKVTVARWLTQPSRLLIL 423
Cdd:PRK13635 99 VQDDVafgLENIGVP---R-EEM-VERvDQALRQVGMEDFLN---------REPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 424 DEPFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALEtADRILVMSENTIVGE 479
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQlKEQKGITVLSIThDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
274-476 |
1.75e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.95 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASA-----IRDGVFLVAKDRastgIVP 348
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK------PISQyehkyLHSKVSLVGQEP----VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPfLPRFSNMSVTRRrAERQTAREQIADLKIVCRSERDDL-ATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:cd03248 101 ARSLQDNIAYG-LQSCSFECVKEA-AQKAHAHSFISELASGYDTEVGEKgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTI 476
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
272-477 |
1.77e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.74 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 272 GAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVPEFN 351
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 IYENMSlpFLPRFSNMSVTRRRAERQTAREQIAdLKIVCRSERDDLatlSGGNQQKVTVARWLTQPSRLLILDEPFQGVD 431
Cdd:PRK10070 123 VLDNTA--FGMELAGINAEERREKALDALRQVG-LENYAHSYPDEL---SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 432 IAARHDIAAKL-RESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK10070 197 PLIRTEMQDELvKLQAKHQRTIVFIShDLDEAMRIGDRIAIMQNGEVV 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-214 |
2.04e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.90 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAfgpnavLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRAGV 83
Cdd:PRK11308 21 LFKPERLVKA------LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNindgVVGALdvasnlvldrlngagsgfffNPRK----------------VRREAREVAERMGLGIDLSAEVTD- 146
Cdd:PRK11308 95 QIVFQN----PYGSL--------------------NPRKkvgqileepllintslSAAERREKALAMMAKVGLRPEHYDr 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 147 ----LPLADRQMVAIARAMAHEPQVMILDEPTSSLS-SNEAERLFALIDRLRARGVAILYISHRMSDIRRLAD 214
Cdd:PRK11308 151 yphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIAD 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-470 |
2.31e-10 |
|
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: 62.88 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSGVHRADrgvmmLGDrPFSPATPAEAMRA----------------GVVTVH--QNI 90
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPN-----LGD-YDEEPSWDEVLKRfrgtelqdyfkklangEIKVAHkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 N------DGVVGALdvasnlvLDRLNGAGSgfffnprkvrreAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHE 164
Cdd:COG1245 170 DlipkvfKGTVREL-------LEKVDERGK------------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 165 PQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRI------------VSLRDGAIVG------ 226
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVhilygepgvygvVSKPKSVRVGinqyld 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 227 --------QFDEKPLDYEgavnamlgqnlgLHSIDARAAGAPVFSARDLRIAPGAKPLSMELG---AGEVVAVTGLVGVG 295
Cdd:COG1245 311 gylpeenvRIRDEPIEFE------------VHAPRREKEEETLVEYPDLTKSYGGFSLEVEGGeirEGEVLGIVGPNGIG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 296 KTRLAETLFGIHAPLAGSMQLDGR-AYAPRTPASAIRDGV--FL--VAKDRASTGIVpEFNIYENMSLpflprfsnmsvt 370
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEVDEDLKiSYKPQYISPDYDGTVeeFLrsANTDDFGSSYY-KTEIIKPLGL------------ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 371 rrraerqtarEQIADlkivcrserDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRA 450
Cdd:COG1245 446 ----------EKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
490 500
....*....|....*....|..
gi 1998276353 451 TLVFLTELDEALE--TADRILV 470
Cdd:COG1245 507 KTAMVVDHDIYLIdyISDRLMV 528
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
276-477 |
2.38e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 60.36 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFG---IHAPLAGSMQLDGRayaPRTPASAIRDGVFLVAKDRastgIVPEFNI 352
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDI----LLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YEnmSLPF-----LPRFSNMSVTRRRAErQTAREQIADLKIvcrseRDDLAT-LSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:cd03234 99 RE--TLTYtailrLPRKSSDAIRKKRVE-DVLLRDLALTRI-----GGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 427 FQGVDIAARHDIAAKLRESARdRATLVFLT---ELDEALETADRILVMSENTIV 477
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLAR-RNRIVILTihqPRSDLFRLFDRILLLSSGEIV 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
271-473 |
2.42e-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: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYapRTPASAIRDgvflvakdraSTGIVPEF 350
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQ----------SLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 NI-YENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:TIGR01257 1012 NIlFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276353 430 VDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSE 473
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQ 1135
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
276-477 |
2.55e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYaprTPASAIRDgvflVAKDRASTGIV---PEFNI 352
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---TSTSKNKD----IKQIRKKVGLVfqfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMSL---PFLPRfsNMSVTRRRAErQTAREQIADLKIvcrseRDDLAT-----LSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:PRK13649 99 FEETVLkdvAFGPQ--NFGVSQEEAE-ALAREKLALVGI-----SESLFEknpfeLSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRATLVFLTEL-DEALETADRILVMSENTIV 477
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmDDVANYADFVYVLEKGKLV 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
9-225 |
2.63e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAF----GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHR------ADRgvMMLGDRPFSPATPAEA 78
Cdd:PRK15093 6 IRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtADR--MRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 79 MRA---GVVTVHQNINDGVVGALDVASNLVLDRLNGAGSGFF---FNPRKvrREAREVAERMGLGI------DLSAEVTD 146
Cdd:PRK15093 84 RKLvghNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWwqrFGWRK--RRAIELLHRVGIKDhkdamrSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 lplADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK15093 162 ---GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
276-479 |
3.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.95 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRdgvflvaKDRASTGIV---PEFNI 352
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR-------PVRKRIGMVfqfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENM---SLPFLPRFSNMSVtrrraerQTAREQIADLKIVCRSERDDLAT----LSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK13646 99 FEDTverEIIFGPKNFKMNL-------DEVKNYAHRLLMDLGFSRDVMSQspfqMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 426 PFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTIVGE 479
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSlQTDENKTIILVShDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-222 |
3.19e-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: 63.11 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPN---AVLRgVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVT 85
Cdd:TIGR01257 931 VKNLVKIFEPSgrpAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHqnindgvvgaldvasNLVLDRLNGAGSGFFFNPRKVRR------EAREVAERMGLGIDLSAEVTDLPLADRQMVAIAR 159
Cdd:TIGR01257 1010 QH---------------NILFHHLTVAEHILFYAQLKGRSweeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRArGVAILYISHRMSDIRRLADRIVSLRDG 222
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
271-481 |
3.42e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDG---RAYAprtpASAIRDGVFLVAKDrastgiV 347
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYT----LASLRNQVALVSQN------V 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFN--IYENMSLPFLPRFSNMSVtRRRAERQTAREQIADLKivcrserDDLAT--------LSGGNQQKVTVARWLTQP 417
Cdd:PRK11176 427 HLFNdtIANNIAYARTEQYSREQI-EEAARMAYAMDFINKMD-------NGLDTvigengvlLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 418 SRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV--GEHR 481
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL-STIEKADEILVVEDGEIVerGTHA 563
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
276-496 |
3.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRdgvflvaKDRASTGIV---PEFNI 352
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVfqfPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMSL---PFLPRfsNMSVTRRRAERqTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:PRK13643 98 FEETVLkdvAFGPQ--NFGIPKEKAEK-IAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 430 VDIAARHDIaAKLRESARDRA-TLVFLTEL-DEALETADRILVMSENTIVGEHRNADV--DMDRLLAEVAG 496
Cdd:PRK13643 175 LDPKARIEM-MQLFESIHQSGqTVVLVTHLmDDVADYADYVYLLEKGHIISCGTPSDVfqEVDFLKAHELG 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
262-473 |
4.78e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 262 FSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR-AYAPRTP---ASAIRDGV-FL 336
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSwimPGTIKDNIiFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 337 VAKDRAS-TGIVPEFNIYENMSLpfLPRFSNMSVTrrraerqtareqiadlkivcrserDDLATLSGGNQQKVTVARWLT 415
Cdd:TIGR01271 511 LSYDEYRyTSVIKACQLEEDIAL--FPEKDKTVLG------------------------EGGITLSGGQRARISLARAVY 564
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 416 QPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSE 473
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHE 622
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-217 |
5.57e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGpNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGdrpfspatpaeamragvVTVH---Q 88
Cdd:PRK13409 346 LTKKLG-DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------------LKISykpQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 89 NIN---DGVVGALdvasnlvLDRLNGAGSGFFFNPrkvrrearEVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEP 165
Cdd:PRK13409 408 YIKpdyDGTVEDL-------LRSITDDLGSSYYKS--------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 166 QVMILDEPTSSLSSNeaERLFA--LIDRL-RARGVAILYISHRMSDIRRLADRIV 217
Cdd:PRK13409 473 DLYLLDEPSAHLDVE--QRLAVakAIRRIaEEREATALVVDHDIYMIDYISDRLM 525
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
276-481 |
5.71e-10 |
|
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: 61.68 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRA--------------YAPRTP---ASAIRDGVFLVA 338
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfinYLPQEPyifSGSILENLLLGA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 339 KDRASTGIVPEF--------NIyENMSLPFLPRFSnmsvtrrraerqtareqiadlkivcrserDDLATLSGGNQQKVTV 410
Cdd:TIGR01193 573 KENVSQDEIWAAceiaeikdDI-ENMPLGYQTELS-----------------------------EEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 411 ARWLTQPSRLLILDEPFQGVDIAARHDIAAKLReSARDRaTLVFLTELDEALETADRILVMSENTIV--GEHR 481
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDK-TIIFVAHRLSVAKQSDKIIVLDHGKIIeqGSHD 693
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
265-477 |
5.82e-10 |
|
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: 59.65 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRAST 344
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVPEFNIYENMSLPFLP--RFsnmsvtRRRAERQTAREQIAD-LKIVCRSerddlatLSGGNQQKVTVARWLTQPSRLL 421
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPpaRF------KKRLDELSELLDLEElLDTPVRQ-------LSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELD----EALetADRILVMSENTIV 477
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmkdiEAL--ARRVLVIDKGRLL 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-227 |
6.29e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG---VHRADRGVMMLGD-----RPFSPATPAEAMRAGV 83
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltGGGAPRGARVTGDvtlngEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINDGVVGALDVASnlvLDRLNGAGSGfffnpRKVRREAREVA----ERMGLGIDLSAEVTDLPLADRQMVAIAR 159
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVL---LGRYPHARRA-----GALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 160 AMAH---------EPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-224 |
7.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 19 NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLGDRpFSPATPAEaMRAGVVTVHQNINDGVVGA 97
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqIIIDGDL-LTEENVWD-IRHKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 L---DVASNLvldrlngAGSGFffnPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEP 173
Cdd:PRK13650 98 TvedDVAFGL-------ENKGI---PHEEMKErVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 174 TSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIrRLADRIVSLRDGAI 224
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
7.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNA-----VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAM- 79
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 ----------------RAGVV-----------TVHQNINDGVVgALDVASNlvldrlngagsgfffnprkvrrEAREVA- 131
Cdd:PRK13631 101 tnpyskkiknfkelrrRVSMVfqfpeyqlfkdTIEKDIMFGPV-ALGVKKS----------------------EAKKLAk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 132 ---ERMGLGID-LSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMS 207
Cdd:PRK13631 158 fylNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
|
250
....*....|....*...
gi 1998276353 208 DIRRLADRIVSLRDGAIV 225
Cdd:PRK13631 238 HVLEVADEVIVMDKGKIL 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
276-494 |
7.47e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRASTGI--VP-EFNI 352
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE------------DISLLPLHARARRGIgyLPqEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 YENMSLpflprFSN-MSV--------TRRRAERqtAREQIADLKIVcrSERDDLA-TLSGGNQQKVTVARWLTQPSRLLI 422
Cdd:PRK10895 90 FRRLSV-----YDNlMAVlqirddlsAEQREDR--ANELMEEFHIE--HLRDSMGqSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 423 LDEPFQGVDIAARHDIaAKLRESARDRATLVFLTE--LDEALETADRILVMSENTIVGEHRNADVDMDRLLAEV 494
Cdd:PRK10895 161 LDEPFAGVDPISVIDI-KRIIEHLRDSGLGVLITDhnVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
277-502 |
7.51e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAP--RTPASAIRDGVFLVAKDraSTGIV-PEFNIY 353
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQD--SISAVnPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLPfLPRFSNMSVTRRRAERQTAREQIaDLKIVCRSERDdlATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:PRK10419 110 EIIREP-LRHLLSLDKAERLARASEMLRAV-DLDDSVLDKRP--PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 434 ARHDIAAKLRESARDRAT-LVFLT-ELDEALETADRILVMSENTIVGEhrnADVDMDRLLAEVAGQRLEPA 502
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTaCLFIThDLRLVERFCQRVMVMDNGQIVET---QPVGDKLTFSSPAGRVLQNA 253
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
276-477 |
1.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.68 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYA-PRTPASAIRDGVFLVAKdrastgiVPEFNIYE 354
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdKKVKLSDIRKKVGLVFQ-------YPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NM---SLPFLPRFSNMSvtrrraERQTAREQIADLKIVCRSeRDDLA-----TLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:PRK13637 99 ETiekDIAFGPINLGLS------EEEIENRVKRAMNIVGLD-YEDYKdkspfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 427 FQGVDIAARHDIAAKLRESARDRATLVFLTE--LDEALETADRILVMSENTIV 477
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVShsMEDVAKLADRIIVMNKGKCE 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
244-476 |
1.30e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 244 GQNLGLHSIDARAAGAPVFSARDLRIApgakplsmelgAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMqLDGRAyap 323
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIP-----------AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 324 rtPASAIRDGVFLVAKDRastgivpefniyenMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSErDDLATLSGG 403
Cdd:PRK11247 75 --PLAEAREDTRLMFQDA--------------RLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRAN-EWPAALSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 404 NQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELD--EALETADRILVMSENTI 476
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvsEAVAMADRVLLIEEGKI 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
274-473 |
1.56e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 59.32 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasairDGVFLVAKDRastGI--VPEF- 350
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR------------DVTDLPPKDR---NIamVFQSy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 ------NIYENMSLPFlpRFSNMSvtrrRAERQTAREQIAD-LKIvcrserDDL-----ATLSGGNQQKVTVARWLTQPS 418
Cdd:COG3839 85 alyphmTVYENIAFPL--KLRKVP----KAEIDRRVREAAElLGL------EDLldrkpKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 419 RLLILDEPFQGVDiaarhdiaAKLRESARD---------RATLVFLT-ELDEALETADRILVMSE 473
Cdd:COG3839 153 KVFLLDEPLSNLD--------AKLRVEMRAeikrlhrrlGTTTIYVThDQVEAMTLADRIAVMND 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
286-481 |
1.57e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 286 VAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRDGVFLVAKDRAStgivpefniyenMSLPFlprFS 365
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDPVV------------LADTF---LA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 366 NMSVTRRRAERQ--TARE--QIADLkivCRSERDDLAT--------LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIA 433
Cdd:PRK10790 434 NVTLGRDISEEQvwQALEtvQLAEL---ARSLPDGLYTplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1998276353 434 ARHDIAAKLREsARDRATLVFLTELDEALETADRILVMSENTIV--GEHR 481
Cdd:PRK10790 511 TEQAIQQALAA-VREHTTLVVIAHRLSTIVEADTILVLHRGQAVeqGTHQ 559
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-225 |
1.59e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 16 FGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKV------MSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQN 89
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 90 INDgvVGALDVASNLVLD-RLNGagsgfffnprkVRREAREVAERMGLGIDLSA---EVTD--------LPLADRQMVAI 157
Cdd:PRK14267 94 PNP--FPHLTIYDNVAIGvKLNG-----------LVKSKKELDERVEWALKKAAlwdEVKDrlndypsnLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRaRGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
276-479 |
1.84e-09 |
|
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: 57.61 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAiRDGVFLVAkdrastgivPEFniYEN 355
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGALIEA---------PGF--YPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSlpflpRFSNMSVTRRRAERqtaREQIAD--LKIVCRSERDDL--ATLSGGNQQKVTVAR-WLTQPSrLLILDEPFQGV 430
Cdd:cd03268 87 LT-----ARENLRLLARLLGI---RKKRIDevLDVVGLKDSAKKkvKGFSLGMKQRLGIALaLLGNPD-LLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 431 DIAARHDIAAKLReSARDRATLVFLTE--LDEALETADRILVMSENTIVGE 479
Cdd:cd03268 158 DPDGIKELRELIL-SLRDQGITVLISShlLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
276-459 |
2.12e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAiRDGVFLVAKDRASTGIVPEFNiyen 355
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-RGLLYLGHAPGIKTTLSVLEN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 msLPFLPRFSNmsvtrrraeRQTAREQIADLKIVCRSERDdLATLSGGNQQKVTVAR-WLTQPsRLLILDEPFQGVDIAA 434
Cdd:cd03231 94 --LRFWHADHS---------DEQVEEALARVGLNGFEDRP-VAQLSAGQQRRVALARlLLSGR-PLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*
gi 1998276353 435 RHDIAAKLRESARDRATLVFLTELD 459
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-217 |
2.47e-09 |
|
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: 57.80 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 28 DLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGvmmlgdrpfspatPAEAMRAGVVTVHQNINDGVVGALDvasNLVLD 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------------DIEIELDTVSYKPQYIKADYEGTVR---DLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 108 RLNGAGSGFFFNprkvrreaREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNeaERLFA 187
Cdd:cd03237 85 ITKDFYTHPYFK--------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 1998276353 188 --LIDR--LRARGVAILyISHRMSDIRRLADRIV 217
Cdd:cd03237 155 skVIRRfaENNEKTAFV-VEHDIIMIDYLADRLI 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
276-499 |
2.48e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGI--HAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRAstgIVPEFNIY 353
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELT---LVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSLP---FLP--RFSNMSVTRRraerqtAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQ 428
Cdd:TIGR02633 97 ENIFLGneiTLPggRMAYNAMYLR------AKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 429 GV---DIAARHDIAAKLResARDRATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQRL 499
Cdd:TIGR02633 171 SLtekETEILLDIIRDLK--AHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREI 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
276-436 |
2.74e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasairdgvflVAKDRAS-----------T 344
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----------------IRRQRDEyhqdllylghqP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVPEFNIYENMslpflpRFSnmsvtrRRAERQTAREQIAD-LKIVCRSERDDL--ATLSGGNQQKVTVAR-WLTQPsRL 420
Cdd:PRK13538 84 GIKTELTALENL------RFY------QRLHGPGDDEALWEaLAQVGLAGFEDVpvRQLSAGQQRRVALARlWLTRA-PL 150
|
170 180
....*....|....*....|.
gi 1998276353 421 LILDEPF-----QGVDIAARH 436
Cdd:PRK13538 151 WILDEPFtaidkQGVARLEAL 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-475 |
2.94e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGV------------------FLVA 338
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVvrtfqhvrlfremtvienLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 339 KDRAS-TGIVPefniyenmSLPFLPRFsnmsvtrRRAERQTAR------EQIADLKIVCRSErddlATLSGGNQQKVTVA 411
Cdd:PRK11300 105 QHQQLkTGLFS--------GLLKTPAF-------RRAESEALDraatwlERVGLLEHANRQA----GNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 412 RWL-TQPsRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEAL--ETADRILVMSENT 475
Cdd:PRK11300 166 RCMvTQP-EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLvmGISDRIYVVNQGT 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-177 |
3.02e-09 |
|
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: 59.18 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVhradrgvmmlgDRPFS-PATPAEAMRAGV 83
Cdd:TIGR03719 4 IYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNgEARPQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 V----------TVHQNINDGVVGALDvasnlVLDRLNGAGSGFFFNPRKVRREAREVAE---------------RMGLGI 138
Cdd:TIGR03719 73 LpqepqldptkTVRENVEEGVAEIKD-----ALDRFNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsQLEIAM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1998276353 139 DL------SAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSL 177
Cdd:TIGR03719 148 DAlrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-227 |
4.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQNINDGVVGAL--- 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT-AENVWNLRRKIGMVFQNPDNQFVGATved 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLVldrlngagsgfffNPRKVRREAREVAERMGLGIDL----SAEVTDLPLADRQMVAIARAMAHEPQVMILDEPT 174
Cdd:PRK13642 102 DVAFGME-------------NQGIPREEMIKRVDEALLAVNMldfkTREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 175 SSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRlADRIVSLRDGAIVGQ 227
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-222 |
4.86e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.32 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 18 PNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG-VHRADRGVMMLGDRPFSPATPAeAMRAgvvTVHQNIndgvvg 96
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPGSIAYVSQEPW-IQNG---TIRENI------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 aldvasnlvldrLNGAgsgfFFNPRKVRrearEVAERMGLGIDLSAevtdLPLAD---------------RQMVAIARAM 161
Cdd:cd03250 87 ------------LFGK----PFDEERYE----KVIKACALEPDLEI----LPDGDlteigekginlsggqKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 162 AHEPQVMILDEPTSSLSSNEAERLF--ALIDRLRARGVAILyISHRMSDIRRlADRIVSLRDG 222
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNG 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-233 |
5.34e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 18 PNAVLRGVGLDLRAGEVTVLMGANGAGKS-----TLVKVMSGVhRADRGVMMLGDRPFSPAtpaeAMRA-GVVTVHQNIN 91
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGV-RQTAGRVLLDGKPVAPC----ALRGrKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 92 DGvvgaldvasnlvldrlngagsgffFNP-RKVRREAREVAERMGLGID---LSAEVTDLPLADRQMVA----------- 156
Cdd:PRK10418 90 SA------------------------FNPlHTMHTHARETCLALGKPADdatLTAALEAVGLENAARVLklypfemsggm 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 157 -----IARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQFDE 230
Cdd:PRK10418 146 lqrmmIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDV 225
|
...
gi 1998276353 231 KPL 233
Cdd:PRK10418 226 ETL 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
262-473 |
6.02e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.17 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 262 FSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR-AYAPRTpaSAIRDGVFlvaKD 340
Cdd:cd03291 42 FSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQF--SWIMPGTI---KE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 341 RASTGIvpEFNIYENMSLpflprfsnmsvtrrrAERQTAREQIADLkivcrSERDDLA------TLSGGNQQKVTVARWL 414
Cdd:cd03291 117 NIIFGV--SYDEYRYKSV---------------VKACQLEEDITKF-----PEKDNTVlgeggiTLSGGQRARISLARAV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 415 TQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSE 473
Cdd:cd03291 175 YKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHE 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-214 |
6.15e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.10 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 2 GDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSgvhradrgvmMLGDrpFSPATPAEamra 81
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFN----------RLND--LIPGFRVE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 82 GVVTVH-QNINDGVVGALDVAS--NLVLDRLNGAGSGFF----FNPR--KVRREAREVAERMGLGIDLSAEVTD------ 146
Cdd:PRK14243 70 GKVTFHgKNLYAPDVDPVEVRRriGMVFQKPNPFPKSIYdniaYGARinGYKGDMDELVERSLRQAALWDEVKDklkqsg 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 147 --LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARgVAILYISHRMSDIRRLAD 214
Cdd:PRK14243 150 lsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
260-434 |
6.42e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIrdgVF 335
Cdd:PRK13539 1 MMLEGEDLACVRGGRVlfsgLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC---HY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 336 LVAKDrastGIVPEFNIYENmsLPFLPRFSNmsvtrrraerqTAREQIADlkIVCRSERDDLAT-----LSGGNQQKVTV 410
Cdd:PRK13539 78 LGHRN----AMKPALTVAEN--LEFWAAFLG-----------GEELDIAA--ALEAVGLAPLAHlpfgyLSAGQKRRVAL 138
|
170 180
....*....|....*....|....
gi 1998276353 411 ARWLTQPSRLLILDEPFQGVDIAA 434
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAA 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-225 |
6.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRpfspATPAEAMRAGVVT-VHQNIndGVVGALDv 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDY----AIPANLKKIKEVKrLRKEI--GLVFQFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNgagSGFFFNPRKVRREAREVAERMGLGIDLSAEVTD--------LPLADRQMVAIARAMAHEPQVMILDE 172
Cdd:PRK13645 100 EYQLFQETIE---KDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyvkrspfeLSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 173 PTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-224 |
7.08e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 5 AIFRIAGLTKAF-GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE---AMr 80
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiAM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 agvvtVHQNIndgvvgAL----DVASNLvldrlngaGSGFffnprKVRREAR-EVAERmglgIDLSAEVTDL-PLAD--- 151
Cdd:PRK11650 81 -----VFQNY------ALyphmSVRENM--------AYGL-----KIRGMPKaEIEER----VAEAARILELePLLDrkp 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 152 -------RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGA 223
Cdd:PRK11650 133 relsggqRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
.
gi 1998276353 224 I 224
Cdd:PRK11650 213 A 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
254-477 |
7.73e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 254 ARAAGAPVFSARDLRIA----PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAprtpasa 329
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSfdgqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 330 irdgvflvakdrastgIVPEFNIYENMSLPFLPRFSNMSVTRRRA----ERQTAREQIAD-----LKIVCRSE--RDDLA 398
Cdd:PRK11607 85 ----------------HVPPYQRPINMMFQSYALFPHMTVEQNIAfglkQDKLPKAEIASrvnemLGLVHMQEfaKRKPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 399 TLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDiaarhdiaAKLRES---------ARDRATLVFLT-ELDEALETADRI 468
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD--------KKLRDRmqlevvdilERVGVTCVMVThDQEEAMTMAGRI 220
|
....*....
gi 1998276353 469 LVMSENTIV 477
Cdd:PRK11607 221 AIMNRGKFV 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
271-499 |
8.29e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPL---SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDrasTGIV 347
Cdd:PRK10982 9 PGVKALdnvNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE---LNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFNIYENMSLPFLPRfSNMSVTRRRAERQTaREQIADLKIVCrSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:PRK10982 86 LQRSVMDNMWLGRYPT-KGMFVDQDKMYRDT-KAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 428 QGV---DIAARHDIAAKLRESArdrATLVFLT-ELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAGQRL 499
Cdd:PRK10982 163 SSLtekEVNHLFTIIRKLKERG---CGIVYIShKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSL 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
274-499 |
1.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.28 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTpASAIRDGVFLVAKDR-----ASTgivp 348
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN-EKWVRSKVGLVFQDPddqvfSST---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 efnIYENMSlpFLPRfsNMSVTRRRAERQTAreqiADLKIVCRSERDDLAT--LSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:PRK13647 97 ---VWDDVA--FGPV--NMGLDKDEVERRVE----EALKAVRMWDFRDKPPyhLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 427 FQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVGEHRNaDVDMDRLLAEVAGQRL 499
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVAThDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRL 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-228 |
1.08e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 152 RQMVAIARAMAHEPQVMILDEPTSSLSSNeAERLF--ALIDRLRARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQF 228
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSN-SEKLIekTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDRTGSF 1440
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-477 |
1.37e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDgvfLVAKDRASTGIV-PEFNIY- 353
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKG---LIRQLRQHVGFVfQNFNLFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 -----EN-MSLPFLprfsnMSVTRRRAERQTAREQIADLKIVCRsERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:PRK11264 99 hrtvlENiIEGPVI-----VKGEPKEEATARARELLAKVGLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEKRTMVIVThEMSFARDVADRAIFMDQGRIV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
274-477 |
1.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTpASAIRD--GVFLVAKDRASTGIVPEFN 351
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-LKEIRKkiGIIFQNPDNQFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 I---YENmslpflprfsnmsvtrRRAERQTAREQIADLKIVCRSE----RDDLaTLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:PRK13632 105 IafgLEN----------------KKVPPKKMKDIIDDLAKKVGMEdyldKEPQ-NLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALEtADRILVMSENTIV 477
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKkTLISIThDMDEAIL-ADKVIVFSEGKLI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
274-468 |
1.76e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASAIRDGVFLVAKDRASTGI------V 347
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ------PMSKLSSAAKAELRNQKLGFIyqfhhlL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 PEFNIYENMSLPFLprfsnMSVTRRRAERQTAREQIADLKIVCRSERDDlATLSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:PRK11629 100 PDFTALENVAMPLL-----IGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 428 QGVDIAARHDIAAKLRESARDRATLVFLTELDeaLETADRI 468
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHD--LQLAKRM 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
400-480 |
1.81e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.76 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRaTLVFLTELDEALETADRILVMSENTIV-- 477
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLTGLEQFDRICVMDNGQIIeq 554
|
...
gi 1998276353 478 GEH 480
Cdd:PRK11160 555 GTH 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
276-438 |
1.84e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.67 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRdgvFLvakdRASTGIV-------P 348
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIP---YL----RRRIGVVfqdfrllP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPflprfsnMSVTRRraERQTAREQIAD-LKIVCRSERDDL--ATLSGGNQQKVTVARWL-TQPSrLLILD 424
Cdd:COG2884 93 DRTVYENVALP-------LRVTGK--SRKEIRRRVREvLDLVGLSDKAKAlpHELSGGEQQRVAIARALvNRPE-LLLAD 162
|
170
....*....|....
gi 1998276353 425 EPFQGVDIAARHDI 438
Cdd:COG2884 163 EPTGNLDPETSWEI 176
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
271-479 |
1.85e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 56.71 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtpasAIRDgvflVAKD--RAST 344
Cdd:COG1132 350 PGDRPvlkdISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV---------DIRD----LTLEslRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVPE----FN--IYENMslpflpRFSNMSVTR---RRAERQT-AREQIADLK-----IVcrSERDdlATLSGGNQQKVT 409
Cdd:COG1132 417 GVVPQdtflFSgtIRENI------RYGRPDATDeevEEAAKAAqAHEFIEALPdgydtVV--GERG--VNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 410 VARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVF---LTeldeALETADRILVMSENTIVGE 479
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIahrLS----TIRNADRILVLDDGRIVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-216 |
1.87e-08 |
|
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: 56.87 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 1 MGDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGdrpfspatpaEAMR 80
Cdd:TIGR03719 318 LGDKVI-EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------ETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGVV-----------TVHQNINDG----VVGALDVASNLVLDRLNGAGSgfffnprkvrrearevaermglgiDLSAEVT 145
Cdd:TIGR03719 387 LAYVdqsrdaldpnkTVWEEISGGldiiKLGKREIPSRAYVGRFNFKGS------------------------DQQKKVG 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 146 DLPLADRQMVAIARAMAHEPQVMILDEPTSSLssnEAERLFALIDRLRARGVAILYISHRmsdiRRLADRI 216
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHD----RWFLDRI 506
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
276-484 |
1.91e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYA-PRTP-ASAIRdgvflvaKDRASTGIV------ 347
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPsEKAIR-------LLRQKVGMVfqqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 -PEFNIYENM-SLPFLPRFSNMSVTRRRAERQTAREQIADlkivcRSERDDLAtLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:COG4161 94 wPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTD-----KADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVgEHRNAD 484
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELSQTGITQVIVThEVEFARKVASQVVYMEKGRII-EQGDAS 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-225 |
2.04e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGD---RPFSPATPAEAMRAGVVTVHQNIndGVVGAL 98
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSF--ALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVASNLVLdrlngaGSGFFFNPRKVRRE-AREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSL 177
Cdd:PRK10070 122 TVLDNTAF------GMELAGINAEERREkALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 178 SSNEAERLFALIDRLRARGV-AILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
275-500 |
2.31e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 275 PLSMELGAGEVVAVTGLVGVGKTRLAETLFGIhAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRASTgIVPEFNiYE 354
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-AMPVFQ-YL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMSLPflprfsnmsVTRRRAERQTAREQIAD-LKIVCRSERDdLATLSGGNQQKVTVARWLTQ------P-SRLLILDEP 426
Cdd:PRK03695 91 TLHQP---------DKTRTEAVASALNEVAEaLGLDDKLGRS-VNQLSGGEWQRVRLAAVVLQvwpdinPaGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 427 FQGVDIAARHDIAAKLRESARD-RATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAG---QRLE 500
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGvnfRRLD 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
271-473 |
2.48e-08 |
|
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: 54.75 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDgRAYAPRTPASAIRDGVFLVakdRAST-GIVPE 349
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQASPREILAL---RRRTiGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FniyenmsLPFLPRFSNMSVT-----RRRAERQTAREQIADLkivcrSERDDL---------ATLSGGNQQKVTVARWLT 415
Cdd:COG4778 101 F-------LRVIPRVSALDVVaepllERGVDREEARARAREL-----LARLNLperlwdlppATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 416 QPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALET-ADRILVMSE 473
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTP 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-229 |
2.61e-08 |
|
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: 54.42 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 17 GPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpATPAEAMRAGVVTVHQninDGVVG 96
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQ---DPVLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 97 ALDVASNLvlDRLNGAGSGfffnprkvrrEAREVAERMGLG--IDLSAEVTDLPLAD---------RQMVAIARAMAHEP 165
Cdd:cd03244 91 SGTIRSNL--DPFGEYSDE----------ELWQALERVGLKefVESLPGGLDTVVEEggenlsvgqRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 166 QVMILDEPTSSLSSNEAERLFALIdRLRARGVAILYISHRMSDIRRlADRIVSLRDGAIVgQFD 229
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV-EFD 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-225 |
2.84e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 27 LDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPaEAMRAGVVTVHqnindgvvgaldvaSNLVL 106
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR-EAYRQLFSAVF--------------SDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 107 -DRLNGAGSGFffnprkVRREAREVAERMGLGIDLSAE-----VTDLPLADRQMVAIARAMAHEPQVMILDE------Pt 174
Cdd:COG4615 418 fDRLLGLDGEA------DPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdP- 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 175 sslssnEAERLF--ALIDRLRARGVAILYISHrmsDIR--RLADRIVSLRDGAIV 225
Cdd:COG4615 491 ------EFRRVFytELLPELKARGKTVIAISH---DDRyfDLADRVLKMDYGKLV 536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-222 |
2.92e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 30 RAGEVTVLMGANGAGKSTLVKVMSGvhRADRGVMMLGDR--PFSPATPAEAMRAGVVTvHQNINdgvVGALDVASNLVLd 107
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRlvNGRPLDSSFQRSIGYVQ-QQDLH---LPTSTVRESLRF- 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 108 rlngagSGFFFNPRKVRREAR-----EVAERMGL-----------GIDLSAEvtdlplaDRQMVAIARAMAHEPQVMI-L 170
Cdd:TIGR00956 860 ------SAYLRQPKSVSKSEKmeyveEVIKLLEMesyadavvgvpGEGLNVE-------QRKRLTIGVELVAKPKLLLfL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 171 DEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMS-DIRRLADRIVSLRDG 222
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaILFEEFDRLLLLQKG 979
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
276-477 |
3.83e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASaiRD--GVFlvakdrASTGIVPEFNIY 353
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDicMVF------QSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMS--LPFLprfsnmsvTRRRAERqtaREQIAD-LKIVcrserdDLA--------TLSGGNQQKVTVARWLTQPSRLLI 422
Cdd:PRK11432 97 ENVGygLKML--------GVPKEER---KQRVKEaLELV------DLAgfedryvdQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 423 LDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRElQQQFNITSLYVThDQSEAFAVSDTVIVMNKGKIM 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
4.07e-08 |
|
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: 56.18 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 4 TAIFRIAGLTKAFGPN---AVLRgVGLDLRAGEVTVLMGANGAGKSTLVKVMSGvhraDRGVMMlGDrpfspATPA-EAM 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTsspAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTG----DTTVTS-GD-----ATVAgKSI 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 RAGVVTVHQNIN-----DGVVGALDVASNLVL-DRLNGAGSgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQ 153
Cdd:TIGR01257 2004 LTNISDVHQNMGycpqfDAIDDLLTGREHLYLyARLRGVPA------EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKR 2077
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 154 MVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGA 223
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
400-495 |
4.80e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWL-TQPSrLLILDEPFQGVDIAARHDIAAKLRESARDRATLVF-LTELDEALETADRILVMSENTIV 477
Cdd:PRK10938 136 LSTGETRKTLLCQALmSEPD-LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLvLNRFDEIPDFVQFAGVLADCTLA 214
|
90
....*....|....*...
gi 1998276353 478 GEHRNADVDMDRLLAEVA 495
Cdd:PRK10938 215 ETGEREEILQQALVAQLA 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
275-453 |
4.82e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 275 PLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVpefnIYE 354
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMT----VRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMSLPFLP------RFSnmsvtrrRAERQTAREQIA--DLKIVCRSERDdlaTLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:PRK10575 105 LVAIGRYPwhgalgRFG-------AADREKVEEAISlvGLKPLAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180
....*....|....*....|....*..
gi 1998276353 427 FQGVDIAARHDIAAKLRESARDRATLV 453
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTV 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
287-496 |
4.94e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 287 AVTGLVGV---GKTRLAETLFGIHAPLAGSMQLDGRA--YAPRTpASAIRDGVFLVAKDrastgivPEFNI-YENMSLPF 360
Cdd:PRK13638 28 PVTGLVGAngcGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRG-LLALRQQVATVFQD-------PEQQIfYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 361 LPRFSNMSVtrrrAERQTAREQIADLKIV--CRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDI 438
Cdd:PRK13638 100 AFSLRNLGV----PEAEITRRVDEALTLVdaQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 439 AAKLRE-SARDRATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLLAEVAG 496
Cdd:PRK13638 176 IAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAG 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
276-479 |
5.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRD-GVFLVAKDRASTGIVPEFNIYE 354
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKiGMVFQNPDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 355 NMSLPFLPRFSNMsvtrRRAERQTAREQIADLKIvcrserDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAA 434
Cdd:PRK13642 106 GMENQGIPREEMI----KRVDEALLAVNMLDFKT------REPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 435 RHDIAAKLREsARDRATLVFLT---ELDEAlETADRILVMSENTIVGE 479
Cdd:PRK13642 176 RQEIMRVIHE-IKEKYQLTVLSithDLDEA-ASSDRILVMKAGEIIKE 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
270-477 |
5.70e-08 |
|
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: 55.14 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 270 APGA-----KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDG---RAYAPRTPASAIrdgvflvakdr 341
Cdd:COG4618 340 PPGSkrpilRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlSQWDREELGRHI----------- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 342 astGIVPE----FN--IYENMSlpflpRFSNMSvtrrrAERQTAREQIADL-KIVCRSER-------DDLATLSGGNQQK 407
Cdd:COG4618 409 ---GYLPQdvelFDgtIAENIA-----RFGDAD-----PEKVVAAAKLAGVhEMILRLPDgydtrigEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 408 VTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTIV 477
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
276-496 |
5.86e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFG-IHAPLA-------GSMQLDGRAYAP-RTPASAIRDGVFLVAKDRASTgi 346
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAiDAPRLARLRAVLPQAAQPAFA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 347 vpeFNIYENMSLPFLPRFSNMSVTRRR----AERQTAREQIADLkivcrsERDDLATLSGGNQQKVTVARWLTQ------ 416
Cdd:PRK13547 98 ---FSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATAL------VGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 417 ---PSRLLILDEPFQGVDIAARHDIAAKLRESARD--RATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDRLL 491
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHI 248
|
....*
gi 1998276353 492 AEVAG 496
Cdd:PRK13547 249 ARCYG 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-225 |
5.91e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFS--PATPAEAMRAGVVTVHQNINDGVVGALDVAS 102
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlSPGKLQALRRDIQFIFQDPYASLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 103 NLVLD-RLNGAGSGfffnpRKVRREAREVAERMGLGIDLSAEVT-DLPLADRQMVAIARAMAHEPQVMILDEPTSSLS-S 179
Cdd:PRK10261 423 SIMEPlRVHGLLPG-----KAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDvS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 180 NEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-205 |
8.64e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVH--RADRGVMMLGDRPFSPATPaeamragvvtvhqnINDGVVGAL 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS--------------LIDAIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 99 DVasNLVLDRLNGAG--SGFFFnprkvRREAREvaermglgidlsaevtdlpLADRQM--VAIARAMAHEPQVMILDEPT 174
Cdd:COG2401 111 DF--KDAVELLNAVGlsDAVLW-----LRRFKE-------------------LSTGQKfrFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|..
gi 1998276353 175 SSLSSNEAERL-FALIDRLRARGVAILYISHR 205
Cdd:COG2401 165 SHLDRQTAKRVaRNLQKLARRAGITLVVATHH 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-230 |
8.82e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKStlvkvmSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTV-- 86
Cdd:NF000106 16 VRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIg* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINDGVVGALDVASNLVLdrlngAGSGFFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQ 166
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYM-----IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV--GQFDE 230
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIadGKVDE 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-54 |
8.87e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 8.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 1 MGDTAIFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG 54
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-220 |
1.09e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSpatpaEAMRAGVVT-VHQNinDGVVGALDV 100
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLVAyVPQS--EEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNGAGSGFFFNPRKVRREAREVA-ERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSS 179
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAlARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276353 180 NEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLR 220
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
274-471 |
1.21e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.88 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAsaiRDGVFLVAKdraSTGIVPEFNIY 353
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA---ERGVGMVFQ---SYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENMSlpFLPRFSNMSvtrrRAERQTAREQIAD-LKIVCRSERDDLAtLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDI 432
Cdd:PRK11000 94 ENMS--FGLKLAGAK----KEEINQRVNQVAEvLQLAHLLDRKPKA-LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1998276353 433 AARHDIAAKL-RESARDRATLVFLTElD--EALETADRILVM 471
Cdd:PRK11000 167 ALRVQMRIEIsRLHKRLGRTMIYVTH-DqvEAMTLADKIVVL 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
400-477 |
1.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 1.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVIThTMEHVLEVADEVIVMDKGKIL 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
271-499 |
1.46e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPL---SMELGAGEVVAVTGLVGVGKTRLAETLFGI--HAPLAGSMQLDGRAYAprtpASAIRD----GVFLVAKDR 341
Cdd:PRK13549 16 GGVKALdnvSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQ----ASNIRDteraGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 342 AstgIVPEFNIYENMslpFL----PRFSNMSVTR--RRAERQTAREQIA---DLKIvcrserddlATLSGGNQQKVTVAR 412
Cdd:PRK13549 92 A---LVKELSVLENI---FLgneiTPGGIMDYDAmyLRAQKLLAQLKLDinpATPV---------GNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 413 WLTQPSRLLILDEPFQGV---DIAARHDIAAKLResARDRATLVFLTELDEALETADRILVMSENTIVGEHRNADVDMDR 489
Cdd:PRK13549 157 ALNKQARLLILDEPTASLtesETAVLLDIIRDLK--AHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDD 234
|
250
....*....|
gi 1998276353 490 LLAEVAGQRL 499
Cdd:PRK13549 235 IITMMVGREL 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-484 |
1.64e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAY--APRTPASAIRdgvflvaKDRASTGIV------ 347
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfSKTPSDKAIR-------ELRRNVGMVfqqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 348 -PEFNIYENM-SLPFlpRFSNMSvtrRRAERQTAREQIADLKIVCRSERDDLaTLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK11124 94 wPHLTVQQNLiEAPC--RVLGLS---KDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 426 PFQGVD--IAARhdIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVgEHRNAD 484
Cdd:PRK11124 168 PTAALDpeITAQ--IVSIIRELAETGITQVIVThEVEVARKTASRVVYMENGHIV-EQGDAS 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-225 |
1.77e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.18 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 12 LTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLG-----DRPFSPATPAEAMRAGVVTV 86
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 87 HQNINDGVvgaldvasnlvldrlngaGSGFffnpRKVRREAREVAERmglgIDLSAEVTDLP-LADR----------QMV 155
Cdd:PRK11432 92 HMSLGENV------------------GYGL----KMLGVPKEERKQR----VKEALELVDLAgFEDRyvdqisggqqQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 156 AIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
283-477 |
2.02e-07 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 51.40 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLA--GSMQLDGRAYAPRTPasairdgvflvakdRASTGIVPEfniyENMSLPF 360
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF--------------RKIIGYVPQ----DDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 361 LprfsnmsvTRRRAERQTAReqiadlkivCRSerddlatLSGGNQQKVTVARWL-TQPSrLLILDEPFQGVDIAARHDIA 439
Cdd:cd03213 97 L--------TVRETLMFAAK---------LRG-------LSGGERKRVSIALELvSNPS-LLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1998276353 440 AKLRESARDRATLVFLTE--LDEALETADRILVMSENTIV 477
Cdd:cd03213 152 SLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-230 |
2.04e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 24 GVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLG-DRPFSPATPAEAMRAGVVTVHQ----------NIN 91
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGkDLLGMKDDEWRAVRSDIQMIFQdplaslnprmTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 92 DGVVGALDVasnlvldrlngagsgffFNPRKVRREAREVAERMGLGIDLsaevtdLP-LADR----------QMVAIARA 160
Cdd:PRK15079 119 EIIAEPLRT-----------------YHPKLSRQEVKDRVKAMMLKVGL------LPnLINRyphefsggqcQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 161 MAHEPQVMILDEPTSSLS-SNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAIV--GQFDE 230
Cdd:PRK15079 176 LILEPKLIICDEPVSALDvSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVelGTYDE 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-177 |
2.88e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVhradrgvmmlgDRPFS-PATPAEAMRAGV 83
Cdd:PRK11819 6 IYTMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFEgEARPAPGIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 V----------TVHQNINDGVVGALDvasnlVLDRLNgAGSGFFFNPRKvrrEAREVAERMGL---------GIDLS--- 141
Cdd:PRK11819 75 LpqepqldpekTVRENVEEGVAEVKA-----ALDRFN-EIYAAYAEPDA---DFDALAAEQGElqeiidaadAWDLDsql 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1998276353 142 -------------AEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSL 177
Cdd:PRK11819 146 eiamdalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
283-462 |
3.74e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.93 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAP-----RTPASAIRDG-VFlvakdrASTGIVPEFNIYENM 356
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRAKHVGfVF------QSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 357 SLPFLPRFSNmsvtrrraERQTAREQIADLKIVCRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAA 434
Cdd:PRK10584 110 ELPALLRGES--------SRQSRNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*...
gi 1998276353 435 RHDIAAKLRESARDRATLVFLTELDEAL 462
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
280-482 |
4.14e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.03 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 280 LGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAI---RDGVFLVAKDRAstgIVPEFNIYENM 356
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT-RLKNREVpflRRQIGMIFQDHH---LLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 357 SLPFLPRFSNMSVTRRRAERQTAREQIADlkivcrSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARH 436
Cdd:PRK10908 101 AIPLIIAGASGDDIRRRVSAALDKVGLLD------KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 437 DIAAKLRESARDRATLVFLTElDEAL--ETADRILVMSENTIVGEHRN 482
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATH-DIGLisRRSYRMLTLSDGHLHGGVGG 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
274-479 |
4.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDG---VFLVAKDRASTGIVPEf 350
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKagmVFQNPDNQIVATIVEE- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 niyenmSLPFLPRfsNMSVtrrraERQTAREQIAD-LKIVCRSERDDLAT--LSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:PRK13633 106 ------DVAFGPE--NLGI-----PPEEIRERVDEsLKKVGMYEYRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 428 QGVDIAARHDIAAKLRE-SARDRATLVFLTE-LDEALEtADRILVMSENTIVGE 479
Cdd:PRK13633 173 AMLDPSGRREVVNTIKElNKKYGITIILITHyMEEAVE-ADRIIVMDSGKVVME 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
274-476 |
4.49e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.12 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYaprtpaSAIRD--GVFLVAKDRAS-------T 344
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI------NLVRDkdGQLKVADKNQLrllrtrlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVPEFNIYENMSLpfLPRFSNMSVTRRRAERQTAREQ----IADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRL 420
Cdd:PRK10619 96 MVFQHFNLWSHMTV--LENVMEAPIQVLGLSKQEARERavkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 421 LILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVThEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-477 |
5.69e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAY-----APRTPASAIRDGVFLVAKdraSTGIVP 348
Cdd:PRK14246 27 KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAIKLRKEVGMVFQ---QPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPFlprfSNMSVTRRRAERQTAREQIADL---KIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK14246 104 HLSIYDNIAYPL----KSHGIKEKREIKKIVEECLRKVglwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTIV 477
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
271-481 |
5.75e-07 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 50.69 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAirdgvflvakdRASTGIVPE- 349
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-----------RSMIGVVLQd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 ---FN--IYENMslpflpRFSNMSVTRRRAERQTAREQIADLkivCRSERDDLAT--------LSGGNQQKVTVARWLTQ 416
Cdd:cd03254 86 tflFSgtIMENI------RLGRPNATDEEVIEAAKEAGAHDF---IMKLPNGYDTvlgenggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 417 PSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDeALETADRILVMSENTIV--GEHR 481
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLS-TIKNADKILVLDDGKIIeeGTHD 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
276-475 |
5.84e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLVAKDRASTGIVpEFNIYEN 355
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSL--PFlprfsnmSVTRRRAERQTAREQiADLKIVCRSERDDLA----TLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:cd03290 99 ITFgsPF-------NKQRYKAVTDACSLQ-PDIDLLPFGDQTEIGergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 430 VDI-AARHDIAAKLRESAR-DRATLVFLTELDEALETADRILVMSENT 475
Cdd:cd03290 171 LDIhLSDHLMQEGILKFLQdDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-222 |
6.09e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRAD--RGVMMLGDRPFSPATpaeAMRAGVVT 85
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQI---LKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VhqniNDGVVGALDVASNLV---LDRLngagsgfffnPRKVRRE-----AREVAERMGLG-----IDLSAEVTDLPLADR 152
Cdd:PLN03211 147 Q----DDILYPHLTVRETLVfcsLLRL----------PKSLTKQekilvAESVISELGLTkcentIIGNSFIRGISGGER 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 153 QMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSD-IRRLADRIVSLRDG 222
Cdd:PLN03211 213 KRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEG 283
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-223 |
7.04e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 23 RGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPfspatpaeaMRAGVVTVHQNI-----NDGVVGA 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP---------IRRQRDEYHQDLlylghQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 98 LDVASNLvldRLNGAGSGfffnprKVRREAREVA-ERMGLgidlsAEVTDLPLA-----DRQMVAIARAMAHEPQVMILD 171
Cdd:PRK13538 89 LTALENL---RFYQRLHG------PGDDEALWEAlAQVGL-----AGFEDVPVRqlsagQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 172 EPTSSLSSNEAERLFALIDRLRARGVAILYISHRmsDIRRLADRIVSLRDGA 223
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLRLGQ 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
259-477 |
8.30e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 259 APVFSARDL--RIAP--GAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAP----------- 323
Cdd:PRK11701 4 QPLLSVRGLtkLYGPrkGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyalseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 324 ----RT--------PASAIRDGVflvakdraSTGIvpefNIYENMslpflprfsnMSVTRRRAE--RQTAREQIADLKIV 389
Cdd:PRK11701 84 rrllRTewgfvhqhPRDGLRMQV--------SAGG----NIGERL----------MAVGARHYGdiRATAGDWLERVEID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 390 cRSERDDL-ATLSGGNQQKVTVARWL-TQPsRLLILDEPFQGVDIAARHDIAAKLRESARDR--ATLVFLTELDEALETA 465
Cdd:PRK11701 142 -AARIDDLpTTFSGGMQQRLQIARNLvTHP-RLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLA 219
|
250
....*....|..
gi 1998276353 466 DRILVMSENTIV 477
Cdd:PRK11701 220 HRLLVMKQGRVV 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-237 |
8.42e-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: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 134 MGLG-IDLSAEVTDLPLADRQMVAIARAMAHEPQ--VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIR 210
Cdd:cd03238 74 VGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLS 153
|
90 100
....*....|....*....|....*..
gi 1998276353 211 RlADRIVSLRDGAivGQFDEKpLDYEG 237
Cdd:cd03238 154 S-ADWIIDFGPGS--GKSGGK-VVFSG 176
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
276-443 |
8.98e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQldgrayapRTPASAIrdgvflvakdrastGIVPEfNIYEN 355
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRI--------------GYVPQ-KLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPF-LPRFSNMSVTRRRAERQTAREQIADLKIVcrseRDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDI-- 432
Cdd:PRK09544 80 TTLPLtVNRFLRLRPGTKKEDILPALKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVng 155
|
170
....*....|..
gi 1998276353 433 -AARHDIAAKLR 443
Cdd:PRK09544 156 qVALYDLIDQLR 167
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-205 |
9.34e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAEAMRAGVVTVHQNINDGvvgaLDV 100
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPY----LTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNGAGSgfffnprkvrREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSN 180
Cdd:PRK13540 92 RENCLYDIHFSPGA----------VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 1998276353 181 EAERLFALIDRLRARGVAILYISHR 205
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-225 |
9.64e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPA-EAMRAGVV----TVHQNINDGVVGALD 99
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSyRSQRIRMIfqdpSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 100 VASnlvldRLNGAgsgffFNPRKVRREAREVAERMGLGIDLSAEVTD-LPLADRQMVAIARAMAHEPQVMILDEPTSSLS 178
Cdd:PRK15112 112 FPL-----RLNTD-----LEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 179 SNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIV 225
Cdd:PRK15112 182 MSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
274-481 |
1.04e-06 |
|
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: 49.85 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayaprtpaSAIRDgvFLVAKDRASTGIVPE---- 349
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG---------VDIRD--LNLRWLRSQIGLVSQepvl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FN--IYENMSLPflpRFSNMSVTRRRAERQT-AREQIADLKIVCRSERDDLAT-LSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:cd03249 89 FDgtIAENIRYG---KPDATDEEVEEAAKKAnIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV--GEHR 481
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVeqGTHD 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
258-479 |
1.19e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 258 GAPVFSAR------DLRIA-PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPL-AGSMQLDGR-AYAPRTP-- 326
Cdd:PLN03232 611 GAPAISIKngyfswDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSvAYVPQVSwi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 327 -ASAIRDGVFLVAKdrastgivpefniYENmslpflPRFSnmsvtrrRAERQTAREQiaDLKIVCRSERDDLA----TLS 401
Cdd:PLN03232 691 fNATVRENILFGSD-------------FES------ERYW-------RAIDVTALQH--DLDLLPGRDLTEIGergvNIS 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 402 GGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTIVGE 479
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
169-299 |
1.64e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIrRLADRIVSLRDGA-IVGQ---FDEKPLDYEGAVNAMLG 244
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPGAgIFGGevlFNGSPREFLAKSDSLTA 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 245 QNL--GLH-SIDARAAGAPVFSARDLRIAPGAKPLSMELGAGEVVAVTGLVGVGKTRL 299
Cdd:PRK00635 580 KYLrqELTiPIPEKRTNSLGTLTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSL 637
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
274-477 |
1.71e-06 |
|
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: 48.80 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAP---LAGSMQLDGRAYAPrTPASAIRDGVFLVAKDRastgivpef 350
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDV--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 niyenmslpflpRFSNMSVtrrraeRQTareqiadLKIVCRSERDD-LATLSGGNQQKVTVARWLTQPSRLLILDEPFQG 429
Cdd:cd03233 94 ------------HFPTLTV------RET-------LDFALRCKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 430 VDIAARHDIAAKLRESARDRATLVFLTEL---DEALETADRILVMSENTIV 477
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFVSLYqasDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
277-477 |
1.96e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAIRDGVFLV------------AKD-RAS 343
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLviqktrfkkikkIKEiRRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 344 TGIV---PEFNIYENM---SLPFLPRfsNMSVTRRRAErQTAREQIA----DLKIVCRSERDdlatLSGGNQQKVTVARW 413
Cdd:PRK13651 107 VGVVfqfAEYQLFEQTiekDIIFGPV--SMGVSKEEAK-KRAAKYIElvglDESYLQRSPFE----LSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 414 LTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVThDLDNVLEWTKRTIFFKDGKII 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
267-477 |
2.28e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 48.64 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 267 LRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASAIRdgvflVAKDRA 342
Cdd:cd03244 10 LRYRPNLPPvlknISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV------DISKIG-----LHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 343 STGIVPE----FN--IYENmsLPFLPRFSNmsvtrrrAERQTAREQIAdLKIVCRSERDDLAT--------LSGGNQQKV 408
Cdd:cd03244 79 RISIIPQdpvlFSgtIRSN--LDPFGEYSD-------EELWQALERVG-LKEFVESLPGGLDTvveeggenLSVGQRQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 409 TVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALEtADRILVMSENTIV 477
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
274-477 |
3.12e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.72 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRtpasairDGVFLVAKDRASTGIVpeFNIY 353
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-------DADALAQLRREHFGFI--FQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 EnmSLPFLPRFSNMSV------TRRRAERQTAREQIADLKIvcrSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK10535 96 H--LLSHLTAAQNVEVpavyagLERKQRLLRAQELLQRLGL---EDRVEYqpSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETADRILVMSENTIV 477
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
152-477 |
3.39e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 152 RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRAR-GVAILYISHRMSDIRRLADRIVSLRDGAIVGQ--- 227
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETgsv 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 228 ---FDEKPLDYEGA-------VNAMLGQNL----GLHSI------------DARAAGAPVFSARDL-------------- 267
Cdd:PRK10261 254 eqiFHAPQHPYTRAllaavpqLGAMKGLDYprrfPLISLehpakqeppieqDTVVDGEPILQVRNLvtrfplrsgllnrv 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 268 -RIAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR---AYAPRTPASAIRDGVFLVAKDRAS 343
Cdd:PRK10261 334 tREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYAS 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 344 tgIVPEFNIYENMSLPFLprfsnmsvTRRRAERQTAREQIADLkivcrSERDDLA---------TLSGGNQQKVTVARWL 414
Cdd:PRK10261 414 --LDPRQTVGDSIMEPLR--------VHGLLPGKAAAARVAWL-----LERVGLLpehawryphEFSGGQRQRICIARAL 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 415 TQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEAL--ETADRILVMSENTIV 477
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVveRISHRVAVMYLGQIV 543
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
260-468 |
3.42e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 260 PVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETL--FGIHAP---LAGSMQLDGR-AYAPRTpasa 329
Cdd:PRK14239 4 PILQVSDLSVYYNKKKalnsVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHnIYSPRT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 330 irDGVFLvakdRASTGIVPE------FNIYENMSLPF-LPRFSNMSVTRRRAERQTAREQIADLkiVCRSERDDLATLSG 402
Cdd:PRK14239 80 --DTVDL----RKEIGMVFQqpnpfpMSIYENVVYGLrLKGIKDKQVLDEAVEKSLKGASIWDE--VKDRLHDSALGLSG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 403 GNQQKVTVARWLTQPSRLLILDEPFQGVDIAArhdiAAKLRESA---RDRATLVFLTeldEALETADRI 468
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPIS----AGKIEETLlglKDDYTMLLVT---RSMQQASRI 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
400-481 |
3.62e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV-- 477
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAqr 530
|
....
gi 1998276353 478 GEHR 481
Cdd:PRK10789 531 GNHD 534
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
264-476 |
3.81e-06 |
|
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: 49.94 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 264 ARDLriAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGrayaprtpasairdgvflvakdraS 343
Cdd:TIGR00957 647 ARDL--PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------------------S 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 344 TGIVPEFNIYENMSLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLA----TLSGGNQQKVTVARWLTQPSR 419
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 420 LLILDEPFQGVDIAARHDIAAKL--RESARDRATLVFLTELDEALETADRILVMSENTI 476
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-224 |
4.49e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.20 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 25 VGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFSPATPAE--AMRAGVVT-VHqnindgvvgaldva 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTdFH-------------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 102 snlVLDRLNGaGSGFFFNPRKVrreaREVAERMGLGIDLSAE---VTDLPLA--DRQMVAIARAMAHEPQVMILDE---- 172
Cdd:PRK10522 408 ---LFDQLLG-PEGKPANPALV----EKWLERLKMAHKLELEdgrISNLKLSkgQKKRLALLLALAEERDILLLDEwaad 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 173 --PTsslssneAERLF--ALIDRLRARGVAILYISHRMSDIRRlADRIVSLRDGAI 224
Cdd:PRK10522 480 qdPH-------FRREFyqVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-485 |
4.80e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRA-----YAPRTpaSAIRdgvfLVAKDrASTGIVP 348
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdYSYRS--QRIR----MIFQD-PSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMSLPFLPRFSNMSVTRRRAERQTAReQIADLKivcrserdDLAT-----LSGGNQQKVTVARWLTQPSRLLIL 423
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIETLR-QVGLLP--------DHASyyphmLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 424 DEPFQGVDIAARHDIAAKLRE-SARDRATLVFLTE-LDEALETADRILVMSENTIVGEHRNADV 485
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLElQEKQGISYIYVTQhLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-216 |
5.20e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 13 TKAFGPNA-VLRGVGLDlRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGvmmlgdRPFSPATPAEAMRAGVVTVHQNIN 91
Cdd:cd03236 7 VHRYGPNSfKLHRLPVP-REGQVLGLVGPNGIGKSTALKILAGKLKPNLG------KFDDPPDWDEILDEFRGSELQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 92 DGVV-GALDVASN-LVLDRLNGAGSG---FFFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQ 166
Cdd:cd03236 80 TKLLeGDVKVIVKpQYVDLIPKAVKGkvgELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1998276353 167 VMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRMSDIRRLADRI 216
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
256-443 |
5.96e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 256 AAGAPVFSARDlriAPGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaPRTPASAIRDGVF 335
Cdd:PRK13543 13 AAHALAFSRNE---EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 336 LvakdRASTGIVPEFNIYENmsLPFLprfsnMSVTRRRAERQTAREqiadLKIVCRSERDD--LATLSGGNQQKVTVARW 413
Cdd:PRK13543 87 L----GHLPGLKADLSTLEN--LHFL-----CGLHGRRAKQMPGSA----LAIVGLAGYEDtlVRQLSAGQKKRLALARL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1998276353 414 LTQPSRLLILDEPFQGVDIAA----RHDIAAKLR 443
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGitlvNRMISAHLR 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
271-477 |
6.84e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 271 PGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAgsmqldgrayAPRTpaSAIRDGVFLVAKD----RASTGI 346
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD----------NPNS--KITVDGITLTAKTvwdiREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 347 VpefniYENMSLPFLPRFSNMSVTRRRAERQTAREQIadLKIVCRSERD---------DLATLSGGNQQKVTVARWLTQP 417
Cdd:PRK13640 89 V-----FQNPDNQFVGATVGDDVAFGLENRAVPRPEM--IKIVRDVLADvgmldyidsEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 418 SRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEAlETADRILVMSENTIV 477
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISIThDIDEA-NMADQVLVLDDGKLL 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-494 |
6.86e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.40 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR--AYAPRTpasairdgvfLVAKdraSTGIVPEFNiyenmslpf 360
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtvSYKPQY----------IKAD---YEGTVRDLL--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 361 lprfsnMSVTRRRAERQTAREQIAD-LKIVCRSERDdLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIA 439
Cdd:cd03237 83 ------SSITKDFYTHPYFKTEIAKpLQIEQILDRE-VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 440 AKLRESARDRATLVFLTELDEALET--ADRILVM----SENTIVGEHRNADVDMDRLLAEV 494
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIDylADRLIVFegepSVNGVANPPQSLRSGMNRFLKNL 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
257-435 |
7.12e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 257 AGAPVFSARDL-RIAPGAKPL-------------SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGR--A 320
Cdd:PRK11308 1 SQQPLLQAIDLkKHYPVKRGLfkperlvkaldgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdlL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 321 YAPRTPASAIRDGVFLVAKD-------RASTGIVPEFNIYENMSLPflprfsnmsvtrrRAERqtaREQIADL--KIVCR 391
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNpygslnpRKKVGQILEEPLLINTSLS-------------AAER---REKALAMmaKVGLR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276353 392 SERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAAR 435
Cdd:PRK11308 145 PEHYDRypHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
270-477 |
7.48e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 270 APGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPASAirdgvflvakdRASTGIVPE 349
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL-----------RRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 ----FN--IYENMSLPfLPRFSNMSVtRRRAERQTAREQIAdlkivcRSErDDLAT--------LSGGNQQKVTVARWLT 415
Cdd:PRK13657 417 daglFNrsIEDNIRVG-RPDATDEEM-RAAAERAQAHDFIE------RKP-DGYDTvvgergrqLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276353 416 QPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELdEALETADRILVMSENTIV 477
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVV 548
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
274-479 |
8.25e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASAIRDGVFLVakdRASTGIV---PEF 350
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE------PIKYDKKSLLEV---RKTVGIVfqnPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 351 NIYE---NMSLPFLPRfsNMSVTRRRAERQTAREqiadLKIVCRS--ERDDLATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK13639 90 QLFAptvEEDVAFGPL--NLGLSKEEVEKRVKEA----LKAVGMEgfENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 426 PFQGVDIAARHDIAAKLRESARDRATLVFLT-ELDEALETADRILVMSENTIVGE 479
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGITIIISThDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
398-500 |
8.31e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 398 ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTE-LDEALETADRILVMSENTI 476
Cdd:NF000106 143 AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQyMEEAEQLAHELTVIDRGRV 222
|
90 100
....*....|....*....|....
gi 1998276353 477 VgehrnADVDMDRLLAEVAGQRLE 500
Cdd:NF000106 223 I-----ADGKVDELKTKVGGRTLQ 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
261-485 |
8.89e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.21 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 261 VFSARDLRIAPGA----KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGI-----HAPLAGSMQLDGRAYApRTPASAIR 331
Cdd:PRK14247 3 KIEIRDLKVSFGQvevlDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF-KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 332 DGVFLVAKdraSTGIVPEFNIYENMSL-PFLPRfsnmsVTRRRAERQTAREQIADLKIVCRSERDDL----ATLSGGNQQ 406
Cdd:PRK14247 82 RRVQMVFQ---IPNPIPNLSIFENVALgLKLNR-----LVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 407 KVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDrATLVFLTEL-DEALETADRILVMSENTIVGEHRNADV 485
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFpQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-240 |
1.07e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 22 LRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVhradrgvmmlgdrpFSPaTPAEAMRAGVVTVHQnINDGVVGALDVA 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGS--------------LSP-TVGKVDRNGEVSVIA-ISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 102 SNLVLDRLNGAgsgffFNPRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNE 181
Cdd:PRK13546 104 ENIEFKMLCMG-----FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 182 AERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLRDGAI--VGQFDEKPLDYEGAVN 240
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLkdYGELDDVLPKYEAFLN 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
363-477 |
1.20e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.80 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 363 RFSNMSVTRR--RAERQTAREQIADLKIVCRSERDdLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAA 440
Cdd:PRK15056 105 RYGHMGWLRRakKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS 183
|
90 100 110
....*....|....*....|....*....|....*...
gi 1998276353 441 KLRE-SARDRATLVFLTELDEALETADRIlVMSENTIV 477
Cdd:PRK15056 184 LLRElRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVL 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-182 |
1.37e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGvhrADRGVMMLGDRPFSPATPAEAMRAGVvtvhqninDGVVGALDV 100
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARI--------SGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 101 ASNLVLDRLNGAGSGFFFNPRKVRREAR-----EVAERMGL-----GIDLSAEVTDLPLADRQMVAIARAMAHEPQVMIL 170
Cdd:PLN03140 964 HSPQVTVRESLIYSAFLRLPKEVSKEEKmmfvdEVMELVELdnlkdAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170
....*....|..
gi 1998276353 171 DEPTSSLSSNEA 182
Cdd:PLN03140 1044 DEPTSGLDARAA 1055
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-229 |
1.39e-05 |
|
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: 48.02 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVK-------------VMSGVHRADRGVMMLGDR----PFSPATPAEAMRAGV 83
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLglfrinesaegeiIIDGLNIAKIGLHDLRFKitiiPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINDGVVGALDVAsnlvldRLNGAGSGFffnPRKVRREAREVAERMGLGidlsaevtdlplaDRQMVAIARAMAH 163
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELA------HLKTFVSAL---PDKLDHECAEGGENLSVG-------------QRQLVCLARALLR 1438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 164 EPQVMILDEPTSSLSSnEAERLFALIDRLRARGVAILYISHRMSDIRRLAdRIVSLrDGAIVGQFD 229
Cdd:TIGR00957 1439 KTKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVL-DKGEVAEFG 1501
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
277-477 |
1.40e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGraYAPRTPASAIRDgvflVAKDRASTGIV---PEFNIY 353
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD--YAIPANLKKIKE----VKRLRKEIGLVfqfPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 354 ENM---SLPFLPrfsnmsvTRRRAERQTAREQIADLKIVCRSERDDLA----TLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:PRK13645 105 QETiekDIAFGP-------VNLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 427 FQGVDIAARHD-IAAKLRESARDRATLVFLTE-LDEALETADRILVMSENTIV 477
Cdd:PRK13645 178 TGGLDPKGEEDfINLFERLNKEYKKRIIMVTHnMDQVLRIADEVIVMHEGKVI 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-225 |
1.44e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 21 VLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDR-----------------PFSPATPAEAMRAGV 83
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfgltdlrrvlsiiPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 84 VTVHQNINDGVVGALDvasnlvldrlngagsgfffnprkvRREAREVAERMGLGIDlsAEVTD----LPLADRQMVAIAR 159
Cdd:PLN03232 1331 DPFSEHNDADLWEALE------------------------RAHIKDVIDRNPFGLD--AEVSEggenFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276353 160 AMAHEPQVMILDEPTSSLSSneaeRLFALIDR-LRA--RGVAILYISHRMSDIRRlADRIVSLRDGAIV 225
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDV----RTDSLIQRtIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
256-480 |
1.98e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 256 AAGAPVFSARDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPrtpasair 331
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPvlhgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-------- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 332 dgvFLVAKDRASTGIVPEFNIYENMSLPF-LPRFSNmsvtRRRAERQTAREQiADLKIVCRSERDDL--------ATLSG 402
Cdd:PLN03232 1303 ---FGLTDLRRVLSIIPQSPVLFSGTVRFnIDPFSE----HNDADLWEALER-AHIKDVIDRNPFGLdaevseggENFSV 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 403 GNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALEtADRILVMSENTIVgEH 480
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL-EY 1450
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
267-477 |
2.04e-05 |
|
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: 45.48 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 267 LRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRDGVFLVAKDra 342
Cdd:cd03369 14 VRYAPDLPPvlknVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 343 stgivpefniyenmslPFLprFS-NMSVTRRRAERQTAREQIADLKIvcrSERDDlaTLSGGNQQKVTVARWLTQPSRLL 421
Cdd:cd03369 91 ----------------PTL--FSgTIRSNLDPFDEYSDEEIYGALRV---SEGGL--NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 422 ILDEPFQGVDIAARHDIAAKLRESARDrATLVFLTELDEALETADRILVMSENTIV 477
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTN-STILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
400-479 |
2.30e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRE-SARDRATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSThQLDLVPEMADYIYVMDKGRIV 217
|
..
gi 1998276353 478 GE 479
Cdd:PRK13652 218 AY 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-62 |
2.63e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 2.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 3 DTAIFRIA----GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGV 62
Cdd:PRK15064 312 DKKLHRNAleveNLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
147-207 |
2.65e-05 |
|
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: 46.67 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 147 LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALidrLRARGVAILYISHRMS 207
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVSHRKS 640
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-54 |
2.81e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 2.81e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1998276353 19 NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSG 54
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
127-225 |
2.83e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 127 AREVAERMGLGID-LSAEVTDLPLADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHR 205
Cdd:PRK13651 145 AAKYIELVGLDESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
90 100
....*....|....*....|
gi 1998276353 206 MSDIRRLADRIVSLRDGAIV 225
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKII 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
277-479 |
3.41e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 45.41 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 277 SMELGAGEVVAVTGLVGVGKTrlaeTLF----GIHAPLAGSMQLDGrayaprtpasairdgvflvaKD--------RAST 344
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKT----TTFymivGLVKPDSGRIFLDG--------------------EDithlpmhkRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVpefniyenmslpFLPR----FSNMSV-----------TRRRAERQTAREQ-IADLKIVCRseRDDLA-TLSGGNQQK 407
Cdd:COG1137 79 GIG------------YLPQeasiFRKLTVednilavlelrKLSKKEREERLEElLEEFGITHL--RKSKAySLSGGERRR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 408 VTVARWL-TQPSRLLiLDEPFQGVD-IAArHDIAAKLREsARDRATLVFLTelD----EALETADRILVMSENTIVGE 479
Cdd:COG1137 145 VEIARALaTNPKFIL-LDEPFAGVDpIAV-ADIQKIIRH-LKERGIGVLIT--DhnvrETLGICDRAYIISEGKVLAE 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-210 |
3.77e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 3.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 152 RQMVAIARAMAHEPQVMILDEPTSSLsSNEAERLF-ALIDRLRARGVAI-LYISHRMSDIR 210
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLKGNENRItIIIAHRLSTIR 644
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
276-476 |
3.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.51 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTpASAIRD--GVFLVAKDRASTGIVPEFNI- 352
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-FEKLRKhiGIVFQNPDNQFVGSIVKYDVa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 353 --YENMSLPFlprfSNMsvtrrraeRQTAREQIADLKIVCRSErDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGV 430
Cdd:PRK13648 107 fgLENHAVPY----DEM--------HRRVSEALKQVDMLERAD-YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 431 DIAARHDIAAKLRESARDR-ATLVFLT-ELDEALEtADRILVMSENTI 476
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHnITIISIThDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
276-466 |
7.82e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAyaprtpasairdgvflVAKDRAS-----------T 344
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS----------------IKKDLCTyqkqlcfvghrS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 345 GIVPEFNIYENMSLPFLPRFSNMSVTRrrAERQTAREQIADLKivCrserddlATLSGGNQQKVTVARWLTQPSRLLILD 424
Cdd:PRK13540 84 GINPYLTLRENCLYDIHFSPGAVGITE--LCRLFSLEHLIDYP--C-------GLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1998276353 425 EPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALETAD 466
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-195 |
8.22e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 8 RIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG-VMMLG----DRPFSPAT-PAEA-MR 80
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVLGgdmaDARHRRAVcPRIAyMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 81 AGV-------VTVHQNINdgvvgaldvasnlvldrlngagsgFF---FNPRKVRREARevaermglgIDLSAEVTDL-PL 149
Cdd:NF033858 83 QGLgknlyptLSVFENLD------------------------FFgrlFGQDAAERRRR---------IDELLRATGLaPF 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 150 ADR----------QMVAIARAMAHEPQVMILDEPTSS---LSsneaERLF-ALIDRLRAR 195
Cdd:NF033858 130 ADRpagklsggmkQKLGLCCALIHDPDLLILDEPTTGvdpLS----RRQFwELIDRIRAE 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-223 |
8.49e-05 |
|
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: 43.86 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 15 AFGPN-AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDR-PFSPATPAEAMRAGVVTVHQNIND 92
Cdd:cd03290 9 SWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 93 GVVGAlDVASNLVLdrlngaGSGFFFNPRKVRREA---------------REVAERmglGIDLSAevtdlplADRQMVAI 157
Cdd:cd03290 89 WLLNA-TVEENITF------GSPFNKQRYKAVTDAcslqpdidllpfgdqTEIGER---GINLSG-------GQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 158 ARAMAHEPQVMILDEPTSSLSSNEAERLF--ALIDRLRARGVAILYISHRMSDIRRlADRIVSLRDGA 223
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
243-479 |
9.91e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 243 LGQNLGLHSIDAraaGAPVFSARDLRIAPGAKPL----SMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAG-----S 313
Cdd:PRK14271 6 LGGQSGAADVDA---AAPAMAAVNLTLGFAGKTVldqvSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 314 MQLDGRAYAPRTPASAIRDGVFLVAKdraSTGIVPeFNIYENMslpfLPRFSNMSVTRRRAERQTAREQIADLKI---VC 390
Cdd:PRK14271 83 VLLGGRSIFNYRDVLEFRRRVGMLFQ---RPNPFP-MSIMDNV----LAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 391 RSERDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESArDRATLVFLTE-LDEALETADRIL 469
Cdd:PRK14271 155 DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHnLAQAARISDRAA 233
|
250
....*....|
gi 1998276353 470 VMSENTIVGE 479
Cdd:PRK14271 234 LFFDGRLVEE 243
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
105-227 |
1.01e-04 |
|
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: 44.14 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 105 VLDRLNGAGSGFFFNPRKVRREAREVAErMGLG-IDLSAEVTDLPLADRQMVAIARAMAHE---PQVMILDEPTSSLSSN 180
Cdd:cd03271 128 VLDMTVEEALEFFENIPKIARKLQTLCD-VGLGyIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFH 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 181 EAERLFALIDRLRARGVAILYISHRMsDIRRLADRIVSL------RDGAIVGQ 227
Cdd:cd03271 207 DVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWIIDLgpeggdGGGQVVAS 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-484 |
1.16e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 400 LSGGNQQKVTVAR-WLTQPsRLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLT-ELDEALETADRILVMSENTI 476
Cdd:PRK15134 157 LSGGERQRVMIAMaLLTRP-ELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFIThNLSIVRKLADRVAVMQNGRC 235
|
....*...
gi 1998276353 477 VgEHRNAD 484
Cdd:PRK15134 236 V-EQNRAA 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
398-477 |
1.55e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 398 ATLSGGNQQKVTVAR-WLTQPSrLLILDEPFQGVDIAARHDIAAKLRESARD-RATLVFLTE-LDEALETADRILVMSEN 474
Cdd:PRK11144 127 GSLSGGEKQRVAIGRaLLTAPE-LLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHsLDEILRLADRVVVLEQG 205
|
...
gi 1998276353 475 TIV 477
Cdd:PRK11144 206 KVK 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-471 |
1.97e-04 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 43.50 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLA---GSMQLDGRAYAPRTPA--SAIRDG-VFLVAKDrASTGIVPE 349
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKelRKIRGReIQMIFQD-PMTSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FNIYENMSLPFLprfsnmsvTRRRAERQTAREQIAD-LKIVCRSERDDLAT-----LSGGNQQKVTVARWL-TQPsRLLI 422
Cdd:COG0444 103 MTVGDQIAEPLR--------IHGGLSKAEARERAIElLERVGLPDPERRLDrypheLSGGMRQRVMIARALaLEP-KLLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 423 LDEPFQGVDIAARHDIAAKLRESARDR-ATLVFLT-ELDEALETADRILVM 471
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRELgLAILFIThDLGVVAEIADRVAVM 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-456 |
2.25e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHApLAGSMQLDGRA-------YAPRTPASAIRDGVFLVakdRASTGIVP 348
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVeffnqniYERRVNLNRLRRQVSMV---HPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 eFNIYENMS-----LPFLPRFSNMSVTRRRAERQTAREQIADLkiVCRSERDdlatLSGGNQQKVTVARWLTQPSRLLIL 423
Cdd:PRK14258 102 -MSVYDNVAygvkiVGWRPKLEIDDIVESALKDADLWDEIKHK--IHKSALD----LSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....
gi 1998276353 424 DEPFQGVDIAARHDIAAKLRESA-RDRATLVFLT 456
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRlRSELTMVIVS 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
270-475 |
2.29e-04 |
|
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: 44.23 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 270 APGAKPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRtpasairdgvflVAKDRASTGIVPE 349
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------------ISDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 350 FNIYENM--SLPFLPRFSNMSVTRRRAERQTAREQIADLKIVCRSERddLA-TLSGGNQQKVTVARWLTQPSRLLILDEP 426
Cdd:TIGR01257 2020 FDAIDDLltGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADR--LAgTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 427 FQGVDIAAR----HDIAAKLREsarDRATLVFLTELDEALETADRILVMSENT 475
Cdd:TIGR01257 2098 TTGMDPQARrmlwNTIVSIIRE---GRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-227 |
2.83e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 9 IAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRG--------VMMLGDRPFSPATPAEAM- 79
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenIPAMSRSRLYTVRKRMSMl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 -RAGVVTVHQNINDGVVGALDVASNL--------VLDRLNGAGsgfffnprkvrreAREVAERMglgidlSAEVTDlPLA 150
Cdd:PRK11831 90 fQSGALFTDMNVFDNVAYPLREHTQLpapllhstVMMKLEAVG-------------LRGAAKLM------PSELSG-GMA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 151 DRqmVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRIVSLRDGAIVGQ 227
Cdd:PRK11831 150 RR--AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
372-485 |
3.10e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 372 RRAERQTAREQIADLKIVCRSERDDL--ATLSGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRE-SARD 448
Cdd:PRK11022 124 KKTRRQRAIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKE 203
|
90 100 110
....*....|....*....|....*....|....*....
gi 1998276353 449 RATLVFLTElDEAL--ETADRILVMSENTIVGEHRNADV 485
Cdd:PRK11022 204 NMALVLITH-DLALvaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
265-477 |
3.27e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 41.74 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGAKP----LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLA--GSMQLDGRayaprtpasairDGVFLVA 338
Cdd:cd03217 4 KDLHVSVGGKEilkgVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGE------------DITDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 339 KDRASTGIVpefniyenMSLPFLPRFSNMSVtrrraerqtareqiADLKivcrseRDDLATLSGGNQQKVTVARWLTQPS 418
Cdd:cd03217 72 EERARLGIF--------LAFQYPPEIPGVKN--------------ADFL------RYVNEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 419 RLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELDEALE--TADRILVMSENTIV 477
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
397-471 |
4.91e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 397 LATLSGGNQQKVTVARWLTQPSR--LLILDEPFQGVDiaarHDIAAKLRESAR---DRATLVFLTELDEA-LETADRILV 470
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH----QQDINQLLEVIKgliDLGNTVILIEHNLDvLSSADWIID 160
|
.
gi 1998276353 471 M 471
Cdd:cd03238 161 F 161
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
274-480 |
5.24e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.79 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRayaprtPASA-----IRDGVFLVAKDRASTGIVP 348
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV------PLVQydhhyLHRQVALVGQEPVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 349 EFNIYENMslpflpRFSNMSVTRRRAERQTAREQIADLKIVCRSERDDLAT-LSGGNQQKVTVARWLTQPSRLLILDEPF 427
Cdd:TIGR00958 572 RENIAYGL------TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 428 QGVDIAARHdiAAKLRESARDRATLVFLTELDEAlETADRILVMSENTIV--GEH 480
Cdd:TIGR00958 646 SALDAECEQ--LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVemGTH 697
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-200 |
6.09e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.37 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 11 GLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRpfsPATPAEAMRAGVVTVHQni 90
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 91 nDGVVGALDVASNL-VLDRLNGagsgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAMAHEPQVMI 169
Cdd:PRK13543 91 -PGLKADLSTLENLhFLCGLHG---------RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1998276353 170 LDEPTSSLSSNEAERLFALID-RLRARGVAIL 200
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISaHLRGGGAALV 192
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-233 |
6.48e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 19 NAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGDRPFsPATPAEAMRAGVVTVHQN---INDgvv 95
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL-TKLQLDSWRSRLAVVSQTpflFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 96 galDVASNLVLDRLNGAgsgfffnPRKVRREAR-----------------EVAERmglGIDLSAevtdlplADRQMVAIA 158
Cdd:PRK10789 404 ---TVANNIALGRPDAT-------QQEIEHVARlasvhddilrlpqgydtEVGER---GVMLSG-------GQKQRISIA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 159 RAMAHEPQVMILDEptsSLSSNEAERLFALIDRLR--ARGVAILYISHRMSDIRRlADRIVSLRDGAIVGQFDEKPL 233
Cdd:PRK10789 464 RALLLNAEILILDD---ALSAVDGRTEHQILHNLRqwGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
29-204 |
7.72e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.83 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 29 LRAGEVTVLMGANGAGKSTLVKVMSgvhradrgVMMLGDRPFsPATPAEAMRAGVvtvhqnindgVVGALDVASNLVLDR 108
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLA--------AAVATGKPW-LGGPRVPEQGKV----------LYVSAEGPADELRRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 109 LNGAGsgfffnpRKVRREAREVAERMGLGIDLSAEVTDLPLADRQMVAIARAM--AHEPQVMILDEPTSSLSSNE----- 181
Cdd:pfam13481 91 LRAAG-------ADLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALeeVEDPDLVVIDPLARALGGDEnsnsd 163
|
170 180
....*....|....*....|....
gi 1998276353 182 AERLFALIDRLRAR-GVAILYISH 204
Cdd:pfam13481 164 VGRLVKALDRLARRtGATVLLVHH 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-67 |
7.92e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 7.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 2 GDTAIfRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLGD 67
Cdd:PRK11819 321 GDKVI-EAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
283-473 |
8.26e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.17 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 283 GEVVAVTGLVGVGKTRLAETLFG-IHAP-LAGSMQLDGRayaprTPASAIRDGVFLVAKDRAstgIVPEFNIYENM---S 357
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGrIQGNnFTGTILANNR-----KPTKQILKRTGFVTQDDI---LYPHLTVRETLvfcS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 358 LPFLPRfsnmSVTRRRAERqTAREQIADLKIV-CRSE---RDDLATLSGGNQQKVTVA-RWLTQPSrLLILDEPFQGVDI 432
Cdd:PLN03211 166 LLRLPK----SLTKQEKIL-VAESVISELGLTkCENTiigNSFIRGISGGERKRVSIAhEMLINPS-LLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1998276353 433 AARHDIAAKLRESARDRATLVflTELDE----ALETADRILVMSE 473
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIV--TSMHQpssrVYQMFDSVLVLSE 282
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-225 |
8.67e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 10 AGLTKAFGPN-----AVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMS----GVHRADRGVMMlgdrpFSPATPAEAM- 79
Cdd:TIGR00956 60 RGFRKLKKFRdtktfDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVIT-----YDGITPEEIKk 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 80 --RAGVVTVHQniNDGVVGALDVASNLVLD-RLNGAGSGFFFNPRKVRREA-REVAER-MGLGIDLSAEVTD-----LPL 149
Cdd:TIGR00956 135 hyRGDVVYNAE--TDVHFPHLTVGETLDFAaRCKTPQNRPDGVSREEYAKHiADVYMAtYGLSHTRNTKVGNdfvrgVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 150 ADRQMVAIARAMAHEPQVMILDEPTSSLSSNEAerlFALIDRLRARG--------VAILYISHrmsDIRRLADRIVSLRD 221
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATA---LEFIRALKTSAnildttplVAIYQCSQ---DAYELFDKVIVLYE 286
|
....
gi 1998276353 222 GAIV 225
Cdd:TIGR00956 287 GYQI 290
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
169-223 |
1.28e-03 |
|
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: 40.32 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1998276353 169 ILDEPTSSLSSNEAERLFALIDRLRARGVAILYISHRmSDIRRLADRIVSLRDGA 223
Cdd:cd03270 162 VLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIGPGA 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
276-476 |
1.32e-03 |
|
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: 41.43 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIhAPLAGSMQLDGRAYaprtpasairDGVFLvAKDRASTGIVPE----FN 351
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSW----------NSVTL-QTWRKAFGVIPQkvfiFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 IYENMSLPFLPRFSNMSVTRRRAE--RQTAREQIAD-LKIVCRserDDLATLSGGNQQKVTVARWLTQPSRLLILDEPFQ 428
Cdd:TIGR01271 1306 GTFRKNLDPYEQWSDEEIWKVAEEvgLKSVIEQFPDkLDFVLV---DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1998276353 429 GVDIAARHDIAAKLRESARDrATLVFLTELDEALETADRILVMSENTI 476
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-227 |
1.37e-03 |
|
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: 41.54 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 116 FFFNPRKVRREAREVAErMGLG-IDLSAEVTDLPLADRQMVAIARAM---AHEPQVMILDEPTSSLSSNEAERLFALIDR 191
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCD-VGLGyIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQR 877
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1998276353 192 LRARGVAILYISHRMsDIRRLADRIVSL------RDGAIVGQ 227
Cdd:TIGR00630 878 LVDKGNTVVVIEHNL-DVIKTADYIIDLgpeggdGGGTVVAS 918
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-236 |
1.79e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 6 IFRIAGLTKAFGPNAVLRGVGLDLRAGEVTVLMGANGAGKSTLVKVMSGVHRADRGVMMLgdrpfspatpAEAMRAGVVT 85
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AKGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 86 VHQ----NINDGVVGALD-VASNLVLDRLNGAGSGFFFNPRKVrreaREVAERMGLGidlsaevtdlplaDRQMVAIARA 160
Cdd:PRK10636 382 QHQleflRADESPLQHLArLAPQELEQKLRDYLGGFGFQGDKV----TEETRRFSGG-------------EKARLVLALI 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 161 MAHEPQVMILDEPTSSLSSNEAERLF-ALIDrlrARGvAILYISHRMSDIRRLADRIVSLRDGAiVGQFDEKPLDYE 236
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTeALID---FEG-ALVVVSHDRHLLRSTTDDLYLVHDGK-VEPFDGDLEDYQ 516
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
265-456 |
1.90e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.21 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 265 RDLRIAPGA----KPLSMELGAGEVVAVTGLVGVGKTRLAETL-----FGIHAPLAGSMQLDGRA-YAPRTPASAIRDGV 334
Cdd:PRK14267 8 VNLRVYYGSnhviKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNiYSPDVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 335 FLVAKdraSTGIVPEFNIYENMSLPFlpRFSNMSVTRRRAERQT--AREQIADLKIVCRSERDDLATLSGGNQQKVTVAR 412
Cdd:PRK14267 88 GMVFQ---YPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERVewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1998276353 413 WLTQPSRLLILDEPFQGVDIAARHDIAAKLREsARDRATLVFLT 456
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFE-LKKEYTIVLVT 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
262-471 |
2.14e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.07 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 262 FSARDLRIAPGAKP--------LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPAS--AIR 331
Cdd:PRK15079 18 FDIKDGKQWFWQPPktlkavdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 332 DGVFLVAKDR-AStgIVPEFNIYENMSLPFLPRFSNMSvtrrraeRQTAREQIADL--------KIVCRSERDdlatLSG 402
Cdd:PRK15079 98 SDIQMIFQDPlAS--LNPRMTIGEIIAEPLRTYHPKLS-------RQEVKDRVKAMmlkvgllpNLINRYPHE----FSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998276353 403 GNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRA-TLVFLT-ELDEALETADRILVM 471
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGlSLIFIAhDLAVVKHISDRVLVM 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
276-425 |
2.33e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 39.70 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 276 LSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYAPRTPaSAIRDGVFLVAKDRASTGIvpefNIYEN 355
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFGD----TVYDN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 356 MSLPFLPRfsnmsvtRRRAERQTAREQIADLKIVCRSERDDLATLSGGNQQKVTVARWLTQPSRLLILDE 425
Cdd:PRK10247 101 LIFPWQIR-------NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
124-248 |
3.93e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 124 RREAREVAERMGLGIDlsAEVTD----LPLADRQMVAIARAMAHEPQVMILDEPTSSLSSneaeRLFALID---RLRARG 196
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLD--AEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDV----RTDALIQktiREEFKS 1423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1998276353 197 VAILYISHRMSDIRRlADRIVSLRDGAIVgQFD--EKPLDYEGAVNAMLGQNLG 248
Cdd:PLN03130 1424 CTMLIIAHRLNTIID-CDRILVLDAGRVV-EFDtpENLLSNEGSAFSKMVQSTG 1475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
150-220 |
4.83e-03 |
|
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: 37.74 E-value: 4.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276353 150 ADRQMVAIARAMAHEPQVMILDEPTSSLSS------NEAERLFALIDRLRARGVAILYISHRMSDIRRLADRIVSLR 220
Cdd:smart00382 64 ELRLRLALALARKLKPDVLILDEITSLLDAeqeallLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
401-477 |
7.43e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 401 SGGNQQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTEL---DEALETADRILVMSENTIV 477
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYqcsQDAYELFDKVIVLYEGYQI 290
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
419-498 |
7.57e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.53 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 419 RLLILDEPFQGVDIAARHDIAAKLRESARDRATLVFLTELD----EALetADRILVMSENTIVgehrnADVDMDRLLAEV 494
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEAL--CDRVIVIDHGRII-----YDGSLEELKERF 246
|
....
gi 1998276353 495 AGQR 498
Cdd:COG4586 247 GPYK 250
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
261-466 |
8.86e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.22 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 261 VFSARDLRIAPGA----KPLSMELGAGEVVAVTGLVGVGKTRLAETlFGIHAPLAGSMQLDGRA-------YAPRTPASA 329
Cdd:PRK14243 10 VLRTENLNVYYGSflavKNVWLDIPKNQITAFIGPSGCGKSTILRC-FNRLNDLIPGFRVEGKVtfhgknlYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 330 IRDGVFLVAKdraSTGIVPEfNIYENMSlpFLPRFS----NMSVTRRRAERQTAR-EQIADlKIvcrseRDDLATLSGGN 404
Cdd:PRK14243 89 VRRRIGMVFQ---KPNPFPK-SIYDNIA--YGARINgykgDMDELVERSLRQAALwDEVKD-KL-----KQSGLSLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276353 405 QQKVTVARWLTQPSRLLILDEPFQGVDIAARHDIAAKLREsARDRATLVFLTE-LDEALETAD 466
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHnMQQAARVSD 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
152-216 |
9.15e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 38.17 E-value: 9.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276353 152 RQMVAIARAMAHEPQVMILDEPTSSLSSNEAERLFALIDRL-RARGVAILYISHRMSDIRRLADRI 216
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKV 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
274-477 |
9.40e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 38.14 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 274 KPLSMELGAGEVVAVTGLVGVGKTRLAETLFGIHAPLAGSMQLDGRAYApRTPASAIRdgvflvaKDRASTGIVPE-FN- 351
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT-ALSERELR-------AARRKIGMIFQhFNl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276353 352 -----IYENMSLPFlpRFSNMSvtrrRAERqtaREQIADL-KIVCRSERDD--LATLSGGNQQKVTVARWL-TQPSrLLI 422
Cdd:COG1135 94 lssrtVAENVALPL--EIAGVP----KAEI---RKRVAELlELVGLSDKADayPSQLSGGQKQRVGIARALaNNPK-VLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276353 423 LDEPFQGVDIAARHDIAAKLREsARDR--ATLVFLT-ELDEALETADRILVMSENTIV 477
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKD-INRElgLTIVLIThEMDVVRRICDRVAVLENGRIV 220
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