|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-497 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 713.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDV-GMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTkGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVGHQ 238
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 239 VTKRVSDRSVAPGREVLVVDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEA 318
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 319 IVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKPEYRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVE 398
Cdd:COG3845 322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 399 RLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
490
....*....|....*....
gi 1550121285 479 GTVRPEETTLLELGMMMAG 497
Cdd:COG3845 482 GEVPAAEATREEIGLLMAG 500
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-487 |
3.34e-170 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 489.91 E-value: 3.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGRePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVGHQ 238
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 239 VTKRVSDRSVAPGREVLVVDHAvaigeWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEA 318
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGL-----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 319 IVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKpeYRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVE 398
Cdd:COG1129 316 VRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDR--LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 399 RLSGGNAQRVILAReFLNAKC-LLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:COG1129 394 NLSGGNQQKVVLAK-WLATDPkVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
490
....*....|
gi 1550121285 478 VGTVRPEETT 487
Cdd:COG1129 473 VGELDREEAT 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-479 |
7.27e-104 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 320.34 E-value: 7.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS--GVIRFKGQVAELNSPADALR 78
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQHFVLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNeITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVG 236
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 237 HQVTKRVSDRSVAPGREVLVVDHAVAigeW-----GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGV-RTLSSG 310
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTA---WdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 311 RFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKpeYRRGPFLDRGKINDLAQRKLEEFRIVA 390
Cdd:PRK13549 319 EIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDR--FTGGSRIDDAAELKTILESIQRLKVKT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 391 ASTDLPVERLSGGNAQRVILAREFL-NAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRI 469
Cdd:PRK13549 397 ASPELAIARLSGGNQQKAVLAKCLLlNPKILIL-DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRV 475
|
490
....*....|
gi 1550121285 470 AVIFKGKIVG 479
Cdd:PRK13549 476 LVMHEGKLKG 485
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-493 |
1.58e-93 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 293.74 E-value: 1.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVAT-VETATTTAESITALMVGH 237
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVATfDDMAQVDRDQLVQAMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 238 QVTKRVSDRSVAPGREVLVVDHAVAIGewgeeVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE 317
Cdd:PRK11288 241 EIGDIYGYRPRPLGEVRLRLDGLKGPG-----LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 318 AIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKpEYRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPV 397
Cdd:PRK11288 316 PIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRH-HLRAGCLINNRWEAENADRFIRSLNIKTPSREQLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 398 ERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
490
....*....|....*....
gi 1550121285 478 VGTV-RPE--ETTLLELGM 493
Cdd:PRK11288 475 AGELaREQatERQALSLAL 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-477 |
1.27e-92 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 291.69 E-value: 1.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSpdvgmLLSK----------STARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEI 150
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGR-----HLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 151 LKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAES 229
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 230 ITALMVGHQVTKRVSDRSVAPGREVL-VVDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS 308
Cdd:PRK09700 237 IVRLMVGRELQNRFNAMKENVSNLAHeTVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 309 SGRFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKPEYRRGP--FLDRGKINDLAQRKLEEF 386
Cdd:PRK09700 317 GGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAmgLFHEVDEQRTAENQRELL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 387 RIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYeKILEKRA-EGFAVFLASEELDDLLRL 465
Cdd:PRK09700 397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-KVMRQLAdDGKVILMVSSELPEIITV 475
|
490
....*....|..
gi 1550121285 466 CDRIAVIFKGKI 477
Cdd:PRK09700 476 CDRIAVFCEGRL 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-491 |
4.76e-91 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 287.01 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 9 NLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGIGMVHQHF 88
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 89 VLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRyPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 168 AVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVGHQVTKRVSDR 246
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 247 SVAPGREVLVVDHAVAIgewGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRE 326
Cdd:PRK10982 243 ENKPGEVILEVRNLTSL---RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 327 MLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKPEYRRGpFLDRGKINDLAQRKLEEFRIVAASTDLPVERLSGGNAQ 406
Cdd:PRK10982 320 AINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVG-LLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 407 RVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEET 486
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTT 478
|
....*
gi 1550121285 487 TLLEL 491
Cdd:PRK10982 479 TQNEI 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-487 |
9.39e-88 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 278.60 E-value: 9.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS--GVIRFKGQVAELNSPADALRLGI 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNeRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAES--ITALMVGH 237
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIETLDCRADEVTEdrIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 238 QVTKRVSDRSVAPGREVLVVDHavaigeW--------GEEVLCDINFTIAENEILGLAGVAGNGQKEL----FEVLMGVR 305
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKN------WtvyhplhpERKVVDDVSLNVRRGEIVGIAGLMGAGRTELamsvFGRSYGRN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 306 TlsSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKpeyrrgpFLDRGKINDLAQRKL-E 384
Cdd:NF040905 315 I--SGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGK-------VSRRGVIDENEEIKVaE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 385 EFR----IVAASTDLPVERLSGGNAQRVILAR-EFLNAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEEL 459
Cdd:NF040905 386 EYRkkmnIKTPSVFQKVGNLSGGNQQKVVLSKwLFTDPDVLIL-DEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
|
490 500
....*....|....*....|....*...
gi 1550121285 460 DDLLRLCDRIAVIFKGKIVGTVRPEETT 487
Cdd:NF040905 465 PELLGMCDRIYVMNEGRITGELPREEAS 492
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-487 |
1.01e-87 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 278.43 E-value: 1.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDV---GMLLSKSTaRQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVnrfGRIDWKKM-YAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVG 236
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFIAEREVADLTEDSLIEMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 237 HQVTKRVSDRSVAPGREVLVVDHAVAIGewgeevLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNG 316
Cdd:PRK10762 240 RKLEDQYPRLDKAPGEVRLKVDNLSGPG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 317 EAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKPEYRRGPfLDRGKINDLAQRKLEEFRIVAASTDLP 396
Cdd:PRK10762 314 HEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGS-LKHADEQQAVSDFIRLFNIKTPSMEQA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 397 VERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
490
....*....|.
gi 1550121285 477 IVGTVRPEETT 487
Cdd:PRK10762 473 ISGEFTREQAT 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-479 |
2.71e-86 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 275.01 E-value: 2.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPdvgmllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLP------KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITALMVGHQV 239
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDIIQAITPAAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 240 TKRVSD------------RSVAPGREVLVVDHAVAigewgeEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTL 307
Cdd:PRK15439 242 EKSLSAsqklwlelpgnrRQQAAGAPVLTVEDLTG------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 308 SSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAEN---LVLGwqrkpeyRRGPFLDRGKINDLAQRKLE 384
Cdd:PRK15439 316 RGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNvcaLTHN-------RRGFWIKPARENAVLERYRR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 385 EFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLR 464
Cdd:PRK15439 389 ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
490
....*....|....*
gi 1550121285 465 LCDRIAVIFKGKIVG 479
Cdd:PRK15439 469 MADRVLVMHQGEISG 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-479 |
2.24e-84 |
|
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: 269.77 E-value: 2.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS--GVIRFKGQVAELNSPADALRLGI 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENIIVGSPdvgmlLSKSTARQKVEDLCLRCG-----IELDLD---REIWQLSVGEQQWVEILKA 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNE-----ITLPGGRMAYNAMYLRAKnllreLQLDADnvtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 154 LYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITA 232
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDDIIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 233 LMVGHQVTKRVSDRSVAPGREVLVVDHAVAIGEWGEEV--LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS-S 309
Cdd:TIGR02633 236 MMVGREITSLYPHEPHEIGDVILEARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 310 GRFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGLISEFGTAENLVLGWQRKpeyrrgpFLDRGKINDLAQ-----RKLE 384
Cdd:TIGR02633 316 GNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKS-------FCFKMRIDAAAElqiigSAIQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 385 EFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLR 464
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG 468
|
490
....*....|....*
gi 1550121285 465 LCDRIAVIFKGKIVG 479
Cdd:TIGR02633 469 LSDRVLVIGEGKLKG 483
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-215 |
9.24e-75 |
|
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: 233.09 E-value: 9.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGIGMV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQhfvlvenftvleniivgspdvgmllskstarqkvedlclrcgieldldreiwqLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03216 81 YQ-----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGR 159
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
251-477 |
8.70e-67 |
|
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: 213.45 E-value: 8.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 251 GREVLVVDHAvaigeWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDR 330
Cdd:cd03215 1 GEPVLEVRGL-----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 331 GVGLVPDDRFREGLISEFGTAENLVLGWQrkpeyrrgpfldrgkindlaqrkleefrivaastdlpverLSGGNAQRVIL 410
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 411 AREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-485 |
5.85e-55 |
|
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: 192.43 E-value: 5.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF--GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRAD---SGVIRFKGQVAeLNSPAD 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRLGIGMVHQHFVLVENFTVLENIIVGSPDVGmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALY 155
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 156 FGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESITAL 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 234 MVGHQVTKRVSDRSVAPGRE-VLVVDHAV---AIGEWGE-EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS 308
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEpLLEVRNLSkryPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 309 SGRFHLNGEAIVAPTSREMLD--RGVGLVPDD-------RFR------EGLIsefgtaenlVLGWQRKPEYRRgpfldrg 373
Cdd:COG1123 319 SGSILFDGKDLTKLSRRSLRElrRRVQMVFQDpysslnpRMTvgdiiaEPLR---------LHGLLSRAERRE------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 374 KINDLaqrkLEEFRIVAASTDLPVERLSGGNAQRVILAREF-LNAKcLLLANQPTRGLDVAasefVYEKILE-----KRA 447
Cdd:COG1123 383 RVAEL----LERVGLPPDLADRYPHELSGGQRQRVAIARALaLEPK-LLILDEPTSALDVS----VQAQILNllrdlQRE 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 1550121285 448 EGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG1123 454 LGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
1.00e-52 |
|
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: 178.40 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADALRLGIGM 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdITGL-PPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVG--------SPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALY 155
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 156 FGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGR 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-211 |
1.41e-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: 168.29 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADALRL 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdITGL-PPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMVHQHFVLVENFTVLENIIVG-------SPDVGMLLSKST------ARQKVEDLCLRCGIELDLDREIWQLSVGEQQ 146
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAaharlgrGLLAALLRLPRArreereARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 147 WVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRR-QGLSIILISHKLREVMQ-SDRVTIL 211
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGlADRIVVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-215 |
2.53e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAElnSPADALRLgIGM 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVAR--DPAEVRRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVgspdVGML--LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELL 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRF----FARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 162 ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-215 |
7.58e-41 |
|
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: 144.85 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGMV 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIivgspdvgmllskstarqkvedlclrcgieldldreiwQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03230 79 PEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGR 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-215 |
7.50e-39 |
|
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: 140.73 E-value: 7.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnspaDALRLGIGM 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdVTGV----PPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIivGSPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:cd03259 77 VFQDYALFPHLTVAENI--AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALAlADRIAVMNEGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-215 |
3.26e-38 |
|
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: 139.99 E-value: 3.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPadALRLGIGM 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGL--FDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILHKGK 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-215 |
2.92e-37 |
|
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: 136.44 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaLRLGIGM 83
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQH----FVlveNFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:cd03225 80 VFQNpddqFF---GPTVEEEVAFGLENLG--LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
3.33e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.71 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPA- 74
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdISSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRLG-IGMVHQHFVLVENFTVLENIIVGspdvgMLL---SKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEI 150
Cdd:COG1136 81 ARLRRRhIGFVFQFFNLLPELTALENVALP-----LLLagvSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 151 LKALYFGAELLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-215 |
1.51e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 133.19 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADAlRL 79
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIA-RM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMVHQHFVLVENFTVLENIIVGSP---DVGML--LSKSTARQKVEDLCL--------RCGIELDLDREIWQLSVGEQQ 146
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHqqlKTGLFsgLLKTPAFRRAESEALdraatwleRVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 147 WVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-215 |
6.85e-35 |
|
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: 130.30 E-value: 6.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGA----VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADAL-- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQHFVLVENFTVLENIIvgspdVGMLLS---KSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKAL 154
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVE-----LPLLLAgvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 155 YFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-215 |
9.47e-35 |
|
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: 129.57 E-value: 9.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPA-DALRLGIGM 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPDV-GMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVkGM--SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 163 LDEPTAVLTPQQSDQlfvILDGMR---RQGLSIILISHKL---REVmqSDRVTILRKGK 215
Cdd:cd03262 159 FDEPTSALDPELVGE---VLDVMKdlaEEGMTMVVVTHEMgfaREV--ADRVIFMDDGR 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-215 |
1.98e-34 |
|
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: 129.09 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADALRLGIGM 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGL-PPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGspdvGMLLSKSTARQKVEDLclrcgieLDL--------DREIWQLSVGEQQWVEILKALY 155
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG----AYARRRAKRKARLERV-------YELfprlkerrKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 156 FGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGR 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
4.05e-34 |
|
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: 128.60 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLgIGM 83
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQH----FVlveNFTVLENIIVGsPdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:COG1122 80 VFQNpddqLF---APTVEEDVAFG-P-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGR 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-215 |
2.42e-33 |
|
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: 125.86 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqvaelNSPADALRLGIGMV 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGL--KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-215 |
3.64e-32 |
|
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: 122.61 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFG--AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIG 82
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENIIVgspdVGML--LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF----YARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVILDGMRRqGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAeALCDRIAIMSDGK 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-215 |
1.97e-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: 120.40 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLgIGMV 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSpdVGMLLSKStarqKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLA--RLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGK 203
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
2.08e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.44 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAeLNSPADAlRlG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEK-R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGspdvgmL----LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFG------LrmrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 157 GAELLILDEPT----AVLTPQQSDQLFVILdgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG3842 153 EPRVLLLDEPLsaldAKLREEMREELRRLQ---RELGITFIYVTHDQEEALAlADRIAVMNDGR 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-215 |
2.85e-31 |
|
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: 120.76 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD--AL 77
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQHFVLVENFTVLENI-----IVGSPdvgmllsKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILK 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENValpleIAGVP-------KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 153 ALYFGAELLILDEPTAVLTPQQSDQ-LFVILDGMRRQGLSIILISHKLrEVMQS--DRVTILRKGK 215
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSiLALLRDINRELGLTIVLITHEM-EVVKRicDRVAVMEKGE 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-215 |
1.36e-30 |
|
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: 118.93 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADALRLG 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEdITGL-PPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDVGmllSKSTARQKVEDLclrcgieLDL--------DREIWQLSVGEQQWVEILK 152
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR---DRAEVRADLERV-------YELfprlkerrRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 153 ALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEiADRAYVLERGR 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-214 |
1.42e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPADALRLG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENF--TVLEniIVGS---PDVGMLLSKSTA-RQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKAL 154
Cdd:COG1121 77 IGYVPQRAEVDWDFpiTVRD--VVLMgryGRRGLFRRPSRAdREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 155 YFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRG 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
1.97e-30 |
|
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: 118.99 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADALRLgIG 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdLASL-SRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENIIVG-SPDVGMLLSKSTA-RQKVEDLCLRCGIElDL-DREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGrYPHLGLFGRPSAEdREAVEEALERTGLE-HLaDRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARyADRLVLLKDGR 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-168 |
2.01e-30 |
|
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: 115.82 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvAELNSPADALRLGIGMVHQHFVLVENFTVLENI 100
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ-DLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 101 IVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIW----QLSVGEQQWVEILKALYFGAELLILDEPTA 168
Cdd:pfam00005 81 RLGLLLKG--LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-208 |
2.40e-30 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 117.33 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNS--PADALRLGIGM 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQeTPPLNSkkASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSpdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGL--KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRV 208
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-214 |
4.12e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 116.86 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPADALRLGIGMVH 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 86 QHFVLVENF--TVLEniIVGS---PDVGMLLSKSTA-RQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:cd03235 75 QRRSIDRDFpiSVRD--VVLMglyGHKGLFRRLSKAdKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQS-DRVTILRKG 214
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-215 |
5.11e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.18 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPAD--AL 77
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdLTAL-SERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQHFVLVENFTVLENI-----IVGspdvgmlLSKSTARQKVEDLclrcgieLDL----DREiW----QLSVGE 144
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpleIAG-------VPKAEIRKRVAEL-------LELvglsDKA-DaypsQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 145 QQWVEILKALYFGAELLILDEPTAVLTPQQSDQ-LFVILDGMRRQGLSIILISHKLrEVMQS--DRVTILRKGK 215
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSiLDLLKDINRELGLTIVLITHEM-DVVRRicDRVAVLENGR 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
7.04e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.50 E-value: 7.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPADA 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK------PVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 LRLGIGMVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGV--PKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQL-FVILDGMRRQGLSIILISHKLRE-VMQSDRVTILRKG 214
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLqDELLRLWQETGKTVLFVTHDVDEaVFLADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
1.53e-29 |
|
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: 114.21 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLGIGM 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGspdvgmllskstarqkvedlclrcgieldldreiwqLSVGEQQWVEILKALYFGAELLIL 163
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-485 |
3.44e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 120.68 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGY--YRADSGVI--------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 62 -------RFKGQVAELNSPADALRLGIG-----MVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGI 129
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVLEALEEIGY--EGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 130 ELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHkLREVMQ--SD 206
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSH-WPEVIEdlSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 207 RVTILRKGKVVATVETATTtaesITALMVGHQVTKRvsDRSVAPGREVL----VVDHAVAIGEWGEEVLCDINFTIAENE 282
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV----VAVFMEGVSEVEK--ECEVEVGEPIIkvrnVSKRYISVDRGVVKAVDNVSLEVKEGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 283 ILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLN-GEAIVAPTSREMLDRG-----VGLVpddrFRE-GLISEFGTAENLV 355
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRGrakryIGIL----HQEyDLYPHRTVLDNLT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 356 --LGWQRKPEYRRgpfldRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVA 433
Cdd:TIGR03269 388 eaIGLELPDELAR-----MKAVITLKMVGFDEEKAEEILDKYPDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 434 ASEFVYEKILEKRAEGFAVFL-ASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIiVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
5.80e-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: 114.32 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPA---DALRLG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE--DLTDSKkdiNKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGsPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLA-PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 161 LILDEPTAVLTPQqsdqlFV--ILDGMR---RQGLSIILISHKL---REVmqSDRVTILRKGK 215
Cdd:COG1126 158 MLFDEPTSALDPE-----LVgeVLDVMRdlaKEGMTMVVVTHEMgfaREV--ADRVVFMDGGR 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-215 |
6.08e-29 |
|
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: 114.14 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRL 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 G--IGMVHQHFVLVEN--FTVLENIIVGSPDVGMlLSKSTARQKVEDLCLrCGIELD---LDREIWQLSVGEQQWVEILK 152
Cdd:cd03257 81 RkeIQMVFQDPMSSLNprMTIGEQIAEPLRIHGK-LSKKEARKEAVLLLL-VGVGLPeevLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 153 ALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
2.50e-28 |
|
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: 112.66 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGA-VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD--ALRLGI 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENIIvgspdVGMLLSKSTARQ-----KVED--LCLRCGIELDLDREIWQ----LSVGEQQWVEI 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVL-----SGRLGRRSTWRSlfglfPKEEkqRALAALERVGLLDKAYQradqLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 151 LKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMdLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-215 |
3.28e-28 |
|
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: 112.33 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAeLNSPADalRLGIGMV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKL--PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTmSDRIAVMNKGK 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-215 |
4.02e-28 |
|
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: 113.12 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 12 KRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADAL----RLGIGMVHQ 86
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdIAAMS--RKELrelrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGV--PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 167 TAVLTP----QQSDQLFVILDGMRRqglSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03294 188 FSALDPlirrEMQDELLRLQAELQK---TIVFITHDLDEALRlGDRIAIMKDGR 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-211 |
5.29e-28 |
|
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: 111.41 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPADALRLG 80
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE------PVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGV--PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 161 LILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLRE-VMQSDRVTIL 211
Cdd:cd03293 153 LLLDEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEaVFLADRVVVL 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-215 |
5.32e-28 |
|
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: 111.82 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD--ALRLGIG 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENiivgspdVGMLL------SKSTARQKVEdLCL-RCGIELDLDREIWQLSVGEQQWVEILKALY 155
Cdd:cd03261 81 MLFQSGALFDSLTVFEN-------VAFPLrehtrlSEEEIREIVL-EKLeAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 156 FGAELLILDEPTAVLTPQQS---DQLfvILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASgviDDL--IRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGK 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.72e-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: 108.67 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRfGAVtanDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGI 81
Cdd:cd03215 2 EPVLEVRGLSVK-GAV---RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMV---HQHFVLVENFTVLENIIVGSpdvgmllskstarqkvedlclrcgieldldreiwQLSVGEQQWVEILKALYFGA 158
Cdd:cd03215 78 AYVpedRKREGLVLDLSVAENIALSS----------------------------------LLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 159 ELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGR 181
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-215 |
2.51e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 107.33 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAdALRLGIGMVH 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 86 qhfvlvenftvleniivgspdvgmllskstarqkvedlclrcgieldldreiwQLSVGEQQWVEILKALYFGAELLILDE 165
Cdd:cd00267 80 -----------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 166 PTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-215 |
5.29e-27 |
|
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: 108.61 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGA----VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqVAELNSPADALRl 79
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMVHQHFVLVENFTVLENIIVGSPDVGMLLSKSTARqkVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTAR--LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGR 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
6.32e-27 |
|
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: 108.91 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPA-DALR 78
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKElYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQHFVLVENFTVLENIivgspdvgML-------LSKSTARQKVEdLCL-RCGIELDLDREIWQLSVGEQQWVEI 150
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENV--------AFplrehtdLSEAEIRELVL-EKLeLVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 151 LKALYFGAELLILDEPTAVLTPQQS---DQLfvILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSaviDEL--IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGK 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-208 |
6.65e-27 |
|
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: 108.29 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF-----GAVT--ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELN-- 71
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 72 --SPADALRL---GIGMVHQHFVLVENFTVLEniIVGSPDVGMLLSKSTARQKVEDLCLRcgieLDLDREIWQL-----S 141
Cdd:COG4778 81 qaSPREILALrrrTIGYVSQFLRVIPRVSALD--VVAEPLLERGVDREEARARARELLAR----LNLPERLWDLppatfS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 142 VGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKlREVMQ--SDRV 208
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD-EEVREavADRV 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-215 |
7.00e-27 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 108.10 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 9 NLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAEL-NSPADALRLGIGMVH 85
Cdd:TIGR02673 6 NVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdVNRLrGRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 86 QHFVLVENFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDE 165
Cdd:TIGR02673 86 QDFRLLPDRTVYENVALPLEVRG--KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 166 PTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRvAHRVIILDDGR 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-215 |
4.08e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPA---DALRLGIGMV 84
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL--KVNDPKvdeRLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDV-GMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGPLRVrGA--SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKL---REVmqSDRVTILRKGK 215
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIgfaEKV--ASRLIFIDKGR 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-215 |
5.99e-26 |
|
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: 106.27 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAelnSPADALRLGIGMVHQ 86
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVG--SPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03296 82 HYALFRHMTVFDNVAFGlrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMR-RQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEvADRVVVMNKGR 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-215 |
6.26e-26 |
|
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: 104.05 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLGIgmV 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdLASLSPKELARKIAY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQhfvlvenftVLEniivgspdvgmllskstarqkvedlclRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03214 79 PQ---------ALE---------------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDGR 175
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
7.06e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.50 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNsPADALRLGigmv 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE--PLD-PEDRRRIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 hqhfVLVE------NFTVLENIIvgspDVGML--LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:COG4152 75 ----YLPEerglypKMKVGEQLV----YLARLkgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGR 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-215 |
7.72e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.13 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNS---PadALRLGIG 82
Cdd:COG2884 5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdLSRLKRreiP--YLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENI-----IVGspdvgmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:COG2884 83 VVFQDFRLLPDRTVYENValplrVTG-------KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD-RVTILRKGK 215
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGR 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-215 |
1.04e-25 |
|
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: 105.11 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTAnDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAdalRLGIGMV 84
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDVgmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKR--KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAwALADKVAIMLNGK 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-215 |
2.56e-25 |
|
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: 103.60 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGMVHQ 86
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH--DVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYG--VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGR 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-215 |
3.45e-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: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADalRlGIGM 83
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdVTDL-PPKD--R-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIivGSPdvgmL----LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:COG3839 80 VFQSYALYPHMTVYENI--AFP----LklrkVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTlADRIAVMNDGR 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
8.27e-25 |
|
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: 101.79 E-value: 8.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGM 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE--PIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVgspdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQGLSIILISH 197
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-215 |
1.26e-24 |
|
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: 101.56 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAlrlGIGMV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKV--PKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQ 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-215 |
1.76e-24 |
|
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: 99.76 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSpaDALRLGIGMVHQHFVLVeNFTVLEN 99
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdLRDLDL--ESLRKNIAYVPQDPFLF-SGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 100 IivgspdvgmllskstarqkvedlclrcgieldldreiwqLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF 179
Cdd:cd03228 96 I---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 1550121285 180 VILDGMrRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03228 137 EALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
269-485 |
5.15e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.52 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVApTSREMLDRgVGLVPDDRfreGLISEF 348
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRR-IGYVPQEP---ALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLgwqrkpeYRRGPFLDRGKINDLAQRKLEEFRIVAASTDlPVERLSGGNAQRVILAREFLNAKCLLLANQPTR 428
Cdd:COG1131 89 TVRENLRF-------FARLYGLPRKEARERIDELLELFGLTDAADR-KVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 429 GLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-208 |
7.04e-24 |
|
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: 102.05 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRA---DSGVIRFKGQ-VAELnSPAD 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdLLKL-SEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRL---GIGMVHQhfvlvENFTVL------ENIIVGSPDVGMLLSKSTARQKVEDLCLRCGI---ELDLDREIWQLSVG 143
Cdd:COG0444 80 LRKIrgrEIQMIFQ-----DPMTSLnpvmtvGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 144 EQQWVEILKALYFGAELLILDEPTAVL--TPQQSdqlfvILDGM----RRQGLSIILISHKL---REVmqSDRV 208
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALdvTIQAQ-----ILNLLkdlqRELGLAILFITHDLgvvAEI--ADRV 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-215 |
7.90e-24 |
|
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: 99.40 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRFGA-VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADA-LRLGIGMV 84
Cdd:cd03292 4 INVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdVSDLRGRAIPyLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENI-----IVGSPdvgmllsKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:cd03292 84 FQDFRLLPDRNVYENVafaleVTGVP-------PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISH--KLREVMQSdRVTILRKGK 215
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHakELVDTTRH-RVIALERGK 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-215 |
1.05e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADA-----LRL 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkaireLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMVHQHFVLVENFTVLENIIVGSPDVgMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRV-LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLrEVMQ--SDRVTILRKGK 215
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEV-EVARktASRVVYMENGH 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
1.80e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.09 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF--GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaLR 78
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQH----FVlveNFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKAL 154
Cdd:PRK13635 81 RQVGMVFQNpdnqFV---GATVQDDVAFGLENIGV--PREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 155 YFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQADRVIVMNKGE 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-215 |
3.76e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.50 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADA----- 76
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 -------LRLGIGMVHQHFVLVENFTVLENIIVGSPDVgMLLSKSTARQKVEDLCLRCGI-ELDLDREIWQLSVGEQQWV 148
Cdd:PRK10619 83 dknqlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 149 EILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKL---REVmqSDRVTILRKGK 215
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMgfaRHV--SSHVIFLHQGK 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
267-478 |
4.04e-23 |
|
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: 98.01 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPDDRFreglIS 346
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KEPREARRQIGVLPDERG----LY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTA-ENL-VLGWQRKPEYRRgpflDRGKINDLAQR-KLEEFRivaastDLPVERLSGGNAQRVILAREFL-NAKCLLL 422
Cdd:COG4555 87 DRLTVrENIrYFAELYGLFDEE----LKKRIEELIELlGLEEFL------DRRVGELSTGMKKKVALARALVhDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 423 aNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG4555 157 -DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-215 |
7.19e-23 |
|
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: 102.14 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNS-PADALRLGIG 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV--DLSDlDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENfTVLENIIVGSPDVGmllskstaRQKVEDLCLRCGI-------ELDLDREI----WQLSVGEQQWVEIL 151
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGRPDAS--------DEELEAALEAAGLdefvaalPDGLDTPLgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 152 KALYFGAELLILDEPTAVLTPqQSDQLfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDA-ETEAE--ILQALRRlaKGRTVILITHRLALLAQADRILVLDDGR 548
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
2.31e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 96.34 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLGIg 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRpLAAWSPWELARRRAV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 mVHQHFVLVENFTVLEniiVgspdVGM-LLSKSTARQKVEDLCLRCGIELDL----DREIWQLSVGEQQWVEILKAL--- 154
Cdd:COG4559 80 -LPQHSSLAFPFTVEE---V----VALgRAPHGSSAAQDRQIVREALALVGLahlaGRSYQTLSGGEQQRVQLARVLaql 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 155 ----YFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG4559 152 wepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGR 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-215 |
2.38e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLgiG 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpLADWSPAELARRR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLEniiVgspdVGM-LLSKSTARQKVEDLCLRCGIELDL----DREIWQLSVGEQQWVEILKALyfg 157
Cdd:PRK13548 80 VLPQHSSLSFPFTVEE---V----VAMgRAPHGLSRAEDDALVAAALAQVDLahlaGRDYPQLSGGEQQRVQLARVL--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 158 AEL---------LILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLR-EVMQSDRVTILRKGK 215
Cdd:PRK13548 150 AQLwepdgpprwLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNlAARYADRIVLLHQGR 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-215 |
2.90e-22 |
|
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: 95.58 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADA 76
Cdd:COG4181 6 APIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 LRLG--IGMVHQHFVLVENFTVLENI-----IVGSPDvgmllskstARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVE 149
Cdd:COG4181 86 RLRArhVGFVFQSFQLLPTLTALENVmlpleLAGRRD---------ARARARALLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 150 ILKALYFGAELLILDEPTAVL---TPQQ-SDQLFvilDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLdaaTGEQiIDLLF---ELNRERGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-215 |
3.05e-22 |
|
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: 95.30 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADAlRLGIGM 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQdITKLPMHKRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPdvGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLE--IRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 164 DEPTAVLTP---QQSDQLFVILdgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03218 158 DEPFAGVDPiavQDIQKIIKIL---KDRGIGVLITDHNVRETLSiTDRAYIIYEGK 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-215 |
3.30e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 100.29 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGI 81
Cdd:COG2274 474 IELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdLRQID--PASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLvenF--TVLENIIVGSPDVGMllskstarQKVEDLCLRCGIE-------LDLDREIW----QLSVGEQQWV 148
Cdd:COG2274 552 GVVLQDVFL---FsgTIRENITLGDPDATD--------EEIIEAARLAGLHdfiealpMGYDTVVGeggsNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 149 EILKALYFGAELLILDEPTAVLtPQQSDQlfVILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG2274 621 AIARALLRNPRILILDEATSAL-DAETEA--IILENLRRllKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-215 |
4.49e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.83 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNspADALRLGIG 82
Cdd:PRK13632 9 KVENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGiTISKEN--LKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQH----FV--LVEN---FTvLENIivgspdvgmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKA 153
Cdd:PRK13632 87 IIFQNpdnqFIgaTVEDdiaFG-LENK---------KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 154 LYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGL-SIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGK 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-215 |
5.72e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.60 E-value: 5.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPadaLRLGIGM 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVG-SPDvgmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGlKQD---KLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 163 LDEPTAVLTPQQSDQL-FVILDGMRRQGLSIILISHKLREVM-QSDRVTILRKGK 215
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMtMAGRIAIMNRGK 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
270-497 |
6.48e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRfreGLISEFG 349
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQEL---NLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWqrkpEYRRGPFLDRGKINDLAQRKLEEFRiVAASTDLPVERLSGGNAQRVILAREF-LNAKCLLLaNQPTR 428
Cdd:COG1129 96 VAENIFLGR----EPRRGGLIDWRAMRRRARELLARLG-LDIDPDTPVGDLSVAQQQLVEIARALsRDARVLIL-DEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 429 GLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELGMMMAG 497
Cdd:COG1129 170 SLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-215 |
8.04e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 96.41 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPA-DALRLGI 81
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdLTALSEKElRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENI-----IVGspdvgmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNValpleLAG-------TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQlfvILDGM----RRQGLSIILISHKLrEVMQS--DRVTILRKGK 215
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRS---ILELLkdinRELGLTIVLITHEM-DVVKRicDRVAVIDAGR 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-211 |
1.77e-21 |
|
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: 97.74 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGIG 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpLADAD--ADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENfTVLENIIVGSPDVGMLLSKSTARQKVEDLC---LRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFvaaLPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 160 LLILDEPTAVLTPqQSDQLfvILDGMRR--QGLSIILISHKLREVMQSDRVTIL 211
Cdd:TIGR02857 479 LLLLDEPTAHLDA-ETEAE--VLEALRAlaQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-215 |
1.81e-21 |
|
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: 93.01 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYG-----YYRADSGVIRFKGQ-VAELNSPADALR 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQHFVLVeNFTVLENIIVGSPDVGMlLSKSTARQKVEDLCLRCGI--ELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQLFVILDGMRRQgLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGR 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-215 |
3.26e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 92.75 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVT-ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGIG 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdIREQD--PVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENIIVgspdVGMLL--SKSTARQKVEDLCLRCGIELD--LDREIWQLSVGEQQWVEILKALYFGA 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIAL----VPKLLkwPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 159 ELLILDEPTAVLTPQQSDQL---FVILDgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLqeeFKRLQ--QELGKTIVFVTHDIDEAFRlADRIAIMKNGE 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
3.30e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.10 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSpaD 75
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdVATLDA--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 AL----RLGIGMVHQHFVLVENFTVLENIIVgsPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEIL 151
Cdd:PRK10535 79 ALaqlrREHFGFIFQRYHLLSHLTAAQNVEV--PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 152 KALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
269-477 |
4.21e-21 |
|
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: 90.53 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPDDRfreGLISEF 348
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYLPEEP---SLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLvlgwqrkpeyrrgpfldrgkindlaqrkleefrivaastdlpveRLSGGNAQRVILAREFL-NAKCLLLaNQPT 427
Cdd:cd03230 89 TVRENL--------------------------------------------KLSGGMKQRLALAQALLhDPELLIL-DEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1550121285 428 RGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
5.13e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.86 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGspdvGMLLSKSTARQKVE---DLCLRCgieldLDREIWQ---LSVGEQQWVEILKAL 154
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG----GFFAERDQFQERIKwvyELFPRL-----HERRIQRagtMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 155 YFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGH 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-215 |
1.15e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 90.43 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 12 KRFGAVTANdsVDLDVrKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQV-----AELNSPADalRLGIGMVHQ 86
Cdd:cd03297 8 KRLPDFTLK--IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrKKINLPPQ--QRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVGSPdvgmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03297 83 QYALFPHLNVRENLAFGLK----RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAeYLADRIVVMEDGR 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-215 |
2.44e-20 |
|
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: 89.24 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelNSPADALRLGIGMVHQH--FVLVENfTVLE 98
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK----PIKAKERRKSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 99 NIIVGSPDVGmlLSKSTARQKVEDLCLrcgieLDL-DREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQ 177
Cdd:cd03226 92 ELLLGLKELD--AGNEQAETVLKDLDL-----YALkERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1550121285 178 LFVILDGMRRQGLSIILISHKLrEVMQ--SDRVTILRKGK 215
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDY-EFLAkvCDRVLLLANGA 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-215 |
2.55e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD------- 75
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRLGIGMVHQHFVLVENFTVLENIIVGsPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALY 155
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEG-PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 156 FGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKL---REVmqSDRVTILRKGK 215
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfaRDV--ADRAIFMDQGR 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
2.74e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTAN-----DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFK--------GQVAEL 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENelvalNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 71 NSP-------ADALRLGIGMVHQhFVLVENF--TVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELD-LDREIWQL 140
Cdd:PRK13631 101 TNPyskkiknFKELRRRVSMVFQ-FPEYQLFkdTIEKDIMFGPVALGV--KKSEAKKLAKFYLNKMGLDDSyLERSPFGL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 141 SVGEQQWVEILKALYFGAELLILDEPTAVLTPQ-QSDQLFVILDGmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDA-KANNKTVFVITHTMEHVLEvADEVIVMDKGK 253
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
268-476 |
3.46e-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: 88.68 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 268 EEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLdRGVGLV---PDDRFregl 344
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR-RKVGLVfqnPDDQF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 iseFGT--AENLVLGwqrkPEYRRgpfLDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRV----ILArefLNAK 418
Cdd:cd03225 89 ---FGPtvEEEVAFG----LENLG---LPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVaiagVLA---MDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 419 CLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:cd03225 155 ILLL-DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-215 |
5.42e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.68 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADA 76
Cdd:PRK10584 4 ENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQpLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 -LRL-GIGMVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKAL 154
Cdd:PRK10584 84 kLRAkHVGFVFQSFMLIPTLNALENVELPALLRGE--SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 155 YFGAELLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-215 |
7.93e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLG 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE--PVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGL--SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGR 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-215 |
8.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTAN---DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaL 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKytlNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQH----FVlveNFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKA 153
Cdd:PRK13650 80 RHKIGMVFQNpdnqFV---GATVEDDVAFGLENKGI--PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 154 LYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQ 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-215 |
8.78e-20 |
|
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: 87.58 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYG--YYRADSGVIRFKGQ-VAELnSPADALRLGI 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEdITDL-PPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLEniIVGSPDVGmllskstarqkvedlclrcgieldldreiwqLSVGEQQWVEILKALYFGAELL 161
Cdd:cd03217 80 FLAFQYPPEIPGVKNAD--FLRYVNEG-------------------------------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 162 ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISH--KLREVMQSDRVTILRKGK 215
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGR 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-478 |
9.85e-20 |
|
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: 92.05 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGA----VTANDSVDLDVRKGEIHCLFGENGAGKS--TLSAC-LYGYYRA-DSGVIRFKGQvaELNS 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrLLPDPAAhPSGSILFDGQ--DLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 73 -PADALR----LGIGMVHQhfvlvE-----N--FTVLENIIvgspDVGML---LSKSTARQKVEDLCLRCGI---ELDLD 134
Cdd:COG4172 81 lSERELRrirgNRIAMIFQ-----EpmtslNplHTIGKQIA----EVLRLhrgLSGAAARARALELLERVGIpdpERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 135 REIWQLSVGEQQWVEILKALYFGAELLILDEPTAVL--TPQQsdQlfvILDGM----RRQGLSIILISHKLREVMQ-SDR 207
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALdvTVQA--Q---ILDLLkdlqRELGMALLLITHDLGVVRRfADR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 208 VTILRKGKvvatvetatttaesitalMV------------GHQVTKR-------VSDRSVAPGREVLV------VDHAVA 262
Cdd:COG4172 227 VAVMRQGE------------------IVeqgptaelfaapQHPYTRKllaaeprGDPRPVPPDAPPLLeardlkVWFPIK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 263 IGEWGEEV-----LCDINFTIAENEILGLAGVAGNGQKELFEVLMGvrtL--SSGRFHLNGEAIVAPTSREM--LDRGVG 333
Cdd:COG4172 289 RGLFRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LipSEGEIRFDGQDLDGLSRRALrpLRRRMQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 334 LVPDD-------RFREGLIsefgTAENLVLgwqrkpeyrRGPFLDRGKINDLAQRKLEEFRIVAASTD-LPVErLSGGNA 405
Cdd:COG4172 366 VVFQDpfgslspRMTVGQI----IAEGLRV---------HGPGLSAAERRARVAEALEEVGLDPAARHrYPHE-FSGGQR 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 406 QRVILAREF-LNAKcLLLANQPTRGLDVAasefVYEKILE-----KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG4172 432 QRIAIARALiLEPK-LLVLDEPTSALDVS----VQAQILDllrdlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
1.27e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGV---IRFKGQVAE----LNSP 73
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQregrLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 74 ADALRLGIGMVHQHFVLVENFTVLENIIVG----SPDVGMLLSKSTARQKVEDL--CLRCGIELDLDREIWQLSVGEQQW 147
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGalgsTPFWRTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 148 VEILKALYFGAELLILDEPTAVLTPQQSDqlfVILDGMR----RQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESAR---IVMDTLRdinqNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
270-478 |
1.30e-19 |
|
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: 87.34 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMldrgvGLVPDDRfreGLISEFG 349
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI-----GYLPEER---GLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLV----LGWQRKPEYRRG--PFLDRGKINDLAQRKLEEfrivaastdlpverLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:cd03269 87 VIDQLVylaqLKGLKKEEARRRidEWLERLELSEYANKRVEE--------------LSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 424 NQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
269-485 |
1.47e-19 |
|
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: 87.49 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRfreGLISEF 348
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRKPEYRRGPFLDRgkINDLAQRkLEEFRIVAASTdlpverLSGGNAQRVILAREFL-NAKCLLLaNQPT 427
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARLER--VYELFPR-LKERRKQLAGT------LSGGEQQMLAIARALMsRPKLLLL-DEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 428 RGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-197 |
2.02e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.94 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 15 GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPADALRLGIGMVHQHFVLV--- 91
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGE------PLDYSRKGLLERRQRVGLVfqd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 92 ---ENF--TVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:TIGR01166 77 pddQLFaaDVDQDVAFGPLNLG--LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPQQSDQLFVILDGMRRQGLSIILISH 197
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.11e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVT-ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADA-LR 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR--EVNAENEKwVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQH-FVLVENFTVLENIIVGSpdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGP--VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGR 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
256-485 |
2.15e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 256 VVDHAVAIGEwgEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLV 335
Cdd:PRK09536 6 VSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-ASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 336 PDDrfrEGLISEFGTAENLVLGwqRKPEyrRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVERLSGGNAQRVILAREFL 415
Cdd:PRK09536 83 PQD---TSLSFEFDVRQVVEMG--RTPH--RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 416 NAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-477 |
5.98e-19 |
|
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: 85.28 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaptsrEMLDRGVGLVPDdrfREGLIS 346
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVPQ---RRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EF-GTAENLVL----------GWQRKPEYRRG-PFLDRGKINDLAQRKLEEfrivaastdlpverLSGGNAQRVILAREF 414
Cdd:cd03235 82 DFpISVRDVVLmglyghkglfRRLSKADKAKVdEALERVGLSELADRQIGE--------------LSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 415 L-NAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:cd03235 148 VqDPDLLLL-DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
267-485 |
1.06e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaPTSREMLDRGVGLVPddRFrEGLIS 346
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLARARIGVVP--QF-DNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLgwqrkpeyrrgpfldRGKINDLAQRKLE-------EFRIVAASTDLPVERLSGGNAQRVILAREFLNAKC 419
Cdd:PRK13536 128 EFTVRENLLV---------------FGRYFGMSTREIEavipsllEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 420 LLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
273-478 |
1.30e-18 |
|
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: 84.73 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPDDRfreGLISEFGTAE 352
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEARRRLGFVSDST---GLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVLgWQRKPEYRRGPFLDRgkINDLAQR-KLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLD 431
Cdd:cd03266 98 NLEY-FAGLYGLKGDELTAR--LEELADRlGMEELL------DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1550121285 432 VAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-215 |
1.42e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTkrfgaVTAND-----SVDLDVRKGEIHCLFGENGAGKSTLSACLYGY--YRADSGVIRFKGQ-VAELnSPADA 76
Cdd:COG0396 1 LEIKNLH-----VSVEGkeilkGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdILEL-SPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 LRLGIGMVHQHFVLVENFTVLE--NIIVGS---PDVGMLLSKSTARQKVEDLclrcGIELD-LDREIWQ-LSVGEQQWVE 149
Cdd:COG0396 75 ARAGIFLAFQYPVEIPGVSVSNflRTALNArrgEELSAREFLKLLKEKMKEL----GLDEDfLDRYVNEgFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 150 ILKALYFGAELLILDEPTAVLtpqQSDQLFVILDG---MRRQGLSIILISHKLR--EVMQSDRVTILRKGK 215
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGL---DIDALRIVAEGvnkLRSPDRGILIITHYQRilDYIKPDFVHVLVDGR 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-215 |
1.52e-18 |
|
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: 84.97 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGIGMVHQHFVLVeNFTVLENII 101
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdIREVT--LDSLRRAIGVVPQDTVLF-NDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGSPDVGmllskstaRQKVEDLCLRCGIeldlDREIWQ---------------LSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03253 97 YGRPDAT--------DEEVIEAAKAAQI----HDKIMRfpdgydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 167 TAVL---TPQQsdqlfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03253 165 TSALdthTERE------IQAALRDvsKGRTTIVIAHRLSTIVNADKIIVLKDGR 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
267-485 |
1.62e-18 |
|
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: 84.69 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRgVGLV---PDDRFreg 343
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVfqnPDDQL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 liseFGT--AENLVLGwqrkPEYRRgpfLDRGKIND-----LAQRKLEEFRivaastDLPVERLSGGNAQRV----ILAr 412
Cdd:COG1122 89 ----FAPtvEEDVAFG----PENLG---LPREEIRErveeaLELVGLEHLA------DRPPHELSGGQKQRVaiagVLA- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 413 efLNAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG1122 151 --MEPEVLVL-DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-215 |
2.18e-18 |
|
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: 84.75 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLDVRKGEiHC-LFGENGAGKSTLSACLYGYYRADSG-VIRFKGQVAELNSPADaLRL 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HWaILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE-LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMV----HQHFVlvENFTVLENIIVGSPDVGMLLSKSTA--RQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKA 153
Cdd:COG1119 79 RIGLVspalQLRFP--RDETVLDVVLSGFFDSIGLYREPTDeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 154 LYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQG-LSIILISHKLREVMQS-DRVTILRKGK 215
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-215 |
2.40e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.91 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnsPADALRLGIGMVHQHFVLVeNFTVLENII 101
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdIRDL--TLESLRRQIGVVPQDTFLF-SGTIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGSPDVgmllskstARQKVEDLCLRCGI-----ELD--LDREIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVL 170
Cdd:COG1132 436 YGRPDA--------TDEEVEEAAKAAQAhefieALPdgYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1550121285 171 TPqQSDQLfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG1132 508 DT-ETEAL--IQEALERlmKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-215 |
2.59e-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: 87.94 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRF-----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSG--VIRFKGQVAELNSPA 74
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRlG-----IGMVHQHFVLVENFTVLENIivgSPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIW-----QLSVGE 144
Cdd:TIGR03269 357 PDGR-GrakryIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMKAVITLKMVGFDEEKAEEILdkypdELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 145 QQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGK 505
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
2.91e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVT-ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnsPAD----- 75
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDysrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 --ALRLGIGMV-----HQHFvlveNFTVLENIIVGSpdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWV 148
Cdd:PRK13636 77 lmKLRESVGMVfqdpdNQLF----SASVYQDVSFGA--VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 149 EILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGR 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
267-478 |
4.98e-18 |
|
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: 82.69 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEaivaPTSREMLDRGVGLVPDDR----FRE 342
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK----PIKAKERRKSIGYVMQDVdyqlFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLISEfgtaenLVLGWQRKPEyrrgpflDRGKINDLaqrkLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLL 422
Cdd:cd03226 88 SVREE------LLLGLKELDA-------GNEQAETV----LKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 423 ANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-215 |
8.66e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLT--KRFGAVTAndsvdlDVRKGEIHCLFGENGAGKSTLSACLYGYYRAdSGVIRFKGQvaELNS-PADALRLGI 81
Cdd:COG4138 1 LQLNDVAvaGRLGPISA------QVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGR--PLSDwSAAELARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENIIVGSPDVGmllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALY------ 155
Cdd:COG4138 72 AYLSQQQSPPFAMPVFQYLALHQPAGA---SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwpti 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 156 -FGAELLILDEPTAVL-TPQQS--DQLfviLDGMRRQGLSIILISHKL-REVMQSDRVTILRKGK 215
Cdd:COG4138 149 nPEGQLLLLDEPMNSLdVAQQAalDRL---LRELCQQGITVVMSSHDLnHTLRHADRVWLLKQGK 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-215 |
1.14e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 9 NLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqvAELNSPADALRLGIGMVHQHF 88
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 89 VLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTA 168
Cdd:PRK13536 124 NLDLEFTVRENLLVFGRYFGM--STREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1550121285 169 VLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGR 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-170 |
1.14e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLgIGMV 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVG-SPDVGML-LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrTPHRSRFdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
....*...
gi 1550121285 163 LDEPTAVL 170
Cdd:PRK09536 163 LDEPTASL 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-215 |
1.25e-17 |
|
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: 81.89 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNS-PADALRLGIGMVHQHFVLVENfTVLENII 101
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI--DIRDiSRKSLRSMIGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGSPdvgmllsksTARQKVEDLCLRcgiELDLDREIWQ---------------LSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03254 99 LGRP---------NATDEEVIEAAK---EAGAHDFIMKlpngydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPqQSDQLfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03254 167 TSNIDT-ETEKL--IQEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGK 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-215 |
1.44e-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: 82.15 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAdALRLGIGMVHQHFVLVeNFTVLENI 100
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA-WLRRQVGVVLQENVLF-NRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGSPdvGMLLSKSTARQKVED-----LCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQS 175
Cdd:cd03252 97 ALADP--GMSMERVIEAAKLAGahdfiSELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1550121285 176 DqlfVILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03252 175 H---AIMRNMHDicAGRTVIIIAHRLSTVKNADRIIVMEKGR 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-215 |
1.44e-17 |
|
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: 81.39 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 13 RFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAlrlGIGMVHQHFVLVE 92
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR---PVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 93 NFTVLENIIVG-SPDVGMllsKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLT 171
Cdd:cd03298 84 HLTVEQNVGLGlSPGLKL---TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1550121285 172 PQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03298 161 PALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGR 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.82 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADAL---RLGIGMVHQH-----FVL 90
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE--PIKYDKKSLlevRKTVGIVFQNpddqlFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 91 venfTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVL 170
Cdd:PRK13639 95 ----TVEEDVAFGPLNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1550121285 171 TPQQSDQLFVILDGMRRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGK 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-215 |
1.80e-17 |
|
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: 81.10 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaLRLGIGMVHQHFVLVeNFTVLENI 100
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDVTLF-YGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGSPDV--GMLLSKSTaRQKVEDLCLR--CGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSD 176
Cdd:cd03245 99 TLGAPLAddERILRAAE-LAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550121285 177 QLFVILDGMRRqGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03245 178 RLKERLRQLLG-DKTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-215 |
2.07e-17 |
|
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: 83.61 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 9 NLTKRFGAVTANdsVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQV-----AELNSPADALRlgIGM 83
Cdd:COG4148 6 DFRLRRGGFTLD--VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsaRGIFLPPHRRR--IGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPDVGmllsKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKRAP----RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARlADHVVLLEQGR 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
270-485 |
2.27e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.39 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVA--PTSREMLDRGVGLVpddrFREG-LIS 346
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMGML----FQSGaLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLgWQRkpEYRRgpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREF-LNAKcLLLANQ 425
Cdd:cd03261 91 SLTVFENVAF-PLR--EHTR---LSEEEIREIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALaLDPE-LLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 426 PTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
273-485 |
2.63e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 82.44 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPDDR-FREGLISEfgta 351
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRKVRRSIGIVPQYAsVDEDLTGR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 352 ENLVL-----GWQRKPEYRRgpfldrgkindlAQRKLEEFRIVAAStDLPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:TIGR01188 85 ENLEMmgrlyGLPKDEAEER------------AEELLELFELGEAA-DRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 427 TRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
266-492 |
2.77e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGEEVLCD-INFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaPTSREMLDRGVGLVPddRFrEGL 344
Cdd:PRK13537 17 YGDKLVVDgLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARHARQRVGVVP--QF-DNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLgwqrkpeYRRGPFLDRGKINDLAQrKLEEFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:PRK13537 92 DPDFTVRENLLV-------FGRYFGLSAAAARALVP-PLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 425 QPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELG 492
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-215 |
2.96e-17 |
|
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: 81.12 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGI 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdVRDYT--LASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVeNFTVLENIIVGSPDVGMLLSKSTARQkVEDLCLRCGIELDLDREIW----QLSVGEQQWVEILKALYFG 157
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARA-ANAHEFIMELPEGYDTVIGergvKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 158 AELLILDEPTAVLTpQQSDQLfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03251 157 PPILILDEATSALD-TESERL--VQAALERlmKNRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
273-481 |
3.10e-17 |
|
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: 80.63 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPDDRfreGLISEFGTAE 352
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGYCPQFD---ALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVLgwqrkpeYRRGPFLDRGKINDLAQRKLEEFRIVAAStDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDV 432
Cdd:cd03263 95 HLRF-------YARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 433 AASEFVYEKILEKRaEGFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTV 481
Cdd:cd03263 167 ASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRciGSP 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
254-477 |
3.29e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 254 VLVVDHA-VAIGewGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRemldrgV 332
Cdd:COG1121 6 AIELENLtVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 333 GLVP-----DDRFReglIsefgTAENLVL-GWQRkpeyRRGPFL-----DRGKIND-LAQRKLEEFRivaastDLPVERL 400
Cdd:COG1121 78 GYVPqraevDWDFP---I----TVRDVVLmGRYG----RRGLFRrpsraDREAVDEaLERVGLEDLA------DRPIGEL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 401 SGGNAQRVILAREFL-NAKcLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:COG1121 141 SGGQQQRVLLARALAqDPD-LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-215 |
3.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGIGMVHQH----FVlveNF 94
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpetqFV---GR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLENIIVGSPDvgMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQ 174
Cdd:PRK13644 94 TVEEDLAFGPEN--LCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1550121285 175 SDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGK 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
273-485 |
3.44e-17 |
|
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: 80.49 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRemLDRGVGLVPDDRFREGLISEFgtaE 352
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VRRRIGIVFQDLSVDDELTGW---E 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVlgWQRKPEYRRGPFLDRGKINDLAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDV 432
Cdd:cd03265 93 NLY--IHARLYGVPGAERRERIDELLDFVGLLEAA------DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 433 AASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03265 165 QTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-215 |
4.60e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 80.27 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 12 KRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELnspadaLRLGIGMvhqhfvlV 91
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL------LGLGGGF-------N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 92 ENFTVLENIIVgspdVGMLLSKSTA--RQKVEDLCLRCGIELDLDREIWQLSVGeqqwveiLKA-LYFG------AELLI 162
Cdd:cd03220 97 PELTGRENIYL----NGRLLGLSRKeiDEKIDEIIEFSELGDFIDLPVKTYSSG-------MKArLAFAiatalePDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 163 LDEPTAVltpqqSDQLFVI-----LDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03220 166 IDEVLAV-----GDAAFQEkcqrrLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGK 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-201 |
5.03e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPaDALRlg 80
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--PVTGP-GADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 iGMVHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGV--PKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 161 LILDEPTAVL---TPQQSDQLfvILDGMRRQGLSIILISHKLRE 201
Cdd:COG4525 156 LLMDEPFGALdalTREQMQEL--LLDVWQRTGKGVFLITHSVEE 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-215 |
6.40e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAL---RLGIGMVHQ--HFVLVENfT 95
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklRKKVSLVFQfpEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 96 VLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDL-DREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQ 174
Cdd:PRK13641 103 VLKDVEFGPKNFG--FSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1550121285 175 SDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGK 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-215 |
6.41e-17 |
|
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: 79.54 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGeIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGMV 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLEniivgspdvgML--------LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:cd03264 78 PQEFGVYPNFTVRE----------FLdyiawlkgIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQLFVILDGMrRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVeSLCNQVAVLNKGK 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-478 |
7.49e-17 |
|
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: 78.25 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRgVGLVPddrfreglis 346
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efgtaenlvlgwQrkpeyrrgpFLDRGKINDLAQRkleefrivaastdlPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:cd03214 80 ------------Q---------ALELLGLAHLADR--------------PFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 427 TRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03214 125 TSHLDIAHQIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-215 |
8.15e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.68 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKR-FGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGIGMV 84
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFV-----LVENFTVLENIivgspdvgMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:cd03267 102 QKTQLwwdlpVIDSFYLLAAI--------YDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVL-TPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:cd03267 174 ILFLDEPTIGLdVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-215 |
9.48e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.41 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANdsVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnSPADalRlGIGM 83
Cdd:COG3840 2 LRLDDLTYRYGDFPLR--FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTAL-PPAE--R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVG-SPdvGMLLSkSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGlRP--GLKLT-AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 163 LDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARiADRVLLVADGR 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-215 |
1.03e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRF---------GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELN- 71
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 72 SPADALRLGIGMVHQHFVLVEN--FTVLEniIVGSPdVGMLLSKSTARQKVEDLCLRCGIELD---LDREIWQLSVGEQQ 146
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNprKTVRE--IIREP-LRHLLSLDKAERLARASEMLRAVDLDdsvLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 147 WVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERfCQRVMVMDNGQ 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-215 |
1.39e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAElNSPADALRlgIGM 83
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRH--VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGspdvgmLLSKSTARQ----KVEDlCLRCgIELD--LDREIWQLSVGEQQWVEILKALYFG 157
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG------LRMQKTPAAeitpRVME-ALRM-VQLEefAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVM-QSDRVTILRKGK 215
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALtMSDRIVVMRDGR 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-215 |
1.44e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspadALRLGIGMVH 85
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdVSRLH----ARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 86 QHFVLVENFTVLENIIVGspdVGML-----LSKSTARQKVedLCLRCGIELD--LDREIWQLSVGEQQWVEILKALYFGA 158
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFG---LTVLprrerPNAAAIKAKV--TQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 159 ELLILDEPTAVLTPQQSDQLFVILdgmrRQ-----GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWL----RQlheelKFTSVFVTHDQEEAMEvADRVVVMSQGN 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-214 |
1.98e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRF--GAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADA-L 77
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTDvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpMSKLSSAAKAeL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 R-LGIGMVHQHFVLVENFTVLENiiVGSPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:PRK11629 85 RnQKLGFIYQFHHLLPDFTALEN--VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-214 |
2.61e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAL---RLGIGMVHQhFVLVENF--TVL 97
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkpvRKKVGVVFQ-FPESQLFeeTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 98 ENIIVGSPDVGmlLSKSTARQKVEDLCLRCGieldLDREIWQ-----LSVGEQQWVEILKALYFGAELLILDEPTAVLTP 172
Cdd:PRK13643 104 KDVAFGPQNFG--IPKEKAEKIAAEKLEMVG----LADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1550121285 173 QQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKG 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
8-204 |
3.10e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRFgavtandsvDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAdalRLGIGMVHQH 87
Cdd:PRK10771 12 HHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 88 FVLVENFTVLENIIVGSpDVGMLLSkSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:PRK10771 80 NNLFSHLTVAQNIGLGL-NPGLKLN-AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1550121285 168 AVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ 204
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAAR 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-215 |
3.59e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.69 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSpaDALRLGIGMVHQHFVLVeNFTVLENIIVGSP 105
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVpLVQYDH--HYLHRQVALVGQEPVLF-SGSVRENIAYGLT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 106 DVGMLLSKSTARQKVED---LCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTpQQSDQLFviL 182
Cdd:TIGR00958 581 DTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD-AECEQLL--Q 657
|
170 180 190
....*....|....*....|....*....|...
gi 1550121285 183 DGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:TIGR00958 658 ESRSRASRTVLLIAHRLSTVERADQILVLKKGS 690
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-215 |
3.70e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTlsaCLY---GYYRADSGVIRFKGQ-VAELNSPADAlRLG 80
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYmivGLVKPDSGRIFLDGEdITHLPMHKRA-RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIivgspdvgML------LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKAL 154
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNI--------LAvlelrkLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 155 YFGAELLILDEPTAVLTP------QQsdqlfvILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPiavadiQK------IIRHLKERGIGVLITDHNVRETLGiCDRAYIISEGK 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-215 |
4.03e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFK---GQVAELNSPADA- 76
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrdGQLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 ----LRLGIGMVHQHFV--LVENFTVLENI-----IVGSPDVGMLlsKSTARQKVEDlclrcgIELDLDReIWQL----S 141
Cdd:PRK11701 83 rrrlLRTEWGFVHQHPRdgLRMQVSAGGNIgerlmAVGARHYGDI--RATAGDWLER------VEIDAAR-IDDLpttfS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 142 VGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVArLLAHRLLVMKQGR 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-215 |
4.77e-16 |
|
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: 81.60 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRF--GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNspADALRLGIGMV 84
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN--LDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGR--SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMrRQGLSIILISHKLREV-MQSDRVTILRKGK 215
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEAdLLGDRIAIISQGR 1137
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
269-478 |
5.78e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 77.16 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRG--VGLVPDD-------R 339
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQMVFQDpmsslnpR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FR-EGLISEfgtaenlvlgwqrkpeyrrgPFLDRGKINDLAQRK---LEEFRIVAASTD----LPVErLSGGNAQRVILA 411
Cdd:cd03257 99 MTiGEQIAE--------------------PLRIHGKLSKKEARKeavLLLLVGVGLPEEvlnrYPHE-LSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 412 REFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
273-476 |
6.06e-16 |
|
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: 74.97 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLVPDdrfreglisefgtae 352
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 nlvlgwqrkpeyrrgpfldrgkindlaqrkleefrivaastdlpverLSGGNAQRVILAREFLNAKCLLLANQPTRGLDV 432
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 433 AASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
249-485 |
7.53e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 80.19 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 249 APGREVLVVDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvAPTSREML 328
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL-SDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 329 DRGVGLVPDDRFregLISefGT-AENLVLGwqrKPEYrrgpflDRGKINDLAQR-KLEEFriVAAST---DLPVE----R 399
Cdd:COG4988 410 RRQIAWVPQNPY---LFA--GTiRENLRLG---RPDA------SDEELEAALEAaGLDEF--VAALPdglDTPLGeggrG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 400 LSGGNAQRVILAREFLNAKCLLLANQPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIVG 479
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLD-AETEAEILQALRRLAKGRTVILITHRL-ALLAQADRILVLDDGRIVE 551
|
....*.
gi 1550121285 480 TVRPEE 485
Cdd:COG4988 552 QGTHEE 557
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-215 |
7.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGA------VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPA 74
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRLGIGMVHQH------FVLVEnftvlENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWV 148
Cdd:PRK13633 81 WDIRNKAGMVFQNpdnqivATIVE-----EDVAFGPENLG--IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 149 EILKALYFGAELLILDEPTAVLTPQ-QSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSgRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGK 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-215 |
1.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQV---AELNSPADALRLGIGMVHQhFVLVENF--TVL 97
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitsTSKNKDIKQIRKKVGLVFQ-FPESQLFeeTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 98 ENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDL-DREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSD 176
Cdd:PRK13649 105 KDVAFGPQNFG--VSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1550121285 177 QLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13649 183 ELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGK 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-200 |
1.28e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTAN-----DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALR 78
Cdd:COG1101 2 LELKNLSKTFNPGTVNekralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 lgIGMVHQHFVL--VENFTVLENIIV-----GSPDVGMLLSKSTA---RQKVEDLCLrcGIELDLDREIWQLSVGEQQWV 148
Cdd:COG1101 82 --IGRVFQDPMMgtAPSMTIEENLALayrrgKRRGLRRGLTKKRRelfRELLATLGL--GLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 149 EILKALYFGAELLILDEPTAVLTPQQSDQL------FVildgmRRQGLSIILISHKLR 200
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVleltekIV-----EENNLTTLMVTHNME 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-214 |
1.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFkGQVAELNSPADA----LRLGIGMVHQ--HFVLVE 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKyirpVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 93 NfTVLENIIVGSPDVGMLLSKstARQKVEDLCLRCGIELD-LDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLT 171
Cdd:PRK13646 101 D-TVEREIIFGPKNFKMNLDE--VKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1550121285 172 PQQSDQLFVILDGMR-RQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARyADEVIVMKEG 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
257-491 |
1.84e-15 |
|
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: 76.00 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 257 VDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLdRGVGLVP 336
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-RRVQMVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 337 DD-------RFR-EGLISEfgtaenlvlgwqrkpeyrrgPFLDRGKinDLAQRKLEEfriVAASTDLPVE-------RLS 401
Cdd:COG1124 86 QDpyaslhpRHTvDRILAE--------------------PLRIHGL--PDREERIAE---LLEQVGLPPSfldryphQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 402 GGNAQRVILAREFLNAKCLLLANQPTRGLDVAasefVYEKILE-----KRAEGFAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVS----VQAEILNllkdlREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
250
....*....|....*
gi 1550121285 477 IVgtvrpEETTLLEL 491
Cdd:COG1124 217 IV-----EELTVADL 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-201 |
2.02e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPAdALRlgiGM 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPG-AER---GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGV--EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1550121285 164 DEPTAVL---TPQQSDQLfvILDGMRRQGLSIILISHKLRE 201
Cdd:PRK11248 153 DEPFGALdafTREQMQTL--LLKLWQETGKQVLLITHDIEE 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
273-482 |
2.44e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.69 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaptSREMLDRgVGLVPDDRfreGLISEFGTAE 352
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRR-IGYLPEER---GLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVlgwqrkpeY---RRGpfLDRGKINDLAQRKLEEFRIVAASTDlPVERLSGGNAQRVILAREFLNAKCLLLANQPTRG 429
Cdd:COG4152 91 QLV--------YlarLKG--LSKAEAKRRADEWLERLGLGDRANK-KVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 430 LDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTVR 482
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsGSVD 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
2.50e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF---GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaL 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQH----FVlveNFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKA 153
Cdd:PRK13642 80 RRKIGMVFQNpdnqFV---GATVEDDVAFGMENQG--IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 154 LYFGAELLILDEPTAVLTPQ-QSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTgRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGE 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-215 |
2.78e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 16 AVTANDsVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADaLRLGIGMVHQHfvlvenft 95
Cdd:PRK13648 22 SFTLKD-VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQN-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 96 vLENIIVGSP---DVGM-LLSKSTARQKVEDLCLRCGIELDL----DREIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:PRK13648 92 -PDNQFVGSIvkyDVAFgLENHAVPYDEMHRRVSEALKQVDMleraDYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550121285 168 AVLTPQQSDQLFVILDGMRR-QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVMNKGT 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
257-477 |
2.99e-15 |
|
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: 74.83 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 257 VDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLD---RGVG 333
Cdd:cd03255 6 LSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 334 LVpddrFRE-GLISEFGTAENLVLgwqrkpeyrrgPFLDRGKINDLAQRK----LEEFRIVAASTDLPVErLSGGNAQRV 408
Cdd:cd03255 86 FV----FQSfNLLPDLTALENVEL-----------PLLLAGVPKKERRERaeelLERVGLGDRLNHYPSE-LSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 409 ILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEElDDLLRLCDRIAVIFKGKI 477
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-211 |
3.48e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYG------YYRADSgvIRFKGQvaelns 72
Cdd:COG4170 2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdnwHVTADR--FRWNGI------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 73 paDALRLG-----------IGMVHQHFV--LVENFTVLENIIVGSPDV---GMLLSKSTAR-QKVEDLCLRCGI---ELD 132
Cdd:COG4170 74 --DLLKLSprerrkiigreIAMIFQEPSscLDPSAKIGDQLIEAIPSWtfkGKWWQRFKWRkKRAIELLHRVGIkdhKDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 133 LDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRR-QGLSIILISHKLREVMQ-SDRVTI 210
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQwADTITV 231
|
.
gi 1550121285 211 L 211
Cdd:COG4170 232 L 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-215 |
3.74e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFgAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNSPADALRLG 80
Cdd:PRK13637 6 ENLTHIYMEGTPF-EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQH--FVLVENfTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELD--LDREIWQLSVGEQQWVEILKALYF 156
Cdd:PRK13637 85 VGLVFQYpeYQLFEE-TIEKDIAFGPINLG--LSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 157 GAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGK 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-215 |
4.45e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.73 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF----------------------GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 59 GVIRFKGQVAELnspadaLRLGIGMVHQhfvlvenFTVLENIIVgspdVGMLL--SKSTARQKVEDLCLRCGIELDLDRE 136
Cdd:COG1134 81 GRVEVNGRVSAL------LELGAGFHPE-------LTGRENIYL----NGRLLglSRKEIDEKFDEIVEFAELGDFIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 137 IWQLSVGEQqwveiLK-----ALYFGAELLILDEPTAVltpqqSDQLFV-----ILDGMRRQGLSIILISHKLREVMQ-S 205
Cdd:COG1134 144 VKTYSSGMR-----ARlafavATAVDPDILLVDEVLAV-----GDAAFQkkclaRIRELRESGRTVIFVSHSMGAVRRlC 213
|
250
....*....|
gi 1550121285 206 DRVTILRKGK 215
Cdd:COG1134 214 DRAIWLEKGR 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-215 |
5.27e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.89 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGA-----VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVI--------------RFKGQV 67
Cdd:PRK13651 5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 68 AELN---------SPADALRLGIGMVHQ--HFVLVENfTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELD-LDR 135
Cdd:PRK13651 85 EKLViqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGV--SKEEAKKRAAKYIELVGLDESyLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 136 EIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDG 241
|
.
gi 1550121285 215 K 215
Cdd:PRK13651 242 K 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-167 |
5.45e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 7 VQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnspadaLRlgIGMVHQ 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVGSPDVGMLLSKS------------------------------TARQKVEDLCLRCGI-ELDLDR 135
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELeeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDR 148
|
170 180 190
....*....|....*....|....*....|..
gi 1550121285 136 EIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
267-480 |
7.24e-15 |
|
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: 73.41 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPtsREMLDRgVGLVPDdrfREGLIS 346
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRR-IGALIE---APGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLgwqrkpeYRRGPFLDRGKINdlaqrklEEFRIV--AASTDLPVERLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:cd03268 86 NLTARENLRL-------LARLLGIRKKRID-------EVLDVVglKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 425 QPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGT 480
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
269-485 |
7.38e-15 |
|
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: 74.25 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRGVGLVpddrFREG-LI 345
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRIGML----FQGGaLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENLVLgwqrkP--EYRRgpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREF-LNAKCLLL 422
Cdd:COG1127 95 DSLTVFENVAF-----PlrEHTD---LSEAEIRELVLEKLELVGLPGAADKMPSE-LSGGMRKRVALARALaLDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 423 aNQPTRGLD-VAASEFVyEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG1127 166 -DEPTAGLDpITSAVID-ELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
273-485 |
7.45e-15 |
|
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: 75.92 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE-------AIVAPTSRemldRGVGLVpddrFREG-L 344
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkGIFLPPEK----RRIGYV----FQEArL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGWQR-KPEYRRGPF---LDRGKINDLAQRkleefrivaastdlPVERLSGGNAQRVILAREFLNAKCL 420
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRaRPSERRISFervIELLGIGHLLGR--------------LPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 421 LLANQPTRGLDVAASefvYEKI--LEK-RAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:TIGR02142 153 LLMDEPLAALDDPRK---YEILpyLERlHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
267-477 |
7.66e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 73.31 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvAPTSREMLDRGVGLVPDDRFREGlis 346
Cdd:COG4619 12 GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPPPEWRRQVAYVPQEPALWG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efGT-AENLVLGWQrkpeYRRGPFlDRGKINDLaqrkLEEFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:COG4619 88 --GTvRDNLPFPFQ----LRERKF-DRERALEL----LERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
267-462 |
8.43e-15 |
|
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: 73.28 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLC-DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPtsREMLDRGVGLVPDdrfREGLI 345
Cdd:COG4133 13 GERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA--REDYRRRLAYLGH---ADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENLVLgWQRkpeyRRGPFLDRGKINDLaqrkLEEFRIVAAStDLPVERLSGGNAQRVILAREFL-NAKCLLLaN 424
Cdd:COG4133 88 PELTVRENLRF-WAA----LYGLRADREAIDEA----LEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLsPAPLWLL-D 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1550121285 425 QPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDL 462
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
9.39e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSAC------LYGYYRAdSGVIRFKGQVAeLNSPADA 76
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARV-SGEVYLDGQDI-FKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 LRLGIGMVHQHFVLVENFTVLENIIVGSPDVGMLLSKSTARQKV----EDLCLRCGIELDLDREIWQLSVGEQQWVEILK 152
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVrwalEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 153 ALYFGAELLILDEPTAVLTPQQS---DQLFVILdgmrRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTakiESLFLEL----KKDMTIVLVTHFPQQAARiSDYVAFLYKGQ 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
270-476 |
1.12e-14 |
|
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: 72.22 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPT-SREMLDRGVGLVpddrFREG-LISE 347
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdELPPLRRRIGMV----FQDFaLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGwqrkpeyrrgpfldrgkindlaqrkleefrivaastdlpverLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:cd03229 91 LTVLENIALG------------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1550121285 428 RGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-215 |
1.13e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 14 FGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAEL-NSPADALRLGIGMVHQHFVLV 91
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLkNREVPFLRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 92 ENFTVLENIIVgsPDVGMLLSKSTARQKVEDLCLRCGIeLDLDREI-WQLSVGEQQWVEILKALYFGAELLILDEPTAVL 170
Cdd:PRK10908 92 MDRTVYDNVAI--PLIIAGASGDDIRRRVSAALDKVGL-LDKAKNFpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1550121285 171 TPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD-RVTILRKGK 215
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGH 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
269-478 |
1.16e-14 |
|
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: 73.52 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeaIVAPTSREMLDRGVGLVPDDRfrEGLISEF 348
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVVFGQK--TQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLgwqRKPEYRRGPFLDRGKINDLAQR-KLEEFrivaasTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:cd03267 111 PVIDSFYL---LAAIYDLPPARFKKRLDELSELlDLEEL------LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 428 RGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
273-485 |
1.26e-14 |
|
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: 73.24 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVaptsremldrgvGLVPDDRFREGL------IS 346
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT------------GLPPHEIARLGIgrtfqiPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGT---AENLVLG---WQRKPEYRRGPFLDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRVILAREF-LNAKC 419
Cdd:cd03219 86 LFPEltvLENVMVAaqaRTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALaTDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 420 LLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03219 165 LLL-DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-215 |
1.54e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGIGM 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIvGSPDVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLM-AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAvCERAYIVSQGH 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
267-485 |
2.22e-14 |
|
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: 73.15 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLVPDDRfreglIS 346
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAYVPQEP-----PA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFG-TAENLV-LGwqRKPeyRRGPFL-----DRGKIND-LAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFL-NA 417
Cdd:COG1120 87 PFGlTVRELVaLG--RYP--HLGLFGrpsaeDREAVEEaLERTGLEHLA------DRPVDELSGGERQRVLIARALAqEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 418 KCLLLaNQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG1120 157 PLLLL-DEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
271-497 |
2.29e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSS--GRFHLNGEAIVAPTSREMLDRGVGLVpddrFRE-GLISE 347
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAGIAII----HQElALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGwqrkPEYRRGPFLDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRVILAREfLNAKC-LLLANQP 426
Cdd:PRK13549 97 LSVLENIFLG----NEITPGGIMDYDAMYLRAQKLLAQLKL-DINPATPVGNLGLGQQQLVEIAKA-LNKQArLLILDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 427 TRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELGMMMAG 497
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
267-497 |
3.24e-14 |
|
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: 74.86 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSS--GRFHLNGEAIVAPTSREMLDRGVGLVPDDRfreGL 344
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQEL---TL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGWQRKpeyRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:TIGR02633 90 VPELSVAENIFLGNEIT---LPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 425 QPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELGMMMAG 497
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-215 |
3.50e-14 |
|
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: 71.73 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTkrFGAVTANDS-----VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSpAD 75
Cdd:cd03248 8 LKGIVKFQNVT--FAYPTRPDTlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRLGIGMVHQHFVLVENfTVLENIIVGSPDVGM-----LLSKSTARQKVEDLCLrcGIELDLDREIWQLSVGEQQWVEI 150
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFecvkeAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 151 LKALYFGAELLILDEPTAVL---TPQQSDQLfvILDGMRRQglSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03248 162 ARALIRNPQVLILDEATSALdaeSEQQVQQA--LYDWPERR--TVLVIAHRLSTVERADQILVLDGGR 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
266-485 |
3.63e-14 |
|
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: 71.98 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVaPTSREMldRGVGLVPDDRfreGLI 345
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEK--RDISYVPQNY---ALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENLVLGWQRKPEYRrgPFLDRgKINDLAqrkleEFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDK--KEIER-KVLEIA-----EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
4.23e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnspadalrLG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVL-------VENFtvleniivgspdvgMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKA 153
Cdd:PRK09544 69 IGYVPQKLYLdttlpltVNRF--------------LRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 154 LYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVM-QSDRVTIL 211
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-215 |
4.59e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKSTLSACLYGYYRAdSGVIRFKGQVAELNSPADALRLGiGMVHQHFVLVENFTVLENIIVGSPD 106
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 107 vgmLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWV-------EILKALYFGAELLILDEPTAVLTPQQSDQLF 179
Cdd:PRK03695 97 ---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1550121285 180 VILDGMRRQGLSIILISHKL-REVMQSDRVTILRKGK 215
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLnHTLRHADRVWLLKQGK 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-215 |
8.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAEL---NSPADALRLGIGMV-----HQHFvlvENf 94
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkkNKKLKPLRKKVGIVfqfpeHQLF---EE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELD-LDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQ 173
Cdd:PRK13634 102 TVEKDICFGPMNFGV--SEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1550121285 174 QSD---QLFVILDgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13634 180 GRKemmEMFYKLH--KEKGLTTVLVTHSMEDAARyADQIVVMHKGT 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
271-485 |
1.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDrgvglvpDDRFREGLISEFGT 350
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK-------KLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 351 A---ENLVLgwqRKPEYrrGPfLDRGKINDLAQRK-LEEFRIVAASTDL----PVErLSGGNAQRVILAREFLNAKCLLL 422
Cdd:PRK13641 96 AqlfENTVL---KDVEF--GP-KNFGFSEDEAKEKaLKWLKKVGLSEDLisksPFE-LSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 423 ANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
269-478 |
1.11e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVA-PTSREMLDrGVGLVPDDRfreGLISE 347
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE-AVAIVPEGR---RVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGwqrkpeyrrGPFLDRGKINDLAQR------KLEEFRIVAASTdlpverLSGGNAQRVILAREFLNAKCLL 421
Cdd:PRK11614 95 MTVEENLAMG---------GFFAERDQFQERIKWvyelfpRLHERRIQRAGT------MSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 422 LANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
269-482 |
1.82e-13 |
|
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: 69.42 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPtsremlDRGVGLVpddrFREGLISEF 348
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP------GPDRGYV----FQQDALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTA-ENLVLGwqrkPEYRRGPfldRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:cd03293 88 LTVlDNVALG----LELQGVP---KAEARERAEELLELVGLSGFENAYPHQ-LSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 428 RGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFK--GKIVGTVR 482
Cdd:cd03293 160 SALDALTREQLQEELLDiWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
267-478 |
2.04e-13 |
|
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: 69.47 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvapTSREMLDRGVGLVPDDRfreGLIS 346
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMVFQDY---ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGWQRKPeyrrgpfLDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:cd03259 86 HLTVAENIAFGLKLRG-------VPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 427 TRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03259 158 LSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
267-480 |
2.08e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 67.84 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVPddrfreglis 346
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVY---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efgtaenlvlgwqrkpeyrrgpfldrgkindlaQrkleefrivaastdlpverLSGGNAQRVILAREF-LNAKCLLLaNQ 425
Cdd:cd03216 82 ---------------------------------Q-------------------LSVGERQMVEIARALaRNARLLIL-DE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGT 480
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-215 |
2.10e-13 |
|
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: 68.49 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFG--AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqvAELNSPADALRLGIG 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--VPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHfVLVENFTVLENIivgspdvgmllskstarqkvedlclrcGIeldldreiwQLSVGEQQWVEILKALYFGAELLI 162
Cdd:cd03247 79 VLNQR-PYLFDTTLRNNL---------------------------GR---------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 163 LDEPTAVLTPQQSDQLF-VILDGMRrqGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03247 122 LDEPTVGLDPITERQLLsLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGK 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
273-427 |
2.16e-13 |
|
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: 67.67 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTsREMLDRGVGLVPDDrfrEGLISEFGTAE 352
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQD---PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 353 NLVLGwqrkpeyRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVER---LSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:pfam00005 79 NLRLG-------LLLKGLSKREKDARAEEALEKLGLGDLADRPVGERpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-215 |
2.45e-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: 69.49 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPadALRLGIGMVHQHFVLVENfTVLEN 99
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdIRDLNLR--WLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 100 IIVGSPDVGMllskstarQKVEDLCLRCGIE---LDL----DREI----WQLSVGEQQWVEILKALYFGAELLILDEPTA 168
Cdd:cd03249 97 IRYGKPDATD--------EEVEEAAKKANIHdfiMSLpdgyDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1550121285 169 VLTPQQSDQLFVILDGMRRqGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03249 169 ALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-215 |
2.97e-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: 68.01 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTAN--DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPaDALRLGIG 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENfTVLENIivgspdvgmllskstarqkvedlclrcgieldldreiwqLSVGEQQWVEILKALYFGAELLI 162
Cdd:cd03246 80 YLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 163 LDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-215 |
3.59e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGY--YRADSGVIRFKGQ-VAELNsPADALRL 79
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGEsILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 80 GIGMVHQHfvLVEnftvleniIVGSPDVGMLLSKSTARQKVEDLCLRCGIE-LDLDREIWQL----------------SV 142
Cdd:CHL00131 85 GIFLAFQY--PIE--------IPGVSNADFLRLAYNSKRKFQGLPELDPLEfLEIINEKLKLvgmdpsflsrnvnegfSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 143 GEQQWVEILKALYFGAELLILDEPTAVLtpqQSDQLFVILDG---MRRQGLSIILISH--KLREVMQSDRVTILRKGK 215
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGL---DIDALKIIAEGinkLMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-215 |
3.86e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.67 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 35 LFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSpaDALRLGIGMVHQHFVLVENfTVLENIIVGSPdvgmlLSK 113
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRpLSSLSH--SVLRQGVAMVQQDPVVLAD-TFLANVTLGRD-----ISE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 114 STARQKVEDLCLRC-------GIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVL---TPQQSDQLFVILd 183
Cdd:PRK10790 444 EQVWQALETVQLAElarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIdsgTEQAIQQALAAV- 522
|
170 180 190
....*....|....*....|....*....|..
gi 1550121285 184 gmrRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK10790 523 ---REHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
269-478 |
4.58e-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: 68.39 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeaivapTSREMLD-----RGVGLVPDDRFreg 343
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG------TDIRQLDpadlrRNIGYVPQDVT--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 LIseFGTA-ENLVLGWQRKPEYRRGPFLDRGKINDLAQRKleefrivAASTDLPV-ER---LSGGNAQRVILAREFLNAK 418
Cdd:cd03245 89 LF--YGTLrDNITLGAPLADDERILRAAELAGVTDFVNKH-------PNGLDLQIgERgrgLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 419 CLLLANQPTRGLDVAASEFVYEKiLEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIV 478
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-215 |
5.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.44 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS---GVIRFKGqvAELNSPAD-ALRLGIGMVHQH----FVlve 92
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG--ITLTAKTVwDIREKVGIVFQNpdnqFV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 93 NFTVLENIIVGspdvgmLLSKSTARQK----VEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTA 168
Cdd:PRK13640 99 GATVGDDVAFG------LENRAVPRPEmikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1550121285 169 VLTPQQSDQ-LFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13640 173 MLDPAGKEQiLKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
268-472 |
5.79e-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: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 268 EEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvAPTSREMLDRGVGLVPDDRFreglISE 347
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADSWRDQIAWVPQHPF----LFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGwqrKPEyrrgpfLDRGKINDLAQRK-LEEF-RIVAASTDLPV----ERLSGGNAQRVILAREFLNAKCLL 421
Cdd:TIGR02857 410 GTIAENIRLA---RPD------ASDAEIREALERAgLDEFvAALPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 422 LANQPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVI 472
Cdd:TIGR02857 481 LLDEPTAHLD-AETEAEVLEALRALAQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
255-488 |
6.26e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 255 LVVDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEaivaPTSREMLDRGVGL 334
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ----PTRQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 335 VPDDrfrEGLISEFGT-AENLVL-------GWQRKPEYRrgpflDRGKIND-LAQRKLEEFRivaastDLPVERLSGGNA 405
Cdd:PRK15056 83 VPQS---EEVDWSFPVlVEDVVMmgryghmGWLRRAKKR-----DRQIVTAaLARVDMVEFR------HRQIGELSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 406 QRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDrIAVIFKGKIVGTvRPEE 485
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLAS-GPTE 226
|
...
gi 1550121285 486 TTL 488
Cdd:PRK15056 227 TTF 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-215 |
7.16e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.75 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAlrlGIG 82
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENIIVGspdVGML-LSKSTARQKVEDlclrcGIEL-DL----DREIWQLSVGEQQWVEILKALYF 156
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYG---LKMLgVPKEERKQRVKE-----ALELvDLagfeDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 157 GAELLILDEP----TAVLTPQQSDQlfvILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11432 154 KPKVLLFDEPlsnlDANLRRSMREK---IRELQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGK 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-167 |
9.78e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 9.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFkGQvaelnspadalRLGIGM 83
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----------TVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHF-VLVENFTVLENIIVGSPDV----------GMLLSKSTARQKVEDlclrcgieldldreiwqLSVGEQQWVEILK 152
Cdd:COG0488 383 FDQHQeELDPDKTVLDELRDGAPGGteqevrgylgRFLFSGDDAFKPVGV-----------------LSGGEKARLALAK 445
|
170
....*....|....*
gi 1550121285 153 ALYFGAELLILDEPT 167
Cdd:COG0488 446 LLLSPPNVLLLDEPT 460
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
273-480 |
1.09e-12 |
|
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: 67.13 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeaiVAPTSREMLDRGVGLVpddrFREG-LISEFGTA 351
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSML----FQENnLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 352 ENLVLGwqRKPEYRRGPfLDRGKIND-LAQRKLEEFrivaaSTDLPvERLSGGNAQRVILAREFLNAKCLLLANQPTRGL 430
Cdd:cd03298 89 QNVGLG--LSPGLKLTA-EDRQAIEVaLARVGLAGL-----EKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 431 DVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGT 480
Cdd:cd03298 160 DPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-478 |
1.23e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRF---GAV-TANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRAD-----SGVIRFKGQvAELNSPA 74
Cdd:PRK15134 5 LLAIENLSVAFrqqQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGE-SLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRL----GIGMVHQH-FVLVENFTVLENII--VGSPDVGMllSKSTARQKVEDlCL-RCGIELDLDREI---WQLSVG 143
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEpMVSLNPLHTLEKQLyeVLSLHRGM--RREAARGEILN-CLdRVGIRQAAKRLTdypHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 144 EQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGKvvatve 221
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNGR------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 222 taTTTAESITALMVG--HQVTK----------------------RVSDRSVA-PGREVL---VVDHAVaigewgeeVLCD 273
Cdd:PRK15134 235 --CVEQNRAATLFSAptHPYTQkllnsepsgdpvplpepaspllDVEQLQVAfPIRKGIlkrTVDHNV--------VVKN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 274 INFTIAENEILGLAGVAGNGQKELFEVLMgvRTLSS-GRFHLNGEAIVAPTSREMLD--RGVGLV---PDDRFREGLISE 347
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALL--RLINSqGEIWFDGQPLHNLNRRQLLPvrHRIQVVfqdPNSSLNPRLNVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLgwqrkpeyrRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:PRK15134 383 QIIEEGLRV---------HQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 428 RGLD--VAASEFVYEKILEKRaEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK15134 454 SSLDktVQAQILALLKSLQQK-HQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
269-482 |
1.30e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 67.22 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRGVGLVpddrFRE-GLI 345
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRIGMI----FQHfNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENL-----VLGWQRKPEYRRGPFLdrgkindLAQRKLEEFRivaasTDLPVErLSGGNAQRVILAREFLNAKCL 420
Cdd:cd03258 95 SSRTVFENValpleIAGVPKAEIEERVLEL-------LELVGLEDKA-----DAYPAQ-LSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 421 LLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTVR 482
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVeeGTVE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
273-479 |
1.61e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 66.55 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAEnEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLD-----RGVGLVpddrFRE-GLIS 346
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSRKKINlppqqRKIGLV----FQQyALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGWQRKpeyrrgpflDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:cd03297 89 HLNVRENLAFGLKRK---------RNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 427 TRGLDVAASEFVyEKILEKRAEGF--AVFLASEELDDLLRLCDRIAVIFKGKIVG 479
Cdd:cd03297 159 FSALDRALRLQL-LPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
1.62e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.85 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTkrFGAVTANDSV----DLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSpaDALR 78
Cdd:PRK11160 338 SLTLNNVS--FTYPDQPQPVlkglSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpIADYSE--AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQHfVLVENFTVLENIIVGSPDVG--MLlskSTARQKVEdlcLRCGIELDLDREIW------QLSVGEQQWVEI 150
Cdd:PRK11160 414 QAISVVSQR-VHLFSATLRDNLLLAAPNASdeAL---IEVLQQVG---LEKLLEDDKGLNAWlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 151 LKALYFGAELLILDEPTAVL---TPQQsdqlfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLdaeTERQ------ILELLAEhaQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-215 |
2.03e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLgiGM 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpISMLSSRQLARRL--AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIIVG-SPDV---GMLLSKStaRQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrSPWLslwGRLSAED--NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGH 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-215 |
2.22e-12 |
|
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: 66.36 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF--GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNS-PADALRLGI 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV--DISKiGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENfTVLENI-IVGSPDVGML---LSKSTARQKVEDLCLrcGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLdPFGEYSDEELwqaLERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 158 AELLILDEPTAVLTPQqSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03244 158 SKILVLDEATASVDPE-TDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGR 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-215 |
2.26e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAElnsPAD-ALRLGIGMVHQ 86
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDiATRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIivgspdvgML------LSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:NF033858 347 AFSLYGELTVRQNL--------ELharlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVIL-DGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLiELSREDGVTIFISTHFMNEAERCDRISLMHAGR 474
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
2.39e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNspADALRLG 80
Cdd:PRK13652 2 HLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGePITKEN--IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFV-LVENFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAE 159
Cdd:PRK13652 80 VGLVFQNPDdQIFSPTVEQDIAFGPINLG--LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 160 LLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEmADYIYVMDKGR 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
270-485 |
2.59e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLVPddrfREGLISEFG 349
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLP----QHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVlgwqrkpEYRRGPFLDR-GKIND----LAQRKLEEFRIVAAStDLPVERLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:PRK11231 92 TVRELV-------AYGRSPWLSLwGRLSAednaRVNQAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 425 QPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-215 |
2.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGvirfKGQVAELNSPADA--------LRLGIGMVHQ--HF 88
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG----QTIVGDYAIPANLkkikevkrLRKEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 89 VLVENfTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELD-LDREIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGE--NKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 168 AVLTPQQSD---QLFVILDgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13645 179 GGLDPKGEEdfiNLFERLN--KEYKKRIIMVTHNMDQVLRiADEVIVMHEGK 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-215 |
3.71e-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: 65.26 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKSTLSACLYGY--YRADSGVIRFKGQvaelNSPADALRLGIGMVHQHFVLVENFTVLENIIVgs 104
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGR----PLDKRSFRKIIGYVPQDDILHPTLTVRETLMF-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 105 pdvgmllsksTArqkvedlCLRCgieldldreiwqLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDG 184
Cdd:cd03213 106 ----------AA-------KLRG------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|...
gi 1550121285 185 MRRQGLSIILISHKLREVMQS--DRVTILRKGK 215
Cdd:cd03213 157 LADTGRTIICSIHQPSSEIFElfDKLLLLSQGR 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-197 |
3.99e-12 |
|
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: 65.07 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAEL-NSPADALrLGIG 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTpLAEQrDEPHENI-LYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 mvHQHFVLVEnFTVLENIIVGSPDVGmllsksTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:TIGR01189 80 --HLPGLKPE-LSALENLHFWAAIHG------GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1550121285 163 LDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISH 197
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-215 |
4.89e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD-ALRLGIG 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 83 MVHQHFVLVENFTVLENIIVGS-PDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELL 161
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSlRNLG--VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 162 ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQ 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-215 |
5.43e-12 |
|
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: 64.80 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 22 SVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAelnspadalrlgigmvhqhFV----LVENFTVL 97
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA-------------------YVsqepWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 98 ENIIVGSPdvgmlLSKSTARQKVEDLCLrcgiELDLDR-------EIWQ----LSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:cd03250 84 ENILFGKP-----FDEERYEKVIKACAL----EPDLEIlpdgdltEIGEkginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPQQSDQLF--VILdGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03250 155 LSAVDAHVGRHIFenCIL-GLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
267-478 |
5.78e-12 |
|
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: 65.67 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRE--MLDRGVGLVpddrFRE-G 343
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQIGMI----FQQfN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 LISEFGTAENLVLG-------WQR-----KPEYRRGPF--LDRGKINDLAQRKleefrivaastdlpVERLSGGNAQRVI 409
Cdd:cd03256 89 LIERLSVLENVLSGrlgrrstWRSlfglfPKEEKQRALaaLERVGLLDKAYQR--------------ADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 410 LAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEK-RAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
267-485 |
6.18e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVPDDrfrEGLIS 346
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGWQRKPEyrrgpfLDRGKINDLAQRKLEEFRIVAASTDLPvERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDD------LSAEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 427 TRGLDvAASEFVYEKILEK-RAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK10895 165 FAGVD-PISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-197 |
7.12e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.81 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRAD---SGVIRFKGQ-VAELNspadALRLG 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRrLTALP----AEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDVgmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPT---IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550121285 161 LILDEPTAVLTPQQSDQL--FViLDGMRRQGLSIILISH 197
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFreFV-FEQIRQRGIPALLVTH 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
271-497 |
7.46e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVpddrFRE-GLISEFG 349
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII----YQElSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRKPEYRRGPFLDRGKINDLAQRKLEEFRIvAASTDLPVERLSGGNAQRVILAREF-LNAKCLLLaNQPTR 428
Cdd:PRK09700 97 VLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLmLDAKVIIM-DEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 429 GLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELGMMMAG 497
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-199 |
8.04e-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: 67.39 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 15 GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqVAELNSPADALRLGIGMVHQHFVLVENf 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-VPVSSLDQDEVRRRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLENIIVGSPDV-GMLLSKSTARQKVEDLC--LRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLT 171
Cdd:TIGR02868 424 TVRENLRLARPDAtDEELWAALERVGLADWLraLPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*....
gi 1550121285 172 PQQSDQLF-VILDGMrrQGLSIILISHKL 199
Cdd:TIGR02868 504 AETADELLeDLLAAL--SGRTVVLITHHL 530
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
8.62e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLygyYRAD--------SGVIRFKGqvAELNS 72
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNdlnpevtiTGSIVYNG--HNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 73 P-ADA--LRLGIGMVHQHfvlvEN---FTVLENIIVGSPDVGmLLSKSTARQKVEDLCLRCGIELDL-DR---EIWQLSV 142
Cdd:PRK14239 77 PrTDTvdLRKEIGMVFQQ----PNpfpMSIYENVVYGLRLKG-IKDKQVLDEAVEKSLKGASIWDEVkDRlhdSALGLSG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 143 GEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQgLSIILISHKLREVMQ-SDR 207
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRiSDR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
267-497 |
8.79e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRfreGLIS 346
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL---NLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGwqRKPeyRRGPFLDRGKINDLAQRKLEEFRIVAASTDlPVERLSGGNAQRVILAREF-LNAKCLLLaNQ 425
Cdd:PRK10982 87 QRSVMDNMWLG--RYP--TKGMFVDQDKMYRDTKAIFDELDIDIDPRA-KVATLSVSQMQMIEIAKAFsYNAKIVIM-DE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLELGMMMAG 497
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-215 |
9.62e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 9 NLTKRFGAVTANdsVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQV-----AELNSPADALRlgIGM 83
Cdd:PRK11144 5 NFKQQLGDLCLT--VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaeKGICLPPEKRR--IGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 84 VHQHFVLVENFTVLENIivgspDVGMllsKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLIL 163
Cdd:PRK11144 81 VFQDARLFPHYKVRGNL-----RYGM---AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 164 DEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11144 153 DEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRlADRVVVLEQGK 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-214 |
1.18e-11 |
|
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: 64.27 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 22 SVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAL---RLGIGMVHQHFVLVeNFTVLE 98
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLL-NATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 99 NIIVGSPdvgmllsksTARQKVEDLCLRCGIELDLD-------REIWQ----LSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:cd03290 98 NITFGSP---------FNKQRYKAVTDACSLQPDIDllpfgdqTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550121285 168 AVLTPQQSDQLFV--ILDGMRRQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
267-493 |
1.77e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLV---PDDRFREG 343
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVfqnPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 LISE---FGtAENLVLgwqrkPEYRRGPFLDRGkindLAQRKLEEFRIVAASTdlpverLSGGNAQRVILAREF-LNAKC 419
Cdd:PRK13644 94 TVEEdlaFG-PENLCL-----PPIEIRKRVDRA----LAEIGLEKYRHRSPKT------LSGGQGQCVALAGILtMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 420 LLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDlLRLCDRIAVIFKGKIVGTVRPE----ETTLLELGM 493
Cdd:PRK13644 158 LIF-DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPEnvlsDVSLQTLGL 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-215 |
1.96e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAG--KSTLSACLYGyyrADSGviRFKGQVAELNSPADALRLG 80
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAG--RRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGmVHQHFVL--VENFTVLENI-IVGSpdvGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:NF000106 87 IG-*HRPVR*grRESFSGRENLyMIGR---*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGR 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-215 |
2.01e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.52 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGIGMVHQHFVLVeNFTVLEN 99
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdIRTVT--RASLRRNIAVVFQDAGLF-NRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 100 IIVGSPDVG---MLLSKSTArqKVEDLCLRCgiELDLDREIW----QLSVGEQQWVEILKALYFGAELLILDEPTAVLTP 172
Cdd:PRK13657 429 IRVGRPDATdeeMRAAAERA--QAHDFIERK--PDGYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1550121285 173 QQSDQLFVILDGMrRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK13657 505 ETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
282-482 |
2.39e-11 |
|
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: 66.58 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 282 EILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVapTSREMLDRGVGLVPddrfreglisEFGTAENLVLGWQRK 361
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TNISDVHQNMGYCP----------QFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 362 PEYRRGPFLDRGKIndlaqRKLEEFRIVAASTDLPVERL----SGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEF 437
Cdd:TIGR01257 2034 YLYARLRGVPAEEI-----EKVANWSIQSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1550121285 438 VYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKG--KIVGTVR 482
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQCLGTIQ 2155
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
267-484 |
2.41e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRGVGLVPDDRFregL 344
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHH---L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLgwqrkpeyrrgPFLDRGKINDLAQRK----LEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCL 420
Cdd:PRK10908 91 LMDRTVYDNVAI-----------PLIIAGASGDDIRRRvsaaLDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 421 LLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPE 484
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
271-490 |
2.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVaptsremlDRGVGLvPDDRFREGLISEFgt 350
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--------DKKVKL-SDIRKKVGLVFQY-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 351 aenlvlgwqrkPEYRR-----------GPF---LDRGKINDlaqRKLEEFRIVAASTDL-----PVErLSGGNAQRVILA 411
Cdd:PRK13637 92 -----------PEYQLfeetiekdiafGPInlgLSEEEIEN---RVKRAMNIVGLDYEDykdksPFE-LSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 412 REF-LNAKCLLLaNQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTVRP--EE 485
Cdd:PRK13637 157 GVVaMEPKILIL-DEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCElqGTPREvfKE 235
|
....*
gi 1550121285 486 TTLLE 490
Cdd:PRK13637 236 VETLE 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-206 |
2.72e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGMVHQHFVLVENFTVLENI 100
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--SIKKDLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGspdvgmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFV 180
Cdd:PRK13540 96 LYD-------IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|....*.
gi 1550121285 181 ILDGMRRQGLSIILISHKLREVMQSD 206
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-215 |
2.90e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 35 LFGENGAGKSTLSACLYGY--YRadsGVIRFKGQvaELNS-PADALRLGIGMVHQHFVLVENfTVLENIIVGSPDVG--- 108
Cdd:PRK11174 381 LVGPSGAGKTSLLNALLGFlpYQ---GSLKINGI--ELRElDPESWRKHLSWVGQNPQLPHG-TLRDNVLLGNPDASdeq 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 109 --MLLSKSTARQKVEDLclrcgiELDLDREIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVLTpQQSDQLfvIL 182
Cdd:PRK11174 455 lqQALENAWVSEFLPLL------PQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD-AHSEQL--VM 525
|
170 180 190
....*....|....*....|....*....|....*
gi 1550121285 183 DGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK11174 526 QALNAasRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
247-485 |
3.38e-11 |
|
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: 65.56 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 247 SVAPGREVLVVDH-AVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvAPTSR 325
Cdd:COG4987 326 APAPGGPSLELEDvSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-RDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 326 EMLDRGVGLVPDDrfreglISEFGT--AENLVLGwqrKPEyrrgpfLDRGKINDLAQR-KLEEFriVAAST---DLPV-- 397
Cdd:COG4987 405 DDLRRRIAVVPQR------PHLFDTtlRENLRLA---RPD------ATDEELWAALERvGLGDW--LAALPdglDTWLge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 398 --ERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEkRAEGFAVFLASEELDDlLRLCDRIAVIFKG 475
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG-LERMDRILVLEDG 545
|
250
....*....|
gi 1550121285 476 KIVGTVRPEE 485
Cdd:COG4987 546 RIVEQGTHEE 555
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
267-478 |
3.94e-11 |
|
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: 65.63 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI--VAPTSremLDRGVGLVP-DDRFREG 343
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrqIDPAS---LRRQIGVVLqDVFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 LIsefgtAENLVLGwqrkpeyrrGPFLDRGKINDLAQR-KLEEFrIVA--ASTDLPV----ERLSGGNAQRVILAREFLN 416
Cdd:COG2274 564 TI-----RENITLG---------DPDATDEEIIEAARLaGLHDF-IEAlpMGYDTVVgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 417 AKCLLLANQPTRGLDVAASEFVYEKiLEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIV 478
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-215 |
4.69e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.67 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNSPA--DAL 77
Cdd:PRK10070 25 IEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvDIAKISDAElrEVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 78 RLGIGMVHQHFVLVENFTVLENIIVGSPDVGmlLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFG 157
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMELAG--INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 158 AELLILDEPTAVLTP----QQSDQLFVILDGMRRqglSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10070 183 PDILLMDEAFSALDPlirtEMQDELVKLQAKHQR---TIVFISHDLDEAMRiGDRIAIMQNGE 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
270-485 |
5.29e-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: 62.56 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvapTSREMLDR---GVGLVPDDR--FREgl 344
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKRarlGIGYLPQEAsiFRK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 iseFGTAENL--VLGWQRKPEYRRgpfldRGKINDLaqrkLEEFRIvAASTDLPVERLSGGNAQRVILAREF-LNAKCLL 421
Cdd:cd03218 90 ---LTVEENIlaVLEIRGLSKKER-----EEKLEEL----LEEFHI-THLRKSKASSLSGGERRRVEIARALaTNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 422 LaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03218 157 L-DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-214 |
5.36e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPAD--ALRLGIGMVHQHFVLVEN--F 94
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDPLASLNprM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLEniIVGSPdvgmL------LSKSTARQKVEDLCLRCGIELDL-DREIWQLSVGEQQWVEILKALYFGAELLILDEPT 167
Cdd:PRK15079 116 TIGE--IIAEP----LrtyhpkLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550121285 168 AVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-215 |
6.34e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADAlrlGIGMVH 85
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 86 QHFVLVENFTVLENIivgspDVGMLLS---KSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:PRK11000 82 QSYALYPHLSVAENM-----SFGLKLAgakKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 163 LDEPTAVLTPQQSDQLFV-ILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIeISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGR 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-215 |
1.08e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGY----YRADSGVIRFkgqvaelnSPAD 75
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRF--------DDID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRLGigMVHQHFVLVENFTvlenIIVGSPDVGMLLSKSTARQKVE-----------------------DLCLRCGIE-- 130
Cdd:PRK15093 75 LLRLS--PRERRKLVGHNVS----MIFQEPQSCLDPSERVGRQLMQnipgwtykgrwwqrfgwrkrraiELLHRVGIKdh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 131 LDLDREI-WQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQ-SDR 207
Cdd:PRK15093 149 KDAMRSFpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQwADK 228
|
....*...
gi 1550121285 208 VTILRKGK 215
Cdd:PRK15093 229 INVLYCGQ 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
264-459 |
1.25e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 264 GEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSR---EMLDRGVGLVPddRF 340
Cdd:PRK11629 18 GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQKLGFIY--QF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 341 REgLISEFGTAENLVLgwqrkpeyrrgPFLDRGKINDLAQRKLEEfrIVAA------STDLPVErLSGGNAQRVILAREF 414
Cdd:PRK11629 96 HH-LLPDFTALENVAM-----------PLLIGKKKPAEINSRALE--MLAAvglehrANHRPSE-LSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1550121285 415 LNAKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEEL 459
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDL 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-214 |
1.33e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADS-----GVIRFKGQ-VAELNSPADALR 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQHFVLVEnFTVLENIIVGSPDVGMllskstaRQKVE-DLCLRCGIEldlDREIW------------QLSVGEQ 145
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGW-------RPKLEiDDIVESALK---DADLWdeikhkihksalDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 146 QWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMR-RQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
267-478 |
1.37e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.22 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRGVGLVPDDrFRegL 344
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyLRRRIGVVFQD-FR--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENL-----VLGWQRKpEYRRgpfldrgKINDLaqrkLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKC 419
Cdd:COG2884 91 LPDRTVYENValplrVTGKSRK-EIRR-------RVREV----LDLVGLSDKAKALPHE-LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 420 LLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLAS--EELDDLLRLcdRIAVIFKGKIV 478
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAThdLELVDRMPK--RVLELEDGRLV 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
267-485 |
1.47e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE--AIVAPTSR--EMLDRGVGLVPddrfre 342
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlSHVPPYQRpiNMMFQSYALFP------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 glisEFGTAENLVLGWQRKPeyrrgpfLDRGKINDLAQRKLEEFRIVAASTDLPvERLSGGNAQRVILAREFLNAKCLLL 422
Cdd:PRK11607 105 ----HMTVEQNIAFGLKQDK-------LPKAEIASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 423 ANQPTRGLDVAASEFVYEK---ILEKraEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEvvdILER--VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-214 |
1.65e-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: 63.88 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVT--ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGyyraDSGVIRFKGQVAelnspADALRLG 80
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG----DTTVTSGDATVA-----GKSILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 81 IGMVHQHFVLVENFTVLENIIVGSPDVGMLLS----KSTARQKVEDLCLRC-GIELDLDREIWQLSVGEQQWVEILKALY 155
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIDDLLTGREHLYLYARlrgvPAEEIEKVANWSIQSlGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 156 FGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKG 214
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKG 2146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-214 |
2.24e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNspADALRLGIGMVHQHFVLVENfTVLENII 101
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpLTKLQ--LDSWRSRLAVVSQTPFLFSD-TVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGSPDVGMLLSKSTAR-QKVEDLCLRC--GIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQl 178
Cdd:PRK10789 411 LGRPDATQQEIEHVARlASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ- 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 1550121285 179 fvILDGMR--RQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:PRK10789 490 --ILHNLRqwGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
266-478 |
2.44e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 60.54 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGEEVLCdINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAptsremldrgvgLVPDDR-----F 340
Cdd:COG3840 11 YGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------LPPAERpvsmlF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 341 REG-LISEFGTAENLVLGwqRKPEYRRGPFlDRGKINDLAQR-KLEEF--RivaastdLPvERLSGGNAQRVILAREFLN 416
Cdd:COG3840 78 QENnLFPHLTVAQNIGLG--LRPGLKLTAE-QRAQVEQALERvGLAGLldR-------LP-GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 417 AKCLLLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
261-477 |
2.61e-10 |
|
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: 59.15 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 261 VAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeAIVAPTSREMLDRGVGLVP-DDR 339
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG-ADISQWDPNELGDHVGYLPqDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FREGLIsefgtAENLvlgwqrkpeyrrgpfldrgkindlaqrkleefrivaastdlpverLSGGNAQRVILAREFLNAKC 419
Cdd:cd03246 87 LFSGSI-----AENI---------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 420 LLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKI 477
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-215 |
2.82e-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: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGyyRADSGVIrFKGQVAELNSP--ADALRLGIGMVHQHFVLVENFTVLENI 100
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGT-TSGQILFNGQPrkPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGSPDVGMLLSKSTARQK-VEDLCLR-CGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQL 178
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKrVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550121285 179 FVILDGMRRQGLSIILISHKLREVMQS--DRVTILRKGK 215
Cdd:cd03234 183 VSTLSQLARRNRIVILTIHQPRSDLFRlfDRILLLSSGE 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
267-478 |
3.28e-10 |
|
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: 60.27 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTL-----SSGRFHLNGEAIVAP-TSREMLDRGVGLVpddrF 340
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdVDVLELRRRVGMV----F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 341 REGLISEFGTAENLVLGwQRKPEYRRGPFLDrgkinDLAQRKLEEfrivAASTD-----LPVERLSGGNAQRVILAREFL 415
Cdd:cd03260 88 QKPNPFPGSIYDNVAYG-LRLHGIKLKEELD-----ERVEEALRK----AALWDevkdrLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 416 NAKCLLLANQPTRGLDVAASEFVYEKILEKRAEgFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
271-477 |
3.36e-10 |
|
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: 60.11 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRGVGLVPDDrFRegLISEF 348
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKIGVVFQD-FR--LLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRKPEYRRgpfldrgkinDLAQRKLEEFRIVAAST---DLPVErLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:cd03292 94 NVYENVAFALEVTGVPPR----------EIRKRVPAALELVGLSHkhrALPAE-LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
269-482 |
3.60e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 60.06 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMldrgvglvpdDRFRE------ 342
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL----------ARLRRrhigfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 ----GLISEFGTAENLVLGWqrkpEYRRgpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAK 418
Cdd:COG1136 92 fqffNLLPELTALENVALPL----LLAG---VSRKERRERARELLERVGLGDRLDHRPSQ-LSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 419 CLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIVGTVR 482
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
270-478 |
4.19e-10 |
|
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: 59.85 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEaiVAPtsreMLDRGVGLVPDDRFREglisefg 349
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSS----LLGLGGGFNPELTGRE------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 taeN-----LVLGWQRKPEYRRGPFldrgkINDLAQrkLEEFRivaastDLPVERLSGGNAQR----VILArefLNAKCL 420
Cdd:cd03220 104 ---NiylngRLLGLSRKEIDEKIDE-----IIEFSE--LGDFI------DLPVKTYSSGMKARlafaIATA---LEPDIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 421 LLANQPTRGlDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03220 165 LIDEVLAVG-DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
8.53e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGvirfkgqvaEL---NSPADALRLGI 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG---------ELlagTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENFTVLENiivgspdVGMLLS---KSTARQKVEDLCLRcgieldlDREI-W--QLSVGEQQWVEILKALY 155
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDN-------VGLGLKgqwRDAALQALAAVGLA-------DRANeWpaALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 156 FGAELLILDEPTA---VLTPQQSDQLFVILdgMRRQGLSIILISHKLRE-VMQSDRVTILRKGK 215
Cdd:PRK11247 150 HRPGLLLLDEPLGaldALTRIEMQDLIESL--WQQHGFTVLLVTHDVSEaVAMADRVLLIEEGK 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
266-478 |
9.12e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGE-EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE-----AIVAPTSREMLDRGVGLVpddr 339
Cdd:COG4161 12 YGShQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsQKPSEKAIRLLRQKVGMV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FRE-GLISEFGTAENL------VLGwqrkpeyrrgpfLDRGKINDLAQRKLEEFRIVAASTDLPVeRLSGGNAQRVILAR 412
Cdd:COG4161 88 FQQyNLWPHLTVMENLieapckVLG------------LSKEQAREKAMKLLARLRLTDKADRFPL-HLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 413 EFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
260-459 |
1.03e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 260 AVAIGEwgEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGvrtlssgrfhlngeaIVAPTSREMLDRG---VGLVP 336
Cdd:PRK09544 11 SVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG---------------LVAPDEGVIKRNGklrIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 337 D----DRFREGLISEFgtaenlvlgWQRKPEYRRG---PFLDRGKINDLAQRkleefrivaastdlPVERLSGGNAQRVI 409
Cdd:PRK09544 74 QklylDTTLPLTVNRF---------LRLRPGTKKEdilPALKRVQAGHLIDA--------------PMQKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 410 LAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEEL 459
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
267-476 |
1.07e-09 |
|
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: 57.39 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRgVGLVPDDRFregLIS 346
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPF---LFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efGT-AENLvlgwqrkpeyrrgpfldrgkindlaqrkleefrivaastdlpverLSGGNAQRVILAREFL-NAKCLLLaN 424
Cdd:cd03228 90 --GTiRENI---------------------------------------------LSGGQRQRIAIARALLrDPPILIL-D 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 425 QPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGK 476
Cdd:cd03228 122 EATSALD-PETEALILEALRALAKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-215 |
1.47e-09 |
|
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: 60.60 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnsPADALRLGIGMVHQHFVLVeNFTVLENII 101
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdIRDV--TQASLRAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGSPDVGmllskstaRQKVEDlclrcGIEL-DLDREI------WQ---------LSVGEQQWVEILKALYFGAELLILDE 165
Cdd:COG5265 454 YGRPDAS--------EEEVEA-----AARAaQIHDFIeslpdgYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 166 PTAVL---TPQQsdqlfvILDGMRR--QGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:COG5265 521 ATSALdsrTERA------IQAALREvaRGRTTLVIAHRLSTIVDADEILVLEAGR 569
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-215 |
1.63e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGY--YRADSGVIRFKGQVAELNSPADALRLGI 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVenftvleniivgsPDVGMLLSKSTARQKV--------------EDLCLRCGIELDLDREIWQLSV----- 142
Cdd:PRK09580 81 FMAFQYPVEI-------------PGVSNQFFLQTALNAVrsyrgqepldrfdfQDLMEEKIALLKMPEDLLTRSVnvgfs 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 143 -GEQQWVEILKALYFGAELLILDEPTAVLtpqQSDQLFVILDG---MRRQGLSIILISHKLR--EVMQSDRVTILRKGK 215
Cdd:PRK09580 148 gGEKKRNDILQMAVLEPELCILDESDSGL---DIDALKIVADGvnsLRDGKRSFIIVTHYQRilDYIKPDYVHVLYQGR 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
267-485 |
1.64e-09 |
|
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: 58.02 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVA-PTSRemldRGVGLVpddrFRE-GL 344
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHK----RPVNTV----FQNyAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGWQRKpeyRRGPFLDRGKIND-LAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:cd03300 84 FPHLTVFENIAFGLRLK---KLPKAEIKERVAEaLDLVQLEGYA------NRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 424 NQPTRGLDVAASEFVYEKI--LEKRAeGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-215 |
1.66e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLgIGMVHQHFVLVENFTVLENIIV 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLFDQLLGPEGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 103 GSPDVGMLLSKSTARQKVEdlcLRCGIELDLdreiwQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSdQLF--V 180
Cdd:PRK10522 421 NPALVEKWLERLKMAHKLE---LEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR-REFyqV 491
|
170 180 190
....*....|....*....|....*....|....*
gi 1550121285 181 ILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-215 |
1.79e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 6 SVQNLTKRF----------GA-----------VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFK 64
Cdd:COG4586 3 EVENLSKTYrvyekepglkGAlkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 65 GQVAELNSPADALRlgIGMV-------HQHFVLVENFTVLENI--IvgspdvgmllSKSTARQKVEDLCLRCGIELDLDR 135
Cdd:COG4586 83 GYVPFKRRKEFARR--IGVVfgqrsqlWWDLPAIDSFRLLKAIyrI----------PDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 136 EIWQLSVGEQQWVEILKALYFGAELLILDEPTA---VLTpQQSDQLFvILDGMRRQGLSIILISHKLREVMQ-SDRVTIL 211
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIgldVVS-KEAIREF-LKEYNRERGTTILLTSHDMDDIEAlCDRVIVI 228
|
....
gi 1550121285 212 RKGK 215
Cdd:COG4586 229 DHGR 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-197 |
1.93e-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: 57.50 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaELNSPADALRLGIGMV 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--PLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HQHFVLVENFTVLENIIVGSPDvgmllsksTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHAD--------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLFVILDGMRRQGLSIILISH 197
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
131-208 |
3.25e-09 |
|
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: 56.18 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 131 LDLDREIWQLSVGEQQWVEILKALYFGAE--LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRV 208
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWI 158
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
271-485 |
3.41e-09 |
|
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: 57.35 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvapTSREMLDRGVGLVpddrFRE-GLISEFG 349
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV----FQHyALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRKPEYRRGPFLD-RGKINDLaqrkLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQPTR 428
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEiRAKVHEL----LKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 429 GLDVAASE----FVYEkiLEKRAEGFAVFLASEElDDLLRLCDRIAVIFKGKI--VGTvrPEE 485
Cdd:cd03296 166 ALDAKVRKelrrWLRR--LHDELHVTTVFVTHDQ-EEALEVADRVVVMNKGRIeqVGT--PDE 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-211 |
3.42e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnsPADALRLGI 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTL--KPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENfTVLENIIVgsPdvGMLLSKSTARQKVEDLCLRCGIELD-LDREIWQLSVGEQQWVEILKALYFGAEL 160
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIF--P--WQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 161 LILDEPTAVLTPQQSDQLFVILDGM-RRQGLSIILISHKLREVMQSDRVTIL 211
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-214 |
3.58e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 18 TANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnSPADALRLG-IGMVHQHFVLVENFTV 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALQKNlVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 97 LENIIVGSPDVG----MLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTP 172
Cdd:PRK15056 96 LVEDVVMMGRYGhmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1550121285 173 QQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
3.85e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYrADSGVI----RFKGQVAeLNS 72
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREI-LNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 73 PADAL-RL---GIGMVHQhfvlvENFTVLENII-VGSP--DVGML---LSKSTARQkvEDLCLRCGIELDLDREIWQL-- 140
Cdd:PRK09473 87 PEKELnKLraeQISMIFQ-----DPMTSLNPYMrVGEQlmEVLMLhkgMSKAEAFE--ESVRMLDAVKMPEARKRMKMyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 141 ---SVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVMQS-DRVTILRKGK 215
Cdd:PRK09473 160 hefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGIcDKVLVMYAGR 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
270-478 |
4.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI-----VAPTSREMLDRGVGLVpddrFRE-G 343
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAIKLRKEVGMV----FQQpN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 344 LISEFGTAENLVL-----GWQRKPEYRrgpfldrgKINDLAQRKLEEFRIVAASTDLPVERLSGGNAQRVILAREFLNAK 418
Cdd:PRK14246 101 PFPHLSIYDNIAYplkshGIKEKREIK--------KIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 419 CLLLANQPTRGLDVAASEFVyEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-81 |
4.36e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.02 E-value: 4.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 6 SVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRLGI 81
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdVATTPSRELAKRLAI 79
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-478 |
6.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS-----SGRFHLNGEAIVAPTSREmLDRGVGLV---PDDrf 340
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIE-LRRRVQMVfqiPNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 341 reglISEFGTAENLVLGWqrkpeyrrgpfldrgKINDLAQRKLEEF-RI------------VAASTDLPVERLSGGNAQR 407
Cdd:PRK14247 94 ----IPNLSIFENVALGL---------------KLNRLVKSKKELQeRVrwalekaqlwdeVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 408 VILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEgFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-215 |
6.39e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 30 GEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELNSPADALRlgIGMVHQHFVLVENFTVLENIIVGS-PDV 107
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpLESWSSKAFARK--VAYLPQQLPAAEGMTVRELVAIGRyPWH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 108 GMLLSKSTA-RQKVEDLCLRCGIELDLDREIWQLSVGEQQ--WVEILKALyfGAELLILDEPTAVL-TPQQSDQLFVILD 183
Cdd:PRK10575 115 GALGRFGAAdREKVEEAISLVGLKPLAHRLVDSLSGGERQraWIAMLVAQ--DSRCLLLDEPTSALdIAHQVDVLALVHR 192
|
170 180 190
....*....|....*....|....*....|...
gi 1550121285 184 GMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10575 193 LSQERGLTVIAVLHDINMAARyCDYLVALRGGE 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
267-485 |
7.53e-09 |
|
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: 56.54 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVApTSREMLDRGVGLVpddrFRE-GLI 345
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVELRRKIGYV----IQQiGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENLVL-----GWQRKpeyrrgpfldrgKIndlAQRKLEEFRIVaastDLP----VER----LSGGNAQRVILAR 412
Cdd:cd03295 88 PHMTVEENIALvpkllKWPKE------------KI---RERADELLALV----GLDpaefADRypheLSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 413 EFLNAKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
274-483 |
8.80e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 274 INFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaPTSREMLDRGVGLVPDDRFregLISEFGTAEN 353
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNI---LFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 354 LVLGWQRKpeyrrgpfldrGKINDLAQRKLEEfriVAASTDLPVER------LSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:TIGR01257 1024 ILFYAQLK-----------GRSWEEAQLEMEA---MLEDTGLHHKRneeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 428 RGLDVAASEFVYEKILEKRAeGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRP 483
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
267-485 |
1.05e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.96 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE--AIVAPTSremLDRGVGLVpddrFREGL 344
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAW---LRRQVGVV----LQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGwqrkpeyrrGPFLDRGKINDLAQ--------RKLEEF--RIVAastdlpvER---LSGGNAQRVILA 411
Cdd:cd03252 87 LFNRSIRDNIALA---------DPGMSMERVIEAAKlagahdfiSELPEGydTIVG-------EQgagLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 412 REFLNAKCLLLANQPTRGLDVaASEFVYEKILEKRAEGFAVFLASEELDDLLRlCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03252 151 RALIHNPRILIFDEATSALDY-ESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
273-486 |
1.08e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 57.03 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREML---DRGVGLVpddrFREG-LISEF 348
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpphRRRIGYV----FQEArLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRKPEYRRGPFLDR-----GkINDLAQRKleefrivaastdlpVERLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEvvellG-IGHLLDRR--------------PATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 424 NQPTRGLDVAASefvyEKI---LEKRAEGFA--VFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEET 486
Cdd:COG4148 158 DEPLAALDLARK----AEIlpyLERLRDELDipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-215 |
1.10e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFG-----------AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAEL 70
Cdd:PRK10261 311 EPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 71 NSPA--DALRLGIGMVHQ--HFVLVENFTVLENIIvgSP-DVGMLLSKSTARQKVEDLCLRCGIeldLDREIW----QLS 141
Cdd:PRK10261 391 LSPGklQALRRDIQFIFQdpYASLDPRQTVGDSIM--EPlRVHGLLPGKAAAARVAWLLERVGL---LPEHAWryphEFS 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 142 VGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIInLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQ 541
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-215 |
1.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGViRFKGQV----AELNSPADAL--R 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVllggRSIFNYRDVLefR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 79 LGIGMVHQH---FVLvenfTVLENIIVGSPDVGMLLSKS---TARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILK 152
Cdd:PRK14271 101 RRVGMLFQRpnpFPM----SIMDNVLAGVRAHKLVPRKEfrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 153 ALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQgLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDRAALFFDGR 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
270-478 |
1.14e-08 |
|
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: 55.28 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIaENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAptSREMLDRGVGLVPDD-RFREGLisef 348
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRRIGYLPQEfGVYPNF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 gTAENLV--LGWQRKPEYRRgpfLDRGKINDLAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:cd03264 88 -TVREFLdyIAWLKGIPSKE---VKARVDEVLELVNLGDRA------KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 427 TRGLDVaASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03264 158 TAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-203 |
1.58e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelNSPA------ 74
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE----NIPAmsrsrl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRLGIGMVHQHFVLVENFTVLENIIVGSPDVGML---LSKSTARQKVEDLCLRCGIELDLDreiwQLSVGEQQWVEIL 151
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLpapLLHSTVMMKLEAVGLRGAAKLMPS----ELSGGMARRAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 152 KALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQ-GLSIILISHKLREVM 203
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVL 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
273-482 |
1.84e-08 |
|
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: 55.83 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGV---RTLSSGRFHLNGEAIVAPTSREMLD---RGVGLVPDD-------R 339
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELRKirgREIQMIFQDpmtslnpV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FREG-LISEfgtaenlVLgwqrkpEYRRGpfLDRGKINDLAQRKLEEFRIVAASTDL---PVErLSGGNAQRVILAREF- 414
Cdd:COG0444 103 MTVGdQIAE-------PL------RIHGG--LSKAEARERAIELLERVGLPDPERRLdryPHE-LSGGMRQRVMIARALa 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 415 LNAKcLLLANQPTRGLDVAasefVYEKILE-----KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTVR 482
Cdd:COG0444 167 LEPK-LLIADEPTTALDVT----IQAQILNllkdlQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVeeGPVE 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-215 |
1.91e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLTKRFG----AVTANDSVDLDVRKGEIHCLFGENGAGKSTLSAclygyyrADSGVIRFKGQVA----ELNSpAD 75
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSL-------AIMGLIDYPGRVMaeklEFNG-QD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 76 ALRLG-----------IGMVHQHFVLVEN------FTVLENIIVGSPDvgmllSKSTARQKVEDLCLRCGI---ELDLDR 135
Cdd:PRK11022 75 LQRISekerrnlvgaeVAMIFQDPMTSLNpcytvgFQIMEAIKVHQGG-----NKKTRRQRAIDLLNQVGIpdpASRLDV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 136 EIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLREVMQS-DRVTILRK 213
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIeLLLELQQKENMALVLITHDLALVAEAaHKIIVMYA 229
|
..
gi 1550121285 214 GK 215
Cdd:PRK11022 230 GQ 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
270-469 |
2.35e-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: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGR--FHLNGEAI--VAPTSREMLD---RGVGLVpddrfre 342
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVdlAQASPREILAlrrRTIGYV------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 gliSEF------GTAENLVLgwqrKPEYRRGpfLDRGKINDLAQRKLEEFRIvaastdlPvERL--------SGGNAQRV 408
Cdd:COG4778 99 ---SQFlrviprVSALDVVA----EPLLERG--VDREEARARARELLARLNL-------P-ERLwdlppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 409 ILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRI 469
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRV 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
2.66e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSAC------LYGYYRADsGVIRFKGQvaELNSP-- 73
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGK--NLYAPdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 74 -ADALRLGIGMVHQHfvlVENF--TVLENIIVGSPDVGM------LLSKSTaRQ-----KVEDLCLRCGIeldldreiwQ 139
Cdd:PRK14243 85 dPVEVRRRIGMVFQK---PNPFpkSIYDNIAYGARINGYkgdmdeLVERSL-RQaalwdEVKDKLKQSGL---------S 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 140 LSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQgLSIILISHKLRevmQSDRVT 209
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQ---QAARVS 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
270-485 |
2.66e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKEL---FEVLMGVR--TLSSGRFHLNGEAIVAPTSREMLDRGVGLVPDDRFREGL 344
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLvthFNGLIKSKygTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFgtaenlvlgwqrkPEYRR-----------GPF-LDRGKINdlaQRKLEEFRIVAASTDLP-VER----LSGGNAQR 407
Cdd:PRK13631 121 VFQF-------------PEYQLfkdtiekdimfGPVaLGVKKSE---AKKLAKFYLNKMGLDDSyLERspfgLSGGQKRR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 408 VILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
267-482 |
2.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM-LDRGVGLV---PDDRFRE 342
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkLRESVGMVfqdPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLISEFGTAENLVLGWQRKPEYRRgpfLDRGkindLAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLL 422
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKR---VDNA----LKRTGIEHLK------DKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 423 ANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTVR 482
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlqGNPK 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-208 |
3.05e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 56.76 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 131 LDLDREIWQLSVGEQQWVEILKALyfGAELL----ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD 206
Cdd:PRK00635 468 LTPERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLAD 545
|
..
gi 1550121285 207 RV 208
Cdd:PRK00635 546 RI 547
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-214 |
3.58e-08 |
|
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: 56.49 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNspADALRLGIGMVHQHFVLVENfTVLENI- 100
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIG--LHDLRFKITIIPQDPVLFSG-SLRMNLd 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 ---IVGSPDVGMLLSKSTARQKVEDLCLRCGIELDLDREiwQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDq 177
Cdd:TIGR00957 1382 pfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN- 1458
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550121285 178 lfVILDGMRRQ--GLSIILISHKLREVMQSDRVTILRKG 214
Cdd:TIGR00957 1459 --LIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKG 1495
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
261-478 |
4.35e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 261 VAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGrFHLNGEAIVAPTS----REMLD--RGVGL 334
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSifnyRDVLEfrRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 335 VpddrFREGLISEFGTAENLVLGwqrkpeYRRGPFLDRGKINDLAQRKLEEFRIVAASTDLPVE---RLSGGNAQRVILA 411
Cdd:PRK14271 106 L----FQRPNPFPMSIMDNVLAG------VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfRLSGGQQQLLCLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 412 REFLNAKCLLLANQPTRGLDVAASEFVyEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
273-491 |
4.42e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRgVGLVPDDRFREGLIsefgTAE 352
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDI----TVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVlgwqRKPEYRRGPFLDRgkindlaQRKLEEFRIVAAS-----TDLP---VERLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:PRK10253 100 ELV----ARGRYPHQPLFTR-------WRKEDEEAVTKAMqatgiTHLAdqsVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 425 QPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEETTLLEL 491
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
269-485 |
4.76e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRemlDRGVGLVpddrFRE-GLISE 347
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR---DRKVGFV----FQHyALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGWQRKPEYRRgpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:PRK10851 89 MTVFDNIAFGLTVLPRRER---PNAAAIKAKVTQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 428 RGLDvAASEFVYEKILEKRAEGF---AVFLASEElDDLLRLCDRIAVIFKGKI--VGTvrPEE 485
Cdd:PRK10851 165 GALD-AQVRKELRRWLRQLHEELkftSVFVTHDQ-EEAMEVADRVVVMSQGNIeqAGT--PDQ 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-214 |
5.13e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNspadalrlgigmvhqhfvlvENFTVLENI 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--------------------REASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 -IVGSPDVGM-LLSkstarqkvedlclRCGIEldlDREIW-----QLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQ 173
Cdd:COG2401 107 gRKGDFKDAVeLLN-------------AVGLS---DAVLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 174 QSDQL-FVILDGMRRQGLSIILISHK--LREVMQSDRVTILRKG 214
Cdd:COG2401 171 TAKRVaRNLQKLARRAGITLVVATHHydVIDDLQPDLLIFVGYG 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-215 |
5.16e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.18 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGA--VTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQ-VAELnsPADALRLGI 81
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTI--PLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQHFVLVENfTVLENIivgspDVgmlLSKSTARQKVEDLCLRCGIEldldreiwQLSVGEQQWVEILKALYFGAELL 161
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNL-----DP---FDEYSDEEIYGALRVSEGGL--------NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 162 ILDEPTAVLTpQQSDQLF--VILDGMrrQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:cd03369 148 VLDEATASID-YATDALIqkTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
237-485 |
5.84e-08 |
|
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: 53.59 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 237 HQVTKRVSDRsvapgrevlvvDHAVAIgewgeevLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNG 316
Cdd:COG4181 12 RGLTKTVGTG-----------AGELTI-------LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 317 EAIVAptsremLD---------RGVGLVpddrFR-EGLISEFgTA-ENLVLgwqrkpeyrrgPFLDRGKiNDLAQRKLEE 385
Cdd:COG4181 74 QDLFA------LDedararlraRHVGFV----FQsFQLLPTL-TAlENVML-----------PLELAGR-RDARARARAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 386 FRIVAAS---TDLPVErLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDD 461
Cdd:COG4181 131 LERVGLGhrlDHYPAQ-LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPAL 209
|
250 260
....*....|....*....|....
gi 1550121285 462 LLRlCDRIAVIFKGKIVGTVRPEE 485
Cdd:COG4181 210 AAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
271-475 |
6.25e-08 |
|
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: 53.62 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLD-RGVGLVPDDRFREGLisefG 349
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVfQNYSLLPWLTVRENI----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRKPEyrrgpfldrgkindlaQRKLEEFRI----VAASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:TIGR01184 77 LAVDRVLPDLSKSE----------------RRAIVEEHIalvgLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKG 475
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
270-478 |
6.34e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 53.43 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMG-VRTLS--SGRFHLNGEaivaPTSREMLDRGVGLVP-DDRFREGL- 344
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGttSGQILFNGQ----PRKPDQFQKCVAYVRqDDILLPGLt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGWQRKPEYRRGPFLDRGKINDLAQRKLEEFRIVAastdlpverLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG---------ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 425 QPTRGLDvAASEFVYEKILEKRAEGFAVFLAS--EELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03234 169 EPTSGLD-SFTALNLVSTLSQLARRNRIVILTihQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-215 |
6.90e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 22 SVDLDVRKGEIHCLFGENGAGKSTLSACLY-------GYYRADSGVIRFKGQVAELNspADALRLGIGMVHQHFVLVENF 94
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQID--AIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLENIivGSPDVGMLLSKSTARQKVEDLCLRcgiELDLDREIW--------QLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:PRK14246 106 SIYDNI--AYPLKSHGIKEKREIKKIVEECLR---KVGLWKEVYdrlnspasQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1550121285 167 TAVLTPQQSDQLFVILDGMRRQgLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGE 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
270-478 |
6.97e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.55 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEaiVAPtsreMLDRGVGLVPddrfreglisEFG 349
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--VSA----LLELGAGFHP----------ELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAEN-----LVLGWQRKpEYRRgpFLDrgKINDLAQrkLEEFRivaastDLPVERLSGGnaQRVILAreF-----LNAKC 419
Cdd:COG1134 105 GRENiylngRLLGLSRK-EIDE--KFD--EIVEFAE--LGDFI------DQPVKTYSSG--MRARLA--FavataVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 420 LL----LAnqptrgldVAASEF---VYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG1134 168 LLvdevLA--------VGDAAFqkkCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
8.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSAC------LYGYYRADSGVIRFKGQVAELNSPA 74
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 75 DALRLGIGMVHQHFVLVENFTVLENIIVGSPDVGMLLSKSTARQKVE----DLCLRCGIELDLDREIWQLSVGEQQWVEI 150
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 151 LKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQgLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARvSDYVAFLYLGK 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
274-477 |
9.03e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.48 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 274 INFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSgrfhlngeaivAPTSR-EMLDRGVG----LVPDDR--------- 339
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-----------SAGSHiELLGRTVQregrLARDIRksrantgyi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FRE-GLISEFGTAENLVLGWQRKPEYRRGPFldRGKINDLAQRKLEEFRIVAAS--TDLPVERLSGGNAQRVILAREFLN 416
Cdd:PRK09984 92 FQQfNLVNRLSVLENVLIGALGSTPFWRTCF--SWFTREQKQRALQALTRVGMVhfAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 417 AKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
269-485 |
9.89e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.27 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLV---PDDRFREGLI 345
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVfqnPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SE---FGTAeNLVLGwQRKPEYRRGPFLDRGKINDLAQRkleefrivaastdLPvERLSGGNAQRVILAREFLNAKCLLL 422
Cdd:PRK13652 97 EQdiaFGPI-NLGLD-EETVAHRVSSALHMLGLEELRDR-------------VP-HHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 423 ANQPTRGLDV--AASEFVYEKILEKRAeGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13652 161 LDEPTAGLDPqgVKELIDFLNDLPETY-GMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-215 |
1.18e-07 |
|
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: 54.57 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELnsPADAlrlgigmvhqhfvLVENFTVLENI 100
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQA-------------WIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGSPdvgmlLSKSTARQKVEDLCLRCGIEL--DLDR-EIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVLTPQ 173
Cdd:TIGR00957 720 LFGKA-----LNEKYYQQVLEACALLPDLEIlpSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 174 QSDQLF--VILDGMRRQGLSIILISHKLREVMQSDRVTILRKGK 215
Cdd:TIGR00957 795 VGKHIFehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-215 |
1.28e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 30 GEIHCLFGENGAGKSTLSACLYGYYRADSgvirFKGQV-AELNSPADALRLGIGMVHQHFVLVENFTVLENIIVGSPdvg 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTIlANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 109 MLLSKSTARQK--------VEDLCL-RCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF 179
Cdd:PLN03211 167 LRLPKSLTKQEkilvaesvISELGLtKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 1550121285 180 VILDGMRRQGLSIILISHK--LREVMQSDRVTILRKGK 215
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGR 284
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
269-478 |
2.11e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.94 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI---VAPTSREM--LDRGVGLVpddrFRE- 342
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIreLRRNVGMV----FQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLISEFGTAENL------VLGWQRKPEYRRG-PFLDRGKINDLAQRkleefrivaastdLPVErLSGGNAQRVILAREFL 415
Cdd:PRK11124 92 NLWPHLTVQQNLieapcrVLGLSKDQALARAeKLLERLRLKPYADR-------------FPLH-LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 416 NAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-478 |
2.12e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRF----GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVI--------RFKGQVAE 69
Cdd:PRK10261 10 RDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 70 LNSPADALRLG-----IGMVHQHFVLVEN--FTVLENIiVGSPDVGMLLSKSTARQKVEDLCLRCGI---ELDLDREIWQ 139
Cdd:PRK10261 90 LSEQSAAQMRHvrgadMAMIFQEPMTSLNpvFTVGEQI-AESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 140 LSVGEQQWVEILKALYFGAELLILDEPTAVL--TPQ-QSDQLFVILDgmRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALdvTIQaQILQLIKVLQ--KEMSMGVIFITHDMGVVAEiADRVLVMYQGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 216 VVATVET-----------ATTTAESITAL--MVGHQVTKR---------------VSDRSVAPGREVLVVDHAVA----- 262
Cdd:PRK10261 247 AVETGSVeqifhapqhpyTRALLAAVPQLgaMKGLDYPRRfplislehpakqeppIEQDTVVDGEPILQVRNLVTrfplr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 263 ---IGEWGEEV--LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI--VAPTSREMLDRGVGLV 335
Cdd:PRK10261 327 sglLNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtLSPGKLQALRRDIQFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 336 PDDRF-----REGL---ISEFGTAENLVLGwqRKPEYRRGPFLDR-GKINDLAQRKLEEFrivaastdlpverlSGGNAQ 406
Cdd:PRK10261 407 FQDPYasldpRQTVgdsIMEPLRVHGLLPG--KAAAARVAWLLERvGLLPEHAWRYPHEF--------------SGGQRQ 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 407 RVILAREF-LNAKcLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK10261 471 RICIARALaLNPK-VIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-148 |
2.13e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRF-GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADalRlGIGM 83
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--R-DIAM 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 84 VHQHFVLVENFTVLENIIVGSPDVGMllSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWV 148
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGM--PKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRV 143
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
273-485 |
3.01e-07 |
|
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: 51.88 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLD---RGVGLVpddrFRE-GLISEF 348
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMV----FQSfALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQ-----RKPEYRRgpfldrgkindlAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:cd03294 118 TVLENVAFGLEvqgvpRAEREER------------AAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 424 NQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-199 |
3.84e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.60 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKSTLSACLYGYYRADSG----------VIR-FKGqvAELNSPADALRLG-IGMVHQhfvlVENF 94
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeILDeFRG--SELQNYFTKLLEGdVKVIVK----PQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 95 TVLENIIVGSpdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQ 174
Cdd:cd03236 97 DLIPKAVKGK--VGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*
gi 1550121285 175 SDQLFVILDGMRRQGLSIILISHKL 199
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-167 |
4.10e-07 |
|
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: 52.63 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAelnspadalrlgI 81
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK------------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQ-HFVLVENFTVLENIIVGSpDVgMLLSKST--ARQKVEDLCLRCGielDLDREIWQLSVGEQQWVEILKALYFGA 158
Cdd:TIGR03719 388 AYVDQsRDALDPNKTVWEEISGGL-DI-IKLGKREipSRAYVGRFNFKGS---DQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
....*....
gi 1550121285 159 ELLILDEPT 167
Cdd:TIGR03719 463 NVLLLDEPT 471
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
267-457 |
4.25e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.24 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSremlDRGVglVPDDrfrEGLIS 346
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGV--VFQN---EGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGWQRkpeyrRGpfLDRGKINDLAQRKLEEFRIVAASTDlPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:PRK11248 84 WRNVQDNVAFGLQL-----AG--VEKMQRLEIAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1550121285 427 TRGLDVAASEFVYEKILEKRAEGF------------AVFLASE 457
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGkqvllithdieeAVFMATE 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-197 |
4.93e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.26 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALR-LGi 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 gmvHQHFvLVENFTVLENI-----IVGSPDVGMllskstarqkVEDLClRCGIELDLDREIWQLSVGEQQWVEILKALYF 156
Cdd:PRK13539 80 ---HRNA-MKPALTVAENLefwaaFLGGEELDI----------AAALE-AVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1550121285 157 GAELLILDEPTAVLTPqQSDQLFV-ILDGMRRQGLSIILISH 197
Cdd:PRK13539 145 NRPIWILDEPTAALDA-AAVALFAeLIRAHLAQGGIVIAATH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
267-431 |
5.60e-07 |
|
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: 50.22 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM-LDRGVGLVpddrFRE-GL 344
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINeLRQKVGMV----FQQfNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVLGwqrkPEYRRGpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREF-LNAKCLLLa 423
Cdd:cd03262 88 FPHLTVLENITLA----PIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALaMNPKVMLF- 159
|
....*...
gi 1550121285 424 NQPTRGLD 431
Cdd:cd03262 160 DEPTSALD 167
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
269-471 |
6.03e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 50.86 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPtsremlDRGVGLVP-DDR---FRegl 344
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------GPDRGVVFqEPAllpWL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 isefgTA-ENLVLGwqrkPEYRRgpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:COG1116 96 -----TVlDNVALG----LELRG---VPKAERRERARELLELVGLAGFEDAYPHQ-LSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1550121285 424 NQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAV 471
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-197 |
6.09e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 28 RKGEIHCLFGENGAGKSTLSACLYGYYRAD---SGVIRFKGQVAElnspADALRLGIGMVHQHFVLVENFTVLENIIVGS 104
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 105 pdvgML-----LSKSTARQKVEDLCLRCGIELDLDREIWQ------LSVGEQqwveilKALYFGAEL------LILDEPT 167
Cdd:TIGR00955 125 ----HLrmprrVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGER------KRLAFASELltdpplLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 1550121285 168 AVLTPQQSDQLFVILDGMRRQGLSIILISH 197
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
270-471 |
6.65e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 50.63 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSremlDRGVglVPDDrfrEGLISEFG 349
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----DRGV--VFQK---DALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRkpeyrRGpfLDRGKINDLAQRKLeefRIV--AASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQPT 427
Cdd:COG4525 93 VLDNVAFGLRL-----RG--VPKAERRARAEELL---ALVglADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1550121285 428 RGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAV 471
Cdd:COG4525 163 GALDALTREQMQELLLDvWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
256-478 |
7.97e-07 |
|
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: 49.83 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 256 VVDHAVAIGewGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVR--TLSSGRFHLNGEAIVAptsremldrgvg 333
Cdd:cd03217 3 IKDLHVSVG--GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 334 LVPDDRFREGLIsefgtaenlvLGWQRKPEYrrgPFLdrgkindlaqrKLEEF-RIVAastdlpvERLSGGNAQRV-ILA 411
Cdd:cd03217 69 LPPEERARLGIF----------LAFQYPPEI---PGV-----------KNADFlRYVN-------EGFSGGEKKRNeILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 412 REFLNAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLAS--EELDDLLRlCDRIAVIFKGKIV 478
Cdd:cd03217 118 LLLLEPDLAIL-DEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYIK-PDRVHVLYDGRIV 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
267-492 |
8.04e-07 |
|
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: 50.31 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLVPDDRFregLIS 346
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVF---LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efGT-AENLVLGwqrKPEYRRGPFLDRGKINDLAQ--RKLEEfrivaaSTDLPVE----RLSGGNAQRVILAREFLNAKC 419
Cdd:cd03251 90 --DTvAENIAYG---RPGATREEVEEAARAANAHEfiMELPE------GYDTVIGergvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 420 LLLANQPTRGLDVaASEFVYEKILEKRAEGFAVFLASEELDDlLRLCDRIAVIFKGKIVGTVRPEEttLLELG 492
Cdd:cd03251 159 ILILDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLST-IENADRIVVLEDGKIVERGTHEE--LLAQG 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
275-478 |
1.09e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.58 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 275 NFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGE--AIVAPTSR--EMLdrgvglvpddrFRE-GLISEFG 349
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRpvSML-----------FQEnNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGwqrkpeyrrgpfLDRG-KINDLAQRKLEEFRIVAASTD----LPVErLSGGNAQRVILAREFLNAKCLLLAN 424
Cdd:PRK10771 88 VAQNIGLG------------LNPGlKLNAAQREKLHAIARQMGIEDllarLPGQ-LSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 425 QPTRGLDVA-ASEFV--YEKILEKRaeGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK10771 155 EPFSALDPAlRQEMLtlVSQVCQER--QLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
399-478 |
1.13e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.38 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 399 RLSGGNAQRVILAREFLNAKCLLLANQPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELDDLLRlCDRIAVIFKGKIV 478
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLD-AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
245-443 |
1.19e-06 |
|
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: 51.21 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 245 DRSVAPGREVLVVDHAVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAiVAPTS 324
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-VSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 325 REMLDRGVGLVPDDrfreglISEFGTA--ENLVLGWQRKPEYRRGPFLDRGKINDLAQRKLEefrivAASTDLpVE---R 399
Cdd:TIGR02868 404 QDEVRRRVSVCAQD------AHLFDTTvrENLRLARPDATDEELWAALERVGLADWLRALPD-----GLDTVL-GEggaR 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 400 LSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKIL 443
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-215 |
1.24e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 8 QNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNSPADALRlgIGMVHQ 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARR--IGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 87 HFVLVENFTVLENIIVGSPDVGMLLSKstARQKVEDLCLRC----GIELDLDREIWQLSVGEQQWVEILKALYFGAELLI 162
Cdd:PRK10253 89 NATTPGDITVQELVARGRYPHQPLFTR--WRKEDEEAVTKAmqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 163 LDEPTAVL-TPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10253 167 LDEPTTWLdISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGK 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
267-485 |
1.49e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.69 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDR-GVGLV---PDDRFRE 342
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRkTVGIVfqnPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLISE---FGTAeNLVLgwqrkpeyrrgpfldrgKINDLAQRKLEEFRIVAAS--TDLPVERLSGGNAQRV----ILAre 413
Cdd:PRK13639 94 PTVEEdvaFGPL-NLGL-----------------SKEEVEKRVKEALKAVGMEgfENKPPHHLSGGQKKRVaiagILA-- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 414 fLNAKCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13639 154 -MKPEIIVL-DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-197 |
1.61e-06 |
|
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: 47.83 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 5 LSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGqvaelnspadalRLGIGMV 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 85 HqhfvlvenftvleniivgspdvgmllskstarqkvedlclrcgieldldreiwQLSVGEQQWVEILKALYFGAELLILD 164
Cdd:cd03221 69 E-----------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|...
gi 1550121285 165 EPTAVLTPQQSDQLfviLDGMRRQGLSIILISH 197
Cdd:cd03221 96 EPTNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
266-510 |
1.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.73 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLnGEAIVAPTSREM----LDRGVGLVpdDRFR 341
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKeikpVRKKVGVV--FQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 342 EGLISEFGTAENLVLGWQRKPeyrrgpfLDRGKINDLAQRKLEefrIVAASTDL----PVErLSGGNAQRVILAREFLNA 417
Cdd:PRK13643 94 ESQLFEETVLKDVAFGPQNFG-------IPKEKAEKIAAEKLE---MVGLADEFweksPFE-LSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 418 KCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRP----EETTLLELGM 493
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPsdvfQEVDFLKAHE 242
|
250
....*....|....*..
gi 1550121285 494 MMAGNASNLGGQVNDFG 510
Cdd:PRK13643 243 LGVPKATHFADQLQKTG 259
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
264-486 |
1.94e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 264 GEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM--LDRgvglvpdDRF- 340
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqLRR-------EHFg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 341 ----REGLISEFGTAENLVL-----GWQRKPEYRRGpfldrgkiNDLAQRKLEEFRIvaastDLPVERLSGGNAQRVILA 411
Cdd:PRK10535 90 fifqRYHLLSHLTAAQNVEVpavyaGLERKQRLLRA--------QELLQRLGLEDRV-----EYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 412 REFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEElDDLLRLCDRIAVIFKGKIVGTVRPEET 486
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEK 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
273-482 |
2.38e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGV-----RTLSSGRFhlNGEAIVAPTSREMldrgvglvpdDRFReglise 347
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaangRIGGSATF--NGREILNLPEKEL----------NKLR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 fgtAENLVLGWQrKPEYRRGPFLDRG----------KINDLAQRKLEEFRIVAAsTDLPVER---------LSGGNAQRV 408
Cdd:PRK09473 96 ---AEQISMIFQ-DPMTSLNPYMRVGeqlmevlmlhKGMSKAEAFEESVRMLDA-VKMPEARkrmkmypheFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 409 ILAREFLNAKCLLLANQPTRGLDVAasefVYEKILE-----KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTV 481
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVT----VQAQIMTllnelKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMeyGNA 246
|
.
gi 1550121285 482 R 482
Cdd:PRK09473 247 R 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
273-478 |
2.46e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGrfhlngEAIVAptsremldrgvGLVPDDRfREGLISEFGtae 352
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG------EVRVL-----------GYVPFKR-RKEFARRIG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 nLVLGwQR-----------------------KPEYRRgpfldrgKINDLAQR-KLEEFrivaasTDLPVERLSGGnaQR- 407
Cdd:COG4586 99 -VVFG-QRsqlwwdlpaidsfrllkaiyripDAEYKK-------RLDELVELlDLGEL------LDTPVRQLSLG--QRm 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 408 ---VILAreFLNAKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:COG4586 162 rceLAAA--LLHRPKILFLDEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-67 |
2.51e-06 |
|
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: 50.18 E-value: 2.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1550121285 23 VDLDVRKGEIhcLF--GENGAGKSTLSACLYGYYRADSGVIRFKGQV 67
Cdd:COG4615 351 IDLTIRRGEL--VFivGGNGSGKSTLAKLLTGLYRPESGEILLDGQP 395
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
270-510 |
3.03e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.33 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvapTSREMLDRGVGLVpddrFRE-GLISEF 348
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICMV----FQSyALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQrkpeyrrgpFLDRGKiNDLAQRKLEEFRIV--AASTDLPVERLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:PRK11432 94 SLGENVGYGLK---------MLGVPK-EERKQRVKEALELVdlAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 427 TRGLDVAASEFVYEKI--LEKR------------AEGFAVflaseelddllrlCDRIAVIFKGKIVGTVRPEETTLLELG 492
Cdd:PRK11432 164 LSNLDANLRRSMREKIreLQQQfnitslyvthdqSEAFAV-------------SDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
250 260
....*....|....*....|....*.
gi 1550121285 493 MMMA---GNASNL-----GGQVNDFG 510
Cdd:PRK11432 231 RFMAsfmGDANIFpatlsGDYVDIYG 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
264-478 |
3.50e-06 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 47.55 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 264 GEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS--SGRFHLNGEaivaPTSREMLDRGVGLVPDDrfr 341
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGR----PLDKRSFRKIIGYVPQD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 342 EGLISEFGTAENLvlgwqrkpeyrrgpfldrgkindlaqrkleefRIVAAstdlpVERLSGGNAQRVILAREFLNAKCLL 421
Cdd:cd03213 91 DILHPTLTVRETL--------------------------------MFAAK-----LRGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 422 LANQPTRGLDvAASEFVYEKILEKRAEGFAVFLAS--EELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03213 134 FLDEPTSGLD-SSSALQVMSLLRRLADTGRTIICSihQPSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
396-485 |
3.89e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 396 PVERLSGGNAQRVILAREFLN-------AKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDR 468
Cdd:PRK03695 123 SVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADR 202
|
90
....*....|....*..
gi 1550121285 469 IAVIFKGKIVGTVRPEE 485
Cdd:PRK03695 203 VWLLKQGKLLASGRRDE 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
269-485 |
4.57e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.17 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDR-GVGLVpddrFRE-GLIS 346
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqEAGMV----FQQfYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVLGwqrkPEYRRGpfLDRGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQP 426
Cdd:PRK09493 91 HLTALENVMFG----PLRVRG--ASKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 427 TRGLDvaaSEFVYE--KILEKRA-EGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK09493 164 TSALD---PELRHEvlKVMQDLAeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
250-431 |
4.92e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 250 PGREVLVVDH---AVAIGEWGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSR- 325
Cdd:PRK10584 2 PAENIVEVHHlkkSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 326 --EMLDRGVGLVpddrFRE-GLISEFGTAENLVLgwqrkPEYRRGPflDRGKINDLAQRKLEEFRIVAASTDLPVErLSG 402
Cdd:PRK10584 82 raKLRAKHVGFV----FQSfMLIPTLNALENVEL-----PALLRGE--SSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSG 149
|
170 180
....*....|....*....|....*....
gi 1550121285 403 GNAQRVILAREFLNAKCLLLANQPTRGLD 431
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
270-478 |
5.35e-06 |
|
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: 47.25 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvapTSREMLDRGVGLV-------PDDRFRE 342
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMVfqnyalyPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLisefgtAENLVLGWQRKPEYRRgpfldrgKINDLAQR-KLEEFrivaasTDLPVERLSGGNAQRVILAREFLNAKCLL 421
Cdd:cd03301 92 NI------AFGLKLRKVPKDEIDE-------RVREVAELlQIEHL------LDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 422 LANQPTRGLDVAASEFVYEKI--LEKRAeGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELkrLQQRL-GTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
15-208 |
5.50e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.64 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 15 GAVTAN-DSVDLDVRKGEIHCLFGENGAGKSTLSAclygyyradsGVIRFKGQVAELNSPADALRLGIGMVHQHFV-LVE 92
Cdd:cd03270 5 GAREHNlKNVDVDIPRNKLVVITGVSGSGKSSLAF----------DTIYAEGQRRYVESLSAYARQFLGQMDKPDVdSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 93 NFT----VLENIIVGSP--DVG----------MLLSKSTARQKVEDLcLRCGIE-LDLDREIWQLSVGEQQWVEILKALy 155
Cdd:cd03270 75 GLSpaiaIDQKTTSRNPrsTVGtvteiydylrLLFARVGIRERLGFL-VDVGLGyLTLSRSAPTLSGGEAQRIRLATQI- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 156 fGAELL----ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRV 208
Cdd:cd03270 153 -GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-174 |
5.94e-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: 47.79 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 26 DVRKGEIHCLFGENGAGKSTLSACLYGYYRADSG-------VIRFKGQVAELNSPadalrlgigmvhqhfVLVENFtvLE 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldTVSYKPQYIKADYE---------------GTVRDL--LS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 99 NIIvgsPDVGmllsksTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQ 174
Cdd:cd03237 84 SIT---KDFY------THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
372-477 |
7.45e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 372 RGKINDLAQRKLEEFRIVAASTDLPVErLSGGNAQRVILAREFLNAKCLLLANQPTRGLDvAASEFVYEKILEK--RAEG 449
Cdd:PRK11247 107 KGQWRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALD-ALTRIEMQDLIESlwQQHG 184
|
90 100
....*....|....*....|....*...
gi 1550121285 450 FAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:PRK11247 185 FTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-62 |
7.92e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 7.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 3 NLLSVQNLTKRFGAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIR 62
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
270-492 |
9.51e-06 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 47.43 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLV---PDDRFREGLIS 346
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKVGMVfqnPDNQFVGATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 E---FGTaENLvlGWQRkPEYRRgpfldrgKIND-LAQRKLEEFRivaastDLPVERLSGGNAQRV----ILArefLNAK 418
Cdd:TIGR04520 97 DdvaFGL-ENL--GVPR-EEMRK-------RVDEaLKLVGMEDFR------DREPHLLSGGQKQRVaiagVLA---MRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 419 CLLLaNQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLrLCDRIAVIFKGKIVGTVRPEE-----TTLLELG 492
Cdd:TIGR04520 157 IIIL-DEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREifsqvELLKEIG 234
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
261-485 |
1.06e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 47.03 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 261 VAIGewGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM-LDRGVglVPDDr 339
Cdd:COG4559 9 VRLG--GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAV--LPQH- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 fregliSEFG---TAENLV-LGwqrkpeyRRGPFLDRGKINDLAQRKLEEfrivaasTDLP--VER----LSGGNAQRVI 409
Cdd:COG4559 84 ------SSLAfpfTVEEVVaLG-------RAPHGSSAAQDRQIVREALAL-------VGLAhlAGRsyqtLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 410 LAR--------EFLNAKCLLLaNQPTRGLDVA--------ASEFVyekilekrAEGFAVFLAseeLDDL---LRLCDRIA 470
Cdd:COG4559 144 LARvlaqlwepVDGGPRWLFL-DEPTSALDLAhqhavlrlARQLA--------RRGGGVVAV---LHDLnlaAQYADRIL 211
|
250
....*....|....*
gi 1550121285 471 VIFKGKIVGTVRPEE 485
Cdd:COG4559 212 LLHQGRLVAQGTPEE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
269-481 |
1.36e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.10 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRE--MLDRGVGLVpddrFRE-GLI 345
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIGMI----FQHfNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 SEFGTAENLVL-----GWQRKPEYRR-GPFLDRGKINDLAQRkleefrivaastdLPVErLSGGNAQRVILAREFLNAKC 419
Cdd:PRK11153 95 SSRTVFDNVALplelaGTPKAEIKARvTELLELVGLSDKADR-------------YPAQ-LSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 420 LLLANQPTRGLDVAASEfvyeKILEKRAE-----GFAVFLASEELDDLLRLCDRIAVIFKGKIV--GTV 481
Cdd:PRK11153 161 VLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVeqGTV 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
399-485 |
1.62e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 399 RLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
....*...
gi 1550121285 478 VGTVRPEE 485
Cdd:PRK11022 233 VETGKAHD 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
274-485 |
1.91e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 274 INFTIAENEILGLAGVAGNGQKELFEVLMGVRT----LSSGRFHLNGEAIVAPTSRE---MLDRGVGLV---------PD 337
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRErrkLVGHNVSMIfqepqscldPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 338 DRFREGLISEfgtaenlVLGWQRK-PEYRRGPFLDRGKINDLAQRKLEEFRIVAAStdLPVErLSGGNAQRVILAREFLN 416
Cdd:PRK15093 106 ERVGRQLMQN-------IPGWTYKgRWWQRFGWRKRRAIELLHRVGIKDHKDAMRS--FPYE-LTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 417 AKCLLLANQPTRGLDVAASEFVYeKILEK--RAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIF-RLLTRlnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
268-485 |
1.95e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.54 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 268 EEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI-VAPTSREMLDRGVGLV---PDDR-FRE 342
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdYSKRGLLALRQQVATVfqdPEQQiFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 GLISEFG-TAENLVLgwqrkPEyrrgpfldrgkiNDLAQRKLEEFRIVAAS--TDLPVERLSGGNAQRVILAREF-LNAK 418
Cdd:PRK13638 94 DIDSDIAfSLRNLGV-----PE------------AEITRRVDEALTLVDAQhfRHQPIQCLSHGQKKRVAIAGALvLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 419 CLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13638 157 YLLL-DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
270-477 |
2.14e-05 |
|
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: 45.92 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVApTSREMLDRGVGLVPddrfREGLISEFG 349
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ-YEHKYLHSKVSLVG----QEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRKPEyrrgpfldrGKINDLAQRKLEEFRIVAASTDLPVE------RLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:cd03248 104 LQDNIAYGLQSCSF---------ECVKEAAQKAHAHSFISELASGYDTEvgekgsQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 424 NQPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELDDLLRlCDRIAVIFKGKI 477
Cdd:cd03248 175 DEATSALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
267-456 |
2.28e-05 |
|
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: 45.56 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaPTSREMLDRGVGLVPDDRFREGLIS 346
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 efgTAENLVLgWQrkpeyrrgPFLDRGKIND-LAQRKLEEFRivaastDLPVERLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:cd03231 90 ---VLENLRF-WH--------ADHSDEQVEEaLARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|.
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAEGFAVFLAS 456
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTT 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
37-215 |
2.93e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 37 GENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNspADALRLGIGMVHQHFVLVENfTVLENIIVGSPDVGMLLSKST 115
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFG--LTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHNDADLWEAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 116 ARQKVEDLCLRCgiELDLDREIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVLTpQQSDQLfvILDGMRRQ--G 189
Cdd:PLN03232 1346 ERAHIKDVIDRN--PFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSL--IQRTIREEfkS 1420
|
170 180
....*....|....*....|....*.
gi 1550121285 190 LSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
270-485 |
4.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 45.37 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLV---PDDRFReGLIS 346
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKIGIIfqnPDNQFI-GATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLvlgwqrkpEYRRgpfLDRGK----INDLAQR-KLEEFrivaasTDLPVERLSGGNAQRV----ILArefLNA 417
Cdd:PRK13632 102 EDDIAFGL--------ENKK---VPPKKmkdiIDDLAKKvGMEDY------LDKEPQNLSGGQKQRVaiasVLA---LNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 418 KCLLLaNQPTRGLDVAASEFVYEKILEKRAEGFAVFLA-SEELDDLLrLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13632 162 EIIIF-DESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-214 |
4.66e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTL-SACLYGYYRADSGVIRFKGQVAELnspadalrlgigmvhQHFVLVENFTVLENII 101
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRGSVAYV---------------PQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 102 VGS---PDVGMLLSKSTARQkvEDLCLRCGIEL-DLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQ 177
Cdd:PLN03232 701 FGSdfeSERYWRAIDVTALQ--HDLDLLPGRDLtEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190
....*....|....*....|....*....|....*....
gi 1550121285 178 LF--VILDGMrrQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:PLN03232 779 VFdsCMKDEL--KGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-187 |
4.96e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 4 LLSVQNLT--KRFGAVTanDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRAD--SGVIRFKGQVAELNSP---ADA 76
Cdd:PRK13547 1 MLTADHLHvaRRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNGEPlaaIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 77 LRLGI--GMVHQHFVLVENFTVLENIIVGS-PDVGMLLSKSTARQKVEDLCL-RCGIELDLDREIWQLSVGEQQWVEILK 152
Cdd:PRK13547 79 PRLARlrAVLPQAAQPAFAFSAREIVLLGRyPHARRAGALTHRDGEIAWQALaLAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 153 AL---------YFGAELLILDEPTAVLTPQQSDQLfviLDGMRR 187
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRL---LDTVRR 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
268-478 |
5.28e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.77 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 268 EEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLS-----SGRFHLNGEAIVAPTSREM-LDRGVGLVpddrFR 341
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTVdLRKEIGMV----FQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 342 EGLISEFGTAENLVLGWQRKPEYrrgpflDRGKINDLAQRKLEEFRIVAASTDLPVER---LSGGNAQRVILAREFLNAK 418
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGIK------DKQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 419 CLLLANQPTRGLDVAASEFVYEKILEKRaEGFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-202 |
5.32e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 24 DLDVRKGEIHCLFGENGAGKSTLSaclygyyRADSG-VIRFKGQ-VAELNSPAdalRLGIGMVHQhfvLVE-----NFTV 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALA-------RALAGeLPLLSGErQSQFSHIT---RLSFEQLQK---LVSdewqrNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 97 LenIIVGSPDVGMllsksTARQKVED------LCLRC----GIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:PRK10938 90 M--LSPGEDDTGR-----TTAEIIQDevkdpaRCEQLaqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1550121285 167 TAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREV 202
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEI 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
271-485 |
5.62e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSRE---MLDRGVGLVpdDRFREGLISE 347
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLV--FQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 FGTAENLVLGWQR----KPEYRRgpfldrgkindLAQRKLeefRIVAASTDL----PVErLSGGNAQRVILAREFLNAKC 419
Cdd:PRK13649 101 ETVLKDVAFGPQNfgvsQEEAEA-----------LAREKL---ALVGISESLfeknPFE-LSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 420 LLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
324-485 |
5.91e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 324 SREMLDRGVGLvpDDRFREGLISEFGTAENLvlgwqrkpeYRRGPFLD--RGKINDLAQRKLEEFRIVAASTDlPVERLS 401
Cdd:NF000106 79 NRRALRRTIG*--HRPVR*GRRESFSGRENL---------YMIGR*LDlsRKDARARADELLERFSLTEAAGR-AAAKYS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 402 GGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTV 481
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
....
gi 1550121285 482 RPEE 485
Cdd:NF000106 227 KVDE 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
273-478 |
7.60e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQK----ELFEVL-MGVRTLSsGRFHLNGEAIVAPTSRemlDRGVGLV-PDDRfregliS 346
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA-GRVLLDGKPVAPCALR---GRKIATImQNPR------S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTAENLVlgwqrkpEYRRGPFLDRGKINDLAQRkLEEFRIVAASTDLPVERL-----SGGNAQRVILAREFLNAKCLL 421
Cdd:PRK10418 91 AFNPLHTMH-------THARETCLALGKPADDATL-TAALEAVGLENAARVLKLypfemSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 422 LANQPTRGLDVAASEFVY---EKILEKRAEGfaVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK10418 163 IADEPTTDLDVVAQARILdllESIVQKRALG--MLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
273-485 |
7.93e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTS---REMLDRGVGLVpddrFRE-GLISEF 348
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMV----FQSfALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRK---PEYRRGPFLDRgkindLAQRKLEEFrivaaSTDLPVErLSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:PRK10070 122 TVLDNTAFGMELAginAEERREKALDA-----LRQVGLENY-----AHSYPDE-LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 426 PTRGLD-VAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK10070 191 AFSALDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-458 |
8.57e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI---VAPTSREMLDRG--VGLVPDDRFREGL 344
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLCFVGhrSGINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 345 ISEFGTAENLVlgwqrkpeyrrgpfldrgKINDLAQR-KLEEFrivaasTDLPVERLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:PRK13540 96 LYDIHFSPGAV------------------GITELCRLfSLEHL------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1550121285 424 NQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEE 458
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
261-485 |
8.68e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 44.38 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 261 VAIGewGEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREM-LDRGVgLvpddR 339
Cdd:PRK13548 10 VRLG--GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELaRRRAV-L----P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 340 FREGLISEFGTAENLVLGwqrkpeyrRGPF-LDRGKINDLAQRKLEEFRIVA-ASTDLPveRLSGGNAQRVILAR----- 412
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMG--------RAPHgLSRAEDDALVAAALAQVDLAHlAGRDYP--QLSGGEQQRVQLARvlaql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 413 -EFLNAKCLLLANQPTRGLDVA--------ASEFVyekilekRAEGFAVF-------LASeelddllRLCDRIAVIFKGK 476
Cdd:PRK13548 153 wEPDGPPRWLLLDEPTSALDLAhqhhvlrlARQLA-------HERGLAVIvvlhdlnLAA-------RYADRIVLLHQGR 218
|
....*....
gi 1550121285 477 IVGTVRPEE 485
Cdd:PRK13548 219 LVADGTPAE 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
273-478 |
8.87e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.95 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvAPTSREMLDRGVGLVpddrFREGLISEFGTAE 352
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTVTRASLRRNIAVV----FQDAGLFNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVLGwqrKP-----EYRRGpfLDRGKINDLAQRKLEEFRIVAAstdlpvER---LSGGNAQRVILAREFL-NAKCLLLa 423
Cdd:PRK13657 428 NIRVG---RPdatdeEMRAA--AERAQAHDFIERKPDGYDTVVG------ERgrqLSGGERQRLAIARALLkDPPILIL- 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 424 NQPTRGLDVAASEFVYEKILEKRaEGFAVFLASEELDDlLRLCDRIAVIFKGKIV 478
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLST-VRNADRILVFDNGRVV 548
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-202 |
1.13e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 19 ANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQvaelnspADALRLGIGMVHQhfvlvenFTVLE 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------AALIAISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 99 NIIVGSPDVGMllskstARQKVEDLCLRCgIEL-DLDREIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVltpq 173
Cdd:PRK13545 105 NIELKGLMMGL------TKEKIKEIIPEI-IEFaDIGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSV---- 173
|
170 180 190
....*....|....*....|....*....|....
gi 1550121285 174 qSDQLFV--ILDGM---RRQGLSIILISHKLREV 202
Cdd:PRK13545 174 -GDQTFTkkCLDKMnefKEQGKTIFFISHSLSQV 206
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
396-485 |
1.16e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 43.68 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 396 PVERLSGGNAQRVILAREFL------NAK-CLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELDDLLRLCDR 468
Cdd:COG4138 123 PLTQLSGGEWQRVRLAAVLLqvwptiNPEgQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADR 202
|
90
....*....|....*..
gi 1550121285 469 IAVIFKGKIVGTVRPEE 485
Cdd:COG4138 203 VWLLKQGKLVASGETAE 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-214 |
1.30e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.08 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANdsVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAelnspadalrlgi 81
Cdd:cd03291 37 DNNLFFSNLCLVGAPVLKN--INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 gmVHQHFVLVENFTVLENIIVG-SPDVGMLLSKSTARQKVEDLCLRCgiELD---LDREIWQLSVGEQQWVEILKALYFG 157
Cdd:cd03291 102 --FSSQFSWIMPGTIKENIIFGvSYDEYRYKSVVKACQLEEDITKFP--EKDntvLGEGGITLSGGQRARISLARAVYKD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550121285 158 AELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSDRVTILRKG 214
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
271-495 |
1.39e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.85 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREmLDRGVGLV---PDDRFREGLISE 347
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVfqnPDNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 348 ---FGTAENlvlGWQRKPEYRRgpfldrgkIND-LAQRKLEEFrivaaSTDLPvERLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:PRK13635 102 dvaFGLENI---GVPREEMVER--------VDQaLRQVGMEDF-----LNREP-HRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550121285 424 NQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRlCDRIAVIFKGKIVGTVRPEEttLLELGMMM 495
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQlKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE--IFKSGHML 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-170 |
1.66e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKST----LSACL---YGYYRADSG---VI-RFKGqvAELNSPADALRLG-IGMVH--QHfvlVE 92
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTavkiLSGELipnLGDYEEEPSwdeVLkRFRG--TELQNYFKKLYNGeIKVVHkpQY---VD 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 93 nftVLENIIVGSpdVGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVL 170
Cdd:PRK13409 171 ---LIPKVFKGK--VRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
111-208 |
1.73e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 111 LSKSTARQKVEDLClRCGIE-LDLDREIWQLSVGEQQWVEILKALYFGAE---LLILDEPTAVLTPQQSDQLFVILDGMR 186
Cdd:PRK00635 781 LDEPSIHEKIHALC-SLGLDyLPLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLT 859
|
90 100
....*....|....*....|..
gi 1550121285 187 RQGLSIILISHKLREVMQSDRV 208
Cdd:PRK00635 860 HQGHTVVIIEHNMHVVKVADYV 881
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-215 |
1.89e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 1 MENLLSVQNLTKRF---------GAVTANDSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVI---------- 61
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 62 --RFKGQVAEL--NSPADAL--RLGIGMVHQhFVLVENfTVLEniivgspdvgmllskSTARQKVEDLCLRcGIELDLDR 135
Cdd:PRK15112 81 dySYRSQRIRMifQDPSTSLnpRQRISQILD-FPLRLN-TDLE---------------PEQREKQIIETLR-QVGLLPDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 136 EIW---QLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLF-VILDGMRRQGLSIILISHKLrEVMQ--SDRVT 209
Cdd:PRK15112 143 ASYyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLInLMLELQEKQGISYIYVTQHL-GMMKhiSDQVL 221
|
....*.
gi 1550121285 210 ILRKGK 215
Cdd:PRK15112 222 VMHQGE 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
267-492 |
2.05e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.00 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIvaptsREM----LDRGVGLVPDDRFre 342
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-----RDLtlesLRRQIGVVPQDTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 343 gLISefGT-AENLVLGwqrKPEYrrgpflDRGKINDLAQR-KLEEFriVAAstdLP-------VER---LSGGNAQRVIL 410
Cdd:COG1132 425 -LFS--GTiRENIRYG---RPDA------TDEEVEEAAKAaQAHEF--IEA---LPdgydtvvGERgvnLSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 411 AREFL-NAKCLLLaNQPTRGLDvAASEFVYEKILEKRAEGFAVF-----LASeelddlLRLCDRIAVIFKGKIVGTVRPE 484
Cdd:COG1132 488 ARALLkDPPILIL-DEATSALD-TETEALIQEALERLMKGRTTIviahrLST------IRNADRILVLDDGRIVEQGTHE 559
|
....*...
gi 1550121285 485 EttLLELG 492
Cdd:COG1132 560 E--LLARG 565
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
267-492 |
2.14e-04 |
|
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: 42.99 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI--VAPTSremLDRGVGLVPDD------ 338
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDS---LRRAIGVVPQDtvlfnd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 339 ----RFREGLISefGTAENLVlgwqrkpEYRRgpfldRGKINDLAQRKLEEFRIVAASTDLpveRLSGGNAQRVILAREF 414
Cdd:cd03253 90 tigyNIRYGRPD--ATDEEVI-------EAAK-----AAQIHDKIMRFPDGYDTIVGERGL---KLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 415 LNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASeelddllRL-----CDRIAVIFKGKIVGTVRPEEttLL 489
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH-------RLstivnADKIIVLKDGRIVERGTHEE--LL 223
|
...
gi 1550121285 490 ELG 492
Cdd:cd03253 224 AKG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
270-478 |
2.14e-04 |
|
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: 43.97 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeAIVAPTSREMLDRGVGLVPDDrfreglISEF- 348
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG-ADLSQWDREELGRHIGYLPQD------VELFd 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GT-AENLVlgwqRKPEyrrgpfLDRGKINDLAQR--------KLE---EFRIVAASTdlpveRLSGGNAQRVILAREFLN 416
Cdd:COG4618 420 GTiAENIA----RFGD------ADPEKVVAAAKLagvhemilRLPdgyDTRIGEGGA-----RLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 417 AKCLLLANQPTRGLDVAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIV 478
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
399-480 |
2.35e-04 |
|
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: 42.91 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 399 RLSGGNAQRVILAREFL-NAKCLLLaNQPTRGLDvAASEFVYEKILEKRAEGFAVFLASEELDDlLRLCDRIAVIFKGKI 477
Cdd:cd03249 139 QLSGGQKQRIAIARALLrNPKILLL-DEATSALD-AESEKLVQEALDRAMKGRTTIVIAHRLST-IRNADLIAVLQNGQV 215
|
....*
gi 1550121285 478 V--GT 480
Cdd:cd03249 216 VeqGT 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
138-197 |
2.51e-04 |
|
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: 41.76 E-value: 2.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550121285 138 WQ--LSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGMrrqGLSIILISH 197
Cdd:cd03223 88 WDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-214 |
2.91e-04 |
|
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: 41.85 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 27 VRKGEIHCLFGENGAGKSTLSACLYGyyRADSGVIrfKGQVAELNSPAD-ALRLGIGMVHQHFVLVENFTVLEniivgsp 105
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TGEILINGRPLDkNFQRSTGYVEQQDVHSPNLTVRE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 106 dvGMLLSKstarqkvedlCLRcgieldldreiwQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQLFVILDGM 185
Cdd:cd03232 99 --ALRFSA----------LLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1550121285 186 RRQGLSIILISHKLREVM--QSDRVTILRKG 214
Cdd:cd03232 155 ADSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-215 |
3.50e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 21 DSVDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRAdsGVIRFKGQVAELNSPADALRLGIGMVHqhfVLVEN----FTV 96
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALRGRKIA---TIMQNprsaFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 97 LENIIVGSPDVGMLLSKSTARQKVEDLCLRCGIELD---LDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTP- 172
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVv 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550121285 173 QQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGK 215
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGR 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
379-485 |
4.54e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 379 AQRKLEEFRIVAASTDLP--VERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYE--KILEKRAEGFAVFL 454
Cdd:PRK10261 146 AKRMLDQVRIPEAQTILSryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEMSMGVIFI 225
|
90 100 110
....*....|....*....|....*....|.
gi 1550121285 455 aSEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK10261 226 -THDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
269-485 |
6.16e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.69 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 269 EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLdRGVglvpddRFREGLISEF 348
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI-RPV------RKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRKPEYrrGP--F-LDRGKINDLAQRKLEEF---RIVAASTDLpveRLSGGNAQRV----ILArefLNAK 418
Cdd:PRK13646 94 PESQLFEDTVEREIIF--GPknFkMNLDEVKNYAHRLLMDLgfsRDVMSQSPF---QMSGGQMRKIaivsILA---MNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 419 CLLLaNQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK13646 166 IIVL-DEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
270-491 |
8.11e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.02 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSReMLDRGVGLVPddrfREGLISEFG 349
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH-YLHRQVALVG----QEPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 350 TAENLVLGWQRKPEyrrgpfldrGKINDLAQRKLEEFRIVAASTDLPVE------RLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:TIGR00958 571 VRENIAYGLTDTPD---------EEIMAAAKAANAHDFIMEFPNGYDTEvgekgsQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550121285 424 NQPTRGLDVAASEFVYEkilEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIVgtvrpEETTLLEL 491
Cdd:TIGR00958 642 DEATSALDAECEQLLQE---SRSRASRTVLLIAHRL-STVERADQILVLKKGSVV-----EMGTHKQL 700
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-478 |
9.12e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.98 E-value: 9.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 400 LSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAEgFAVFLASEELDDLLRLCDRIAVIFKGKIV 478
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
270-485 |
9.14e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 270 VLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGeAIVAPTSREMLDRGVGLVPDD--------RFR 341
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-CDVAKFGLTDLRRVLSIIPQSpvlfsgtvRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 342 EGLISEFGTAENlvlgWQRkpeyrrgpfLDRGKINDLAQRKleEFRIVAASTDlPVERLSGGNAQRVILAREFLNAKCLL 421
Cdd:PLN03232 1330 IDPFSEHNDADL----WEA---------LERAHIKDVIDRN--PFGLDAEVSE-GGENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 422 LANQPTRGLDVAASEFVYEKILEKrAEGFAVFLASEELDDLLRlCDRIAVIFKGKIVGTVRPEE 485
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREE-FKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
267-431 |
9.66e-04 |
|
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: 41.84 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTlssgrfHLNGEAIVAP-----------------TSREMLD 329
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFNGEARPQPgikvgylpqepqldptkTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 330 RGVGLVPD--DRFRE-------------GLISEFGTAENLvlgwqrkpeyrrgpfLDRGKINDLaQRKLEefriVAAST- 393
Cdd:TIGR03719 91 EGVAEIKDalDRFNEisakyaepdadfdKLAAEQAELQEI---------------IDAADAWDL-DSQLE----IAMDAl 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1550121285 394 -----DLPVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLD 431
Cdd:TIGR03719 151 rcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
273-485 |
9.68e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.40 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 273 DINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREML---DRGVGLVpddrFREG-LISEF 348
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppeKRRIGYV----FQDArLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 349 GTAENLVLGWQRKpeyrrgpflDRGKINDLAQ-----RKLEEFRIvaastdlpveRLSGGNAQRVILAREFLNAKCLLLA 423
Cdd:PRK11144 92 KVRGNLRYGMAKS---------MVAQFDKIVAllgiePLLDRYPG----------SLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 424 NQPTRGLDVAASEFV--YekiLEKRAEGF--AVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK11144 153 DEPLASLDLPRKRELlpY---LERLAREIniPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-206 |
1.28e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.68 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 140 LSVGEQQWVEILKALYF---GAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD 206
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCAD 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
266-485 |
1.41e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 40.72 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 266 WGE-EVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAI-----------VAPTSREMLDRGVG 333
Cdd:PRK10619 15 YGEhEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 334 LVPDDRFRegLISEFGTAENL------VLGWQRKPEYRRGPF-LDRGKINDLAQRKLeefrivaastdlPVErLSGGNAQ 406
Cdd:PRK10619 95 TMVFQHFN--LWSHMTVLENVmeapiqVLGLSKQEARERAVKyLAKVGIDERAQGKY------------PVH-LSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 407 RVILAREFLNAKCLLLANQPTRGLDvaaSEFVYE--KILEKRA-EGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRP 483
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALD---PELVGEvlRIMQQLAeEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
..
gi 1550121285 484 EE 485
Cdd:PRK10619 237 EQ 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
267-485 |
1.54e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.54 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSReMLDRGVGLVPDD-RFREGLi 345
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQlPAAEGM- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 346 sefgTAENLV-LGwqrkpeyrRGPF---LDRGKINDlaQRKLEEFRIVAASTDLP---VERLSGGNAQRVILAREFL-NA 417
Cdd:PRK10575 101 ----TVRELVaIG--------RYPWhgaLGRFGAAD--REKVEEAISLVGLKPLAhrlVDSLSGGERQRAWIAMLVAqDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 418 KCLLLaNQPTRGLDVAASEFVYEKILE-KRAEGFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK10575 167 RCLLL-DEPTSALDIAHQVDVLALVHRlSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
271-491 |
1.55e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 271 LCDINFTIAENEILGLAGVAGNGQKELFEVLMGvrtlssgrfhlngEAIVAPTSREMLDRGVGLVPDDRFreglISEFGT 350
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------ELSHAETSSVVIRGSVAYVPQVSW----IFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 351 AENLVLGWQRKPEyRRGPFLDRGKIndlaQRKLEEFrivaASTDLPV--ER---LSGGNAQRVILAREFLNAKCLLLANQ 425
Cdd:PLN03232 696 RENILFGSDFESE-RYWRAIDVTAL----QHDLDLL----PGRDLTEigERgvnISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550121285 426 PTRGLDVAASEFVYEKILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGKIvgtvrPEETTLLEL 491
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI-----KEEGTFAEL 826
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
107-170 |
1.77e-03 |
|
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: 40.92 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 107 VGMLLSKSTARQKVEDLCLRCGIELDLDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVL 170
Cdd:COG1245 180 VRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
274-485 |
1.89e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 39.97 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 274 INFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAPTSREMLDRGVGLVpddrFRE-GLISEFGTAE 352
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT----FQHvRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 353 NLVLGWQRK------------PEYRRGP---------FLDRGKINDLAQRkleefrivAASTdlpverLSGGNAQRVILA 411
Cdd:PRK11300 100 NLLVAQHQQlktglfsgllktPAFRRAEsealdraatWLERVGLLEHANR--------QAGN------LAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550121285 412 REFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAE-GFAVFLASEELDDLLRLCDRIAVIFKGKIVGTVRPEE 485
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-206 |
2.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 131 LDLDREIWQLSVGEQQWVEILKALYFGAE---LLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD 206
Cdd:PRK00635 1691 LPLGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQAD 1769
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-233 |
2.06e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 2 ENLLSVQNLTKRFGAVTANDSVDLdvRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAELNSPADALRLGI 81
Cdd:PRK10982 248 EVILEVRNLTSLRQPSIRDVSFDL--HKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 82 GMVHQH--------FVLVENFTVLENIIVGSPDVGMLLSK--STARQKVEDlCLRCGIElDLDREIWQLSVGEQQWVEIL 151
Cdd:PRK10982 326 ALVTEErrstgiyaYLDIGFNSLISNIRNYKNKVGLLDNSrmKSDTQWVID-SMRVKTP-GHRTQIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 152 KALYFGAELLILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQ-SDRVTILRKGKVVATVETATTTAESI 230
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAGIVDTKTTTQNEI 483
|
...
gi 1550121285 231 TAL 233
Cdd:PRK10982 484 LRL 486
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-211 |
2.81e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550121285 140 LSVGEQQWVEILKALYFGAELLILDEPTAVLTpQQSDQLF--VILDGMRRQGLSIILISHKLREVMQSDRVTIL 211
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIekTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-215 |
3.17e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYY--RADSGVIrFKGQVAelnspadalrlgigMVHQhFVLVENFTVLENI 100
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELppRSDASVV-IRGTVA--------------YVPQ-VSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 101 IVGSP----------DVgmllsksTARQKveDLCLRCGIELDldrEIWQ----LSVGEQQWVEILKALYFGAELLILDEP 166
Cdd:PLN03130 700 LFGSPfdperyeraiDV-------TALQH--DLDLLPGGDLT---EIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1550121285 167 TAVLTPQQSDQLF--VILDGMRRQglSIILISHKLREVMQSDRVTILRKGK 215
Cdd:PLN03130 768 LSALDAHVGRQVFdkCIKDELRGK--TRVLVTNQLHFLSQVDRIILVHEGM 816
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-214 |
3.36e-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: 40.28 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 23 VDLDVRKGEIHCLFGENGAGKSTLSACLYGYYRADSGVIRFKGQVAelNSPadalrlgigmvhqHFVLVENFTVLENIIV 102
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS--FSP-------------QTSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 103 G-SPDVGMLLSKSTARQKVEDLCLRCgiELD---LDREIWQLSVGEQQWVEILKALYFGAELLILDEPTAVLTPQQSDQL 178
Cdd:TIGR01271 510 GlSYDEYRYTSVIKACQLEEDIALFP--EKDktvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1550121285 179 F------VILDGMRrqglsiILISHKLREVMQSDRVTILRKG 214
Cdd:TIGR01271 588 FesclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
267-442 |
4.16e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 38.93 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 267 GEEVLCDINFTIAENEILGLAGVAGNGQKELFEVLMGVRTLSSGRFHLNGEAIVAptsremldrgvglVPDDRFREGLIS 346
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-------------LKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 347 EFGTA--------ENLVLGWQ-RKPEYRRGPFLDrgkinDLAQRKLEEfrivaASTDLPVERLSGGNAQRVILAR--EFL 415
Cdd:PRK10247 86 CAQTPtlfgdtvyDNLIFPWQiRNQQPDPAIFLD-----DLERFALPD-----TILTKNIAELSGGEKQRISLIRnlQFM 155
|
170 180
....*....|....*....|....*..
gi 1550121285 416 nAKCLLLaNQPTRGLDVAASEFVYEKI 442
Cdd:PRK10247 156 -PKVLLL-DEITSALDESNKHNVNEII 180
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
396-432 |
4.20e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 4.20e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1550121285 396 PVERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDV 432
Cdd:PRK11147 437 PVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-215 |
5.71e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 37 GENGAGKSTLSACLYGYYRADSGVIRFKG-QVAELNSpADaLRLGIGMVHQHFVLVENfTVLENIIVGSPDVGMLLSKST 115
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGL-MD-LRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDADLWESL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 116 ARQKVEDLCLRCgiELDLDREIWQ----LSVGEQQWVEILKALYFGAELLILDEPTAVLTpQQSDQLfvILDGMRRQGLS 191
Cdd:PLN03130 1349 ERAHLKDVIRRN--SLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDAL--IQKTIREEFKS 1423
|
170 180
....*....|....*....|....*.
gi 1550121285 192 --IILISHKLREVMQSDRVTILRKGK 215
Cdd:PLN03130 1424 ctMLIIAHRLNTIIDCDRILVLDAGR 1449
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-208 |
5.82e-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: 39.61 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 131 LDLDREIWQLSVGEQQwvEILKALYFGAELL----ILDEPTAVLTPQQSDQLFVILDGMRRQGLSIILISHKLREVMQSD 206
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQ--RIRLATQIGSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAAD 557
|
..
gi 1550121285 207 RV 208
Cdd:TIGR00630 558 YV 559
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
397-476 |
5.98e-03 |
|
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: 37.43 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 397 VERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKRAegfAVFLASEELDDLLRLCDRIAVIFKGK 476
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
398-478 |
6.27e-03 |
|
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: 37.68 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 398 ERLSGGNAQRVILAREFLNAKCLLLANQPTRGLDVAASEFVYEKILEKrAEGFAVFLASEELDDLLRLcDRIAVIFKGKI 477
Cdd:cd03247 97 RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
.
gi 1550121285 478 V 478
Cdd:cd03247 175 I 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
400-476 |
8.14e-03 |
|
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: 37.83 E-value: 8.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550121285 400 LSGGNAQRVILAREFL-NAKCLLLaNQPTRGLDVAASEFVYEK-ILEKRAEGFAVFLASEELdDLLRLCDRIAVIFKGK 476
Cdd:cd03250 128 LSGGQKQRISLARAVYsDADIYLL-DDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-485 |
8.31e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 38.87 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 400 LSGGNAQRVILAREFLNAKCLLLANQPTRGLDvAASEFVYEKILEKRAEG--FAVFLASEELDDLLRLCDRIAVIFKGKI 477
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLD-SFMAYSVVQVLKGLAQKgkTIICTIHQPSSELFELFDKIILMAEGRV 245
|
....*...
gi 1550121285 478 VGTVRPEE 485
Cdd:TIGR00955 246 AYLGSPDQ 253
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-197 |
8.41e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.59 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 37 GENGAGKST-LSACLYGYYRAdsgVIRFKGQVAELNSPAdalRLG--IGMVHQHF--------VLVENFTVLENIIVgsp 105
Cdd:cd03240 29 GQNGAGKTTiIEALKYALTGE---LPPNSKGGAHDPKLI---REGevRAQVKLAFenangkkyTITRSLAILENVIF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550121285 106 dvgmllskstARQKvedlclrcgiELD--LDREIWQLSVGEQQWVEILKAL----YFGA--ELLILDEPTAVLTPQQSD- 176
Cdd:cd03240 100 ----------CHQG----------ESNwpLLDMRGRCSGGEKVLASLIIRLalaeTFGSncGILALDEPTTNLDEENIEe 159
|
170 180
....*....|....*....|..
gi 1550121285 177 QLFVILDGMRRQGLS-IILISH 197
Cdd:cd03240 160 SLAEIIEERKSQKNFqLIVITH 181
|
|
| |
