|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-497 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 652.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLAR-LGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNRE 240
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 241 VQEMYPKAQVELGEPLLQVRGLNLARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRS 320
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 321 PGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQ 400
Cdd:COG1129 321 PRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 401 QKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGE 480
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREE 480
|
490
....*....|....*..
gi 2545433469 481 AGSDQLLACATGAVQST 497
Cdd:COG1129 481 ATEEAIMAAATGGAAAA 497
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-486 |
2.14e-163 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 472.59 E-value: 2.14e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQF 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYfELQLPADALVGELNSAERQVLQITRALIRQPKIL 162
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERY-GLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 163 VFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNREVQ 242
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 243 EMYPKAQVELGEPLLQVRGLNLARRY-----RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLR 317
Cdd:COG3845 244 LRVEKAPAEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 318 LRSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGR--FSRWGLLSQRKEQAESLRLIDELAIKTPGPQAAVSQL 395
Cdd:COG3845 324 GLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRppFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 396 SGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
490
....*....|.
gi 2545433469 476 FHAGEAGSDQL 486
Cdd:COG3845 484 VPAAEATREEI 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-492 |
8.51e-160 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 463.63 E-value: 8.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI--HKADSGQVSIDGQPYAALSPRQVDALGVQ 81
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQ-LKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNREV 241
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGREL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 242 QEMYPKAQVELGEPLLQVRGLNL----ARRYRQID---LELRRGEIVGLTGLVGSGAKDLLKTLFGVVR-ADSGSIHLEG 313
Cdd:PRK13549 245 TALYPREPHTIGEVILEVRNLTAwdpvNPHIKRVDdvsFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 314 RLLRLRSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTPGPQAAVS 393
Cdd:PRK13549 325 KPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 394 QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
490
....*....|....*....
gi 2545433469 474 GEFHAGEAGSDQLLACATG 492
Cdd:PRK13549 485 GDLINHNLTQEQVMEAALR 503
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-490 |
2.00e-155 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 452.06 E-value: 2.00e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEH-LGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP-RHTSSAQIARLMVNR 239
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 240 EVQEMYPKAQVELGEPLLQVRGLnLARRYRQ-IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRL 318
Cdd:PRK11288 241 EIGDIYGYRPRPLGEVRLRLDGL-KGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 319 RSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSRWG-LLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSG 397
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLIMNLSG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 398 GNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFH 477
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
490
....*....|...
gi 2545433469 478 AGEAGSDQLLACA 490
Cdd:PRK11288 480 REQATERQALSLA 492
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-492 |
4.66e-135 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 400.15 E-value: 4.66e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRrGPF--VDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFV-NRFgrIDWKKMYAEADKLLAR-LNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNREV 241
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 242 QEMYPKAQVELGEPLLQVRGLNlARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSP 321
Cdd:PRK10762 243 EDQYPRLDKAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 322 GEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSR-WGLLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQ 400
Cdd:PRK10762 322 QDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 401 QKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGE 480
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
490
....*....|..
gi 2545433469 481 AGSDQLLACATG 492
Cdd:PRK10762 482 ATQEKLMAAAVG 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-481 |
5.86e-129 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 384.53 E-value: 5.86e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADS--GQVSIDGQPYAALSPRQVDALGVQ 81
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAK-VGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR--HTSSAQIARLMVNR 239
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 240 EVQEMYPKAQVELGEPLLQVRGLNL---ARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFG--VVRADSGSIH 310
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFEVKNWTVyhpLHPERKVvddvSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 311 LEGRLLRLRSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSRWGLLSQRKEQ--AESLRliDELAIKTPGP 388
Cdd:NF040905 321 KDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIkvAEEYR--KKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 389 QAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLH 468
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490
....*....|...
gi 2545433469 469 RGEIAGEFHAGEA 481
Cdd:NF040905 479 EGRITGELPREEA 491
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-491 |
1.04e-128 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 383.70 E-value: 1.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 11 KRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFIHQERLLP 90
Cdd:PRK10982 6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 91 ASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVA 170
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDE-LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 171 LVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNREVQEMYPKAQV 250
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPDKEN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 251 ELGEPLLQVRGLNLARR--YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQG 328
Cdd:PRK10982 245 KPGEVILEVRNLTSLRQpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERRSQGISPLLSVLENLTLAGLGRF-SRWGLLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQQKVALGK 407
Cdd:PRK10982 325 FALVTEERRSTGIYAYLDIGFNSLISNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 408 WLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGSDQLL 487
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
....
gi 2545433469 488 ACAT 491
Cdd:PRK10982 485 RLAS 488
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-490 |
2.04e-128 |
|
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: 383.41 E-value: 2.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI--HKADSGQVSIDGQPYAALSPRQVDALGVQ 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHEL-RRGPFVDRRRQQREAERLLAEyfeLQLPADAL---VGELNSAERQVLQITRALIR 157
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEItLPGGRMAYNAMYLRAKNLLRE---LQLDADNVtrpVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 158 QPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMV 237
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 238 NREVQEMYPKAQVELGEPLLQVRGLNL-------ARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVR-ADSGSI 309
Cdd:TIGR02633 239 GREITSLYPHEPHEIGDVILEARNLTCwdvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 310 HLEGRLLRLRSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTPGPQ 389
Cdd:TIGR02633 319 FINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 390 AAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHR 469
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
490 500
....*....|....*....|.
gi 2545433469 470 GEIAGEFHAGEAGSDQLLACA 490
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAA 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-485 |
2.94e-123 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 370.27 E-value: 2.94e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFIHQ 85
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEALFFGHELRRG----PFVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:PRK09700 88 ELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLR-VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVNREV 241
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGREL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 242 QEMYPKAQVELG----EPLLQVRglNLARR----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG 313
Cdd:PRK09700 247 QNRFNAMKENVSnlahETVFEVR--NVTSRdrkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 314 RLLRLRSPGEAIAQGIALVPEERRSQGISPLLSVLENLTLA---GLGRFS-RWGLLSQRKEQ--AESLRliDELAIKTPG 387
Cdd:PRK09700 325 KDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKgAMGLFHEVDEQrtAENQR--ELLALKCHS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 388 PQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVL 467
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
490
....*....|....*...
gi 2545433469 468 HRGEIAGEFHAGEAGSDQ 485
Cdd:PRK09700 483 CEGRLTQILTNRDDMSEE 500
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-499 |
5.06e-101 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 313.14 E-value: 5.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGheLRRGPfvdrrRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFG--LPKRQ-----ASMQKMKQLLAA-LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 164 FDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRdVAVVEPRHTSS-AQIarlmvnreVQ 242
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGT-IALSGKTADLStDDI--------IQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 243 EMYPKAQ-----------VEL---------GEPLLQVRGLNlARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVV 302
Cdd:PRK15439 235 AITPAARekslsasqklwLELpgnrrqqaaGAPVLTVEDLT-GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 303 RADSGSIHLEGRLLRLRSPGEAIAQGIALVPEERRSQGI---SPLLSVLENLTLAGLGRFSRWGllsqrKEQAESLRLID 379
Cdd:PRK15439 314 PARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLyldAPLAWNVCALTHNRRGFWIKPA-----RENAVLERYRR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 380 ELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLG 459
Cdd:PRK15439 389 ALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQ 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2545433469 460 ICDRILVLHRGEIAGEFHAGEAGSDQLLACATGAVQSTVA 499
Cdd:PRK15439 469 MADRVLVMHQGEISGALTGAAINVDTIMRLAFGEHQAQEA 508
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
253-472 |
8.87e-76 |
|
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: 236.56 E-value: 8.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 253 GEPLLQVRGLNLARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIALV 332
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 PEERRSQGISPLLSVLENLTLAglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavSQLSGGNQQKVALGKWLSRR 412
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALS--------------------------------------SLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
1.07e-64 |
|
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: 206.90 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQerllpasftvgealffghelrrgpfvdrrrqqreaerllaeyfelqlpadalvgeLNSAERQVLQITRALIRQPKILV 163
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 164 FDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-472 |
5.21e-54 |
|
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: 189.73 E-value: 5.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRF--GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD---SGQVSIDGQPYAALSPRqVD 76
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA-LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 ALGVQFIHQE---RLLPAsfTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITR 153
Cdd:COG1123 82 GRRIGMVFQDpmtQLNPV--TVGDQIAEALENLG---LSRAEARARVLELLEA-VGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQI 232
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 233 ARLMVNREVQEMYPKAQV-ELGEPLLQVRglNLARRYRQ-----------IDLELRRGEIVGLTGLVGSGAKDLLKTLFG 300
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAaAAAEPLLEVR--NLSKRYPVrgkggvravddVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 301 VVRADSGSIHLEGRLLRLRSPGE--AIAQGIALVPEERRSQgISPLLSVLENLT--LAGLGRFSRwgllSQRKEQAESL- 375
Cdd:COG1123 314 LLRPTSGSILFDGKDLTKLSRRSlrELRRRVQMVFQDPYSS-LNPRMTVGDIIAepLRLHGLLSR----AERRERVAELl 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 376 ---RLIDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLS 451
Cdd:COG1123 389 ervGLPPDLADRYPH------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIS 462
|
490 500
....*....|....*....|.
gi 2545433469 452 SDLPELLGICDRILVLHRGEI 472
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRI 483
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-221 |
1.69e-50 |
|
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: 172.73 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGvqFIHQ 85
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG--VLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEAL-FFGhELRRGPfvdrRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVF 164
Cdd:COG4555 82 ERGLYDRLTVRENIrYFA-ELYGLF----DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 165 DEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
2.88e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFi 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 hQERLLPASFTVGEAL-FFGhELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKIL 162
Cdd:COG1131 80 -QEPALYPDLTVRENLrFFA-RLYG---LPRKEARERIDELL-ELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 163 VFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-217 |
4.67e-48 |
|
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: 163.72 E-value: 4.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGvqFI 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALffghELRRGpfvdrrrqqreaerllaeyfelqlpadalvgelnsaERQVLQITRALIRQPKILV 163
Cdd:cd03230 79 PEEPSLYENLTVRENL----KLSGG------------------------------------MKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 164 FDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-245 |
3.06e-44 |
|
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: 156.74 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 ----QFIhqeRLLPaSFTVGEAL-----------FFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAE 145
Cdd:COG0411 82 artfQNP---RLFP-ELTVLENVlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 146 RQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRD-QGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250 260
....*....|....*....|.
gi 2545433469 225 rhtssAQIARlmvNREVQEMY 245
Cdd:COG0411 238 -----AEVRA---DPRVIEAY 250
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-220 |
9.13e-44 |
|
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: 154.52 E-value: 9.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV--- 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIgrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 -QFIhqeRLLPaSFTVGEALFFGHELRRGPFVDRRRQQREAERL------LAEYFELQLPADALVGELNSAERQVLQITR 153
Cdd:cd03219 81 fQIP---RLFP-ELTVLENVMVAAQARTGSGLLLARARREEREAreraeeLLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
2.23e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.47 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyaaLSPRQVDALGvqF 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIG--Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASFTVGEAL-FFGhELrRGpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvYLA-RL-KG--LSKAEAKRRADEWL-ERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 162 LVFDEP-----SVAlvkreVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:COG4152 151 LILDEPfsgldPVN-----VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
8.18e-37 |
|
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: 142.35 E-value: 8.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 G--VQFIHQ--ERLLPASFTVGEALFFGHELRRGpfVDRRRQQREAERLLAeyfELQLPADAL---VGELNSAERQVLQI 151
Cdd:COG1123 341 RrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGL--LSRAERRERVAELLE---RVGLPPDLAdryPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR---IVE 485
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-220 |
4.31e-36 |
|
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: 133.33 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRrqqreaerlLAEYFELqLPA-----DALVGELNSAERQVLQITRALIRQ 158
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKAR---------LERVYEL-FPRlkerrKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 159 PKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
2.12e-35 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 131.49 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFI 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN---IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPfvdrRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVP----KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 164 FDEPSVALvkrevDQLLR------IVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:cd03259 154 LDEPLSAL-----DAKLReelreeLKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
4.50e-35 |
|
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: 130.48 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyaaLSPRQVDALGvqFI 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---LDIAARNRIG--YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDE----WLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 164 FDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
1.77e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRqvdalgV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASF--TVGEALFFGHELRRGPF--VDRRRQQREAERL----LAEYfelqlpADALVGELNSAERQ-VLqI 151
Cdd:COG1121 78 GYVPQRAEVDWDFpiTVRDVVLMGRYGRRGLFrrPSRADREAVDEALervgLEDL------ADRPIGELSGGQQQrVL-L 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-223 |
2.87e-34 |
|
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: 128.78 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALG 79
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 --VQFIHQERL--LPASFTVGEALFFGHELRRGPFVDrrrqQREAERLLAEYFELQLPADAL---VGELNSAERQVLQIT 152
Cdd:cd03257 82 keIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKK----EARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 153 RALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK---IVE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-225 |
6.17e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 128.62 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQF 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-ARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASFTVGEALFFGhelrRGPFVDRRRQQREAERLLA----EYFELQLPADALVGELNSAERQVLQITRALIRQ 158
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALG----RYPHLGLFGRPSAEDREAVeealERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 159 PKILVFDEPSVAL-VKREVDqLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:COG1120 156 PPLLLLDEPTSHLdLAHQLE-VLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-245 |
3.59e-33 |
|
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: 125.86 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGpfvdrrrqQREAERLLAEYFELqLP-----ADALVGELNSAERQVLQITRAL 155
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRD--------RAEVRADLERVYEL-FPrlkerRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 156 IRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAvveprhtsSAQIARL 235
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVL--------EGTAAEL 223
|
250
....*....|
gi 2545433469 236 MVNREVQEMY 245
Cdd:COG0410 224 LADPEVREAY 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-217 |
7.36e-33 |
|
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: 124.54 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFG--ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG-----QPYAALSPrqvd 76
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtDRKAARQS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 aLGVqfIHQERLLPASFTVGEALFFGHELRRGPfvdrRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:cd03263 77 -LGY--CPQFDALFDELTVREHLRFYARLKGLP----KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRLRdQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
257-472 |
4.86e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.86 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlaRRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIAQGIA 330
Cdd:COG1131 1 IEVRGLT--KRYgdktalDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEErrsQGISPLLSVLENLTL-AGLGRFSRwgllSQRKEQAEslRLIDELAIkTPGPQAAVSQLSGGNQQKVALGKWL 409
Cdd:COG1131 77 YVPQE---PALYPDLTVRENLRFfARLYGLPR----KEARERID--ELLELFGL-TDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 410 SRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-221 |
9.06e-32 |
|
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: 121.71 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGA----TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyAALSPRQVDAlG 79
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQERLLPASFTVGEAL-FFG--HELRRGPFVDRRRQqreaerlLAEYFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeYFAglYGLKGDELTARLEE-------LADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
9.47e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 9.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP----RQVdalg 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrRQV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 vQFIHQErllPASF--TVGEALFFGHELRRGPFvdrrrQQREAERLLAEyfeLQLPADAL---VGELNSAERQVLQITRA 154
Cdd:COG4619 77 -AYVPQE---PALWggTVRDNLPFPFQLRERKF-----DRERALELLER---LGLPPDILdkpVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 155 LIRQPKILVFDEPSVAL---VKREVDQLLRivKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:COG4619 145 LLLQPDVLLLDEPTSALdpeNTRRVEELLR--EYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-224 |
1.06e-31 |
|
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: 121.32 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 7 QHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGqpYAALS-PRQVDA-LGVQFih 84
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVRePREVRRrIGIVF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 85 QERLLPASFTVGEALFF--------GHELRRgpfvdrrrqqreAERLLAEYFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:cd03265 80 QDLSVDDELTGWENLYIharlygvpGAERRE------------RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
1.27e-31 |
|
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: 119.27 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 5 HLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAlGVQFIH 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 85 QerllpasftvgealffghelrrgpfvdrrrqqreaerllaeyfelqlpadalvgeLNSAERQVLQITRALIRQPKILVF 164
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 165 DEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
1.49e-31 |
|
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: 120.65 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRF--GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQFI 83
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQErllPASF----TVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:cd03225 81 FQN---PDDQffgpTVEEEVAFGLENLG---LPEEEIEERVEEALEL-VGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 160 KILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-220 |
1.08e-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: 118.40 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 5 HLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRqvdalgVQFIH 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 85 QERLLPASF--TVGEALFFGHELRRGPFvdrrrqqreaERLLAEYFELQLPADALVG----------ELNSAERQVLQIT 152
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLF----------RRLSKADKAKVDEALERVGlseladrqigELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 153 RALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLrNGRDVA 220
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
257-488 |
1.23e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 118.69 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLArrY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIA 330
Cdd:cd03224 1 LEVENLNAG--YgksqilFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEERRsqgISPLLSVLENLTLAGLGRF---SRWGL---------LSQRKEQaeslrlidelaiktpgpqaAVSQLSGG 398
Cdd:cd03224 79 YVPEGRR---IFPELTVEENLLLGAYARRrakRKARLervyelfprLKERRKQ-------------------LAGTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 399 NQQKVALGKWLSRRSAVYLLDEPCVG-----VDvgakvEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGlapkiVE-----EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
250
....*....|....*
gi 2545433469 474 gefHAGEAgsDQLLA 488
Cdd:cd03224 212 ---LEGTA--AELLA 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-232 |
1.32e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 121.07 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVq 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 fIHQERLLPASFTVGEALF-FGHElrrgpFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK13537 85 -VPQFDNLDPDFTVRENLLvFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQI 232
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-226 |
1.39e-30 |
|
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: 119.14 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATL----ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdAL 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GVQFIHQErllPAS-----FTVGEALffgHELRRGPFVDRRRQQREAerLLAEyfeLQLPADAL---VGELNSAERQVLQ 150
Cdd:COG1124 80 RVQMVFQD---PYAslhprHTVDRIL---AEPLRIHGLPDREERIAE--LLEQ---VGLPPSFLdryPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 151 ITRALIRQPKILVFDEPSVAL---VKREVdqlLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:COG1124 149 IARALILEPELLLLDEPTSALdvsVQAEI---LNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
1.69e-30 |
|
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: 118.59 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQF 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQ--ERLLPASfTVGEALFFG--------HELRRGpfVDRrrqqreaerlLAEYFELQLPADALVGELNSAERQVLQIT 152
Cdd:COG1122 80 VFQnpDDQLFAP-TVEEDVAFGpenlglprEEIRER--VEE----------ALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 153 RALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-220 |
1.93e-30 |
|
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: 116.77 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQFIHQ 85
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-ARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 erllpasftvgeALffghelrrgpfvdrrrqqreaerllaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFD 165
Cdd:cd03214 81 ------------AL--------------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 166 EPSVAL-VKREVdQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03214 123 EPTSHLdIAHQI-ELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-217 |
1.14e-29 |
|
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: 115.39 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP--RQVDALgvq 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 fIHQERLLPAsFTVGEALFFGHELRRGPFVDRRRqqreaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:cd03268 78 -IEAPGFYPN-LTARENLRLLARLLGIRKKRIDE--------VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
254-473 |
2.70e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLARRYRQ----IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGeaiaqgI 329
Cdd:COG1121 4 MPAIELENLTVSYGGRPvledVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 330 ALVPEERRSQGISPLlSVLEnltLAGLGRFSRWGLL----SQRKEQA-ESLRL--IDELAiktpgpQAAVSQLSGGNQQK 402
Cdd:COG1121 78 GYVPQRAEVDWDFPI-TVRD---VVLMGRYGRRGLFrrpsRADREAVdEALERvgLEDLA------DRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 403 VALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-472 |
5.08e-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: 120.29 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI--HKADSGQV----------------SIDGQ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 66 PY----AALSPRQVDALGVQFIHQERL-------LPASFTV-GEALFFGHELRRGPFVDRRRQQREAERL-LAEYFELQL 132
Cdd:TIGR03269 81 PCpvcgGTLEPEEVDFWNLSDKLRRRIrkriaimLQRTFALyGDDTVLDNVLEALEEIGYEGKEAVGRAVdLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 133 PADALVGELNSAERQVLQITRALIRQPKILVFDEPSVAL----VKREVDQLLRIVKrlrDQGLSILYISHYLQEIDSLCD 208
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLdpqtAKLVHNALEEAVK---ASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 209 EVTVLRNGRDVAVVEPrhtsSAQIARLMvnREVQEMYPKAQVELGEPLLQVRglNLARRYRQID-----------LELRR 277
Cdd:TIGR03269 238 KAIWLENGEIKEEGTP----DEVVAVFM--EGVSEVEKECEVEVGEPIIKVR--NVSKRYISVDrgvvkavdnvsLEVKE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 278 GEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLE-----------GRLLRLRSpgeaiAQGIALVPEErrsQGISPLLS 346
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRA-----KRYIGILHQE---YDLYPHRT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTlaglgrfsrwgllsqrkeQAESLRLIDELA-------IKTPG--PQAAVS-------QLSGGNQQKVALGKWLS 410
Cdd:TIGR03269 382 VLDNLT------------------EAIGLELPDELArmkavitLKMVGfdEEKAEEildkypdELSEGERHRVALAQVLI 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
257-472 |
2.27e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 110.57 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRglNLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrlLRLRSPGEAIAQGIA 330
Cdd:cd03230 1 IEVR--NLSKRYGKktalddISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--KDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEERRsqgISPLLSVLENLtlaglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavsQLSGGNQQKVALGKWLS 410
Cdd:cd03230 77 YLPEEPS---LYENLTVRENL------------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-223 |
3.66e-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: 111.79 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRqvdalg 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQE-RLLPAsFTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQ 158
Cdd:cd03293 75 RGYVFQQdALLPW-LTVLDNVALGLELQG---VPKAEARERAEELLEL-VGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 159 PKILVFDEPSVAL--VKREV--DQLLRIvkrLRDQGLSILYISHYLQEIDSLCDEVTVL--RNGRDVAVVE 223
Cdd:cd03293 150 PDVLLLDEPFSALdaLTREQlqEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
5.13e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 109.97 E-value: 5.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALS---PRQVDALGV 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFihQERLLPASFTVGEALFFGhelrrgpfvdrrrqqreaerllaeyfelqlpadalvgeLNSAERQVLQITRALIRQPK 160
Cdd:cd03229 81 VF--QDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
263-473 |
5.30e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.09 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrsPGEAIAQGIALVPEER 336
Cdd:cd03235 4 DLTVSYGGhpvledVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 RSQGISPLlSVLEnltLAGLGRFSRWGLLsqRKEQAESLRLIDElAIKTPG----PQAAVSQLSGGNQQKVALGKWLSRR 412
Cdd:cd03235 78 SIDRDFPI-SVRD---VVLMGLYGHKGLF--RRLSKADKAKVDE-ALERVGlselADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-223 |
6.92e-28 |
|
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: 111.13 E-value: 6.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGAT----LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL- 78
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 -GVQFIHQERLLPASFTVGEALFFGHELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIR 157
Cdd:cd03258 82 rRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAEIEERVLELL-ELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 158 QPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE---VVE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
2.60e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRqvd 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 aLGVQFihQE-RLLPAsFTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRAL 155
Cdd:COG1116 82 -RGVVF--QEpALLPW-LTVLDNVALGLELRG---VPKAERRERARELLEL-VGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 156 IRQPKILVFDEPSVAL--VKREV--DQLLRIvkrLRDQGLSILYISHYLQEIDSLCDEVTVLRNG-----RDVAVVEPR 225
Cdd:COG1116 154 ANDPEVLLMDEPFGALdaLTRERlqDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPR 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-221 |
5.73e-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: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--- 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 -GVQFihQERLLPASFTVGEALFFGheLRRgpfvdrrrQQREAERLLAEYFELQLpadALVGeLNSAE------------ 145
Cdd:COG1127 84 iGMLF--QGGALFDSLTVFENVAFP--LRE--------HTDLSEAEIRELVLEKL---ELVG-LPGAAdkmpselsggmr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 146 RQVlQITRALIRQPKILVFDEPSVAL---VKREVDQLLRivkRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:COG1127 148 KRV-ALARALALDPEILLYDEPTAGLdpiTSAVIDELIR---ELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-239 |
7.83e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 7.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP-YAALSPRQvdaLGVQF 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRE---RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLpasF---TVGEALFFGheLRRGPfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:COG1118 80 VFQHYAL---FphmTVAENIAFG--LRVRP-PSKAEIRARVEELLEL-VQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 160 KILVFDEPSVAL---VKREVDQLLRivKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP----RHTSSAQI 232
Cdd:COG1118 153 EVLLLDEPFGALdakVRKELRRWLR--RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPdevyDRPATPFV 230
|
....*....
gi 2545433469 233 ARLM--VNR 239
Cdd:COG1118 231 ARFLgcVNV 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-236 |
9.27e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLR-KRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQ 81
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERL---LPASFTVGEALFFGH----ELRRGPFVDRRRQQREAERLLAEyFELQLP-ADALVGEL---NsaeRQVLQ 150
Cdd:COG3845 337 YIPEDRLgrgLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAEELIEE-FDVRTPgPDTPARSLsggN---QQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 151 ITRALIRQPKILVFDEP-------SVALVKRevdqllRIVKrLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVE 223
Cdd:COG3845 413 LARELSRDPKLLIAAQPtrgldvgAIEFIHQ------RLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVP 485
|
250
....*....|...
gi 2545433469 224 PRHTSSAQIARLM 236
Cdd:COG3845 486 AAEATREEIGLLM 498
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-217 |
9.64e-27 |
|
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: 108.20 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 7 QHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQvdaLGVQFIHQE 86
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 87 RLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDE 166
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 167 PSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
256-473 |
1.23e-26 |
|
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: 108.21 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 256 LLQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIAL 331
Cdd:COG1120 1 MLEAENLSVGYGGRPVlddvSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 332 VPEERRSqgiSPLLSVLEnltLAGLGRF---SRWGLLSQRKEQA--ESLRL--IDELAiktpgpQAAVSQLSGGNQQKVA 404
Cdd:COG1120 80 VPQEPPA---PFGLTVRE---LVALGRYphlGLFGRPSAEDREAveEALERtgLEHLA------DRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 405 LGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLV-EEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
257-472 |
1.53e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.52 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLnlARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIA 330
Cdd:cd03219 1 LEVRGL--TKRFgglvalDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 lvpeerRS-QGISPL--LSVLENLTLAGLGR-FSRWGLLSQRKEQAESLRLIDELaIKTPGPQA----AVSQLSGGNQQK 402
Cdd:cd03219 79 ------RTfQIPRLFpeLTVLENVMVAAQARtGSGLLLARARREEREARERAEEL-LERVGLADladrPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 403 VALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-245 |
2.70e-26 |
|
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: 106.86 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEE-FHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 164 FDEP-------SVALVKrevdqllRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAvveprHTSSAQIARlm 236
Cdd:cd03218 157 LDEPfagvdpiAVQDIQ-------KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA-----EGTPEEIAA-- 222
|
....*....
gi 2545433469 237 vNREVQEMY 245
Cdd:cd03218 223 -NELVRKVY 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-217 |
4.17e-26 |
|
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: 105.64 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGvq 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQreaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDE------ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHylQEIDSLCDEVTVLRNGR 217
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
5.14e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.03 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP--RQV--- 75
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPekRNVgmv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 ---DALgvqFIHqerllpasFTVGEALFFGHELRRGPfvdrrrqQREAERLLAEYFEL-QLP--ADALVGELNSAERQVL 149
Cdd:COG3842 83 fqdYAL---FPH--------LTVAENVAFGLRMRGVP-------KAEIRARVAELLELvGLEglADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 150 QITRALIRQPKILVFDEPSVAL---VKREV-DQLLRIVKRLrdqGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALdakLREEMrEELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-167 |
6.67e-26 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 103.11 E-value: 6.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAlGVQFIHQERLLPASFTVGEA 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 99 LFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEP 167
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
7.35e-26 |
|
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: 104.97 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGtIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyaalSPRQVDAL--GVQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD----VLKQPQKLrrRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVL-ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLrDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-225 |
8.32e-26 |
|
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: 105.50 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGaTLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPrqvDALGVQFI 83
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLE----IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 164 FDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-217 |
9.16e-26 |
|
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: 104.88 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGA----TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 --GVQFIHQE-RLLPaSFTVGE----ALFFGHELRRgpfvdrrRQQREAERLLaEYFELQLPADALVGELNSAERQVLQI 151
Cdd:cd03255 81 rrHIGFVFQSfNLLP-DLTALEnvelPLLLAGVPKK-------ERRERAEELL-ERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYlQEIDSLCDEVTVLRNGR 217
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-220 |
1.30e-25 |
|
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: 104.89 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL----GVQ 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FihQERLLPASFTVGEAL-FFGHELRRGPfvDRRRQQREAERLlaEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:cd03261 83 F--QSGALFDSLTVFENVaFPLREHTRLS--EEEIREIVLEKL--EAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 161 ILVFDEPSVAL---VKREVDQLLRivkRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03261 157 LLLYDEPTAGLdpiASGVIDDLIR---SLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-217 |
1.88e-25 |
|
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: 104.24 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP--RQVDAlgvq 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhkRPVNT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 fIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLA-EYFELQLPAdalvgELNSAERQVLQITRALIRQPK 160
Cdd:cd03300 77 -VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQlEGYANRKPS-----QLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-217 |
6.26e-25 |
|
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: 103.18 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKR-FGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQ-PYAAlSPRQVDALGVQFI 83
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKR-RKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERL---LPasftVGEALFFGHELRRGPFVDRRRQQREaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:cd03267 102 QKTQLwwdLP----VIDSFYLLAAIYDLPPARFKKRLDE----LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVAL---VKREVDQLLRIVKRLRdqGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03267 174 ILFLDEPTIGLdvvAQENIRNFLKEYNRER--GTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
269-471 |
7.50e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 102.16 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRSQGISP----- 343
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGLVFQNPDDQFFGPtveee 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLSVLENLtlaGLGRFSRWgllsQRKEQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03225 97 VAFGLENL---GLPEEEIE----ERVEEALELVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
257-475 |
8.94e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 100.58 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlaRRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIA 330
Cdd:cd03216 1 LELRGIT--KRFggvkalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPeerrsqgispllsvlenltlaglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavsQLSGGNQQKVALGKWLS 410
Cdd:cd03216 79 MVY------------------------------------------------------------QLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-217 |
1.36e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDA 77
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 L-----GvqFIHQE-RLLPaSFTVGEALFFGHELRRGPFVDRRRQQREaerlLAEYFELQLPADALVGELNSAERQVLQI 151
Cdd:COG1136 83 LrrrhiG--FVFQFfNLLP-ELTALENVALPLLLAGVSRKERRERARE----LLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLqEIDSLCDEVTVLRNGR 217
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-217 |
6.13e-24 |
|
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: 99.68 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVE---RGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPY------AALSPRQvdaLGVQFIHQERLL 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQ---RKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 90 PASFTVGEALFFGHELRRgPFVDRRRQQReaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:cd03297 87 FPHLNVRENLAFGLKRKR-NREDRISVDE-----LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545433469 170 ALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
6.90e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.60 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYaalsPRQVDA--L 78
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLarA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GVQFIHQERLLPASFTVGEAL-----FFGHELRRGPFVdrrrqqreaERLLAEYFELQLPADALVGELNSAERQVLQITR 153
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLlvfgrYFGMSTREIEAV---------IPSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 154 ALIRQPKILVFDEPSVALvkrevDQLLR--IVKRLRD---QGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTS 228
Cdd:PRK13536 186 ALINDPQLLILDEPTTGL-----DPHARhlIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
....
gi 2545433469 229 SAQI 232
Cdd:PRK13536 261 DEHI 264
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
1.10e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.69 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--G 79
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAArrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQE-RLLpASFTVGE--ALffghelrrgPF----VDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQIT 152
Cdd:COG1135 84 IGMIFQHfNLL-SSRTVAEnvAL---------PLeiagVPKAEIRKRVAELL-ELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 153 RALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGR---IVE 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-254 |
1.32e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQErllpAS-F---TVGE----ALffghELRRgpfVDRRRQQREAERLLAEyFELQ----LPADALVGelnsAERQV 148
Cdd:COG1137 81 GYLPQE----ASiFrklTVEDnilaVL----ELRK---LSKKEREERLEELLEE-FGIThlrkSKAYSLSG----GERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 149 LQITRALIRQPKILVFDEP-------SVALVKrevdqllRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAv 221
Cdd:COG1137 145 VEIARALATNPKFILLDEPfagvdpiAVADIQ-------KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLA- 216
|
250 260 270
....*....|....*....|....*....|...
gi 2545433469 222 veprHTSSAQIARlmvNREVQEMYpkaqveLGE 254
Cdd:COG1137 217 ----EGTPEEILN---NPLVRKVY------LGE 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.42e-23 |
|
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: 98.48 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFI 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD---IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELqlpaDALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLL----DRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 164 FDEPSVALvkrevDQLLRI-----VKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03301 154 MDEPLSNL-----DAKLRVqmraeLKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-223 |
3.06e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 103.76 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFG--ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALG 79
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VqfIHQERLLpasF--TVGEALFFGHelrrgPFVDRRRQQREAERLLAEYFELQLPA--DALVGE----LNSAERQVLQI 151
Cdd:COG2274 553 V--VLQDVFL---FsgTIRENITLGD-----PDATDEEIIEAARLAGLHDFIEALPMgyDTVVGEggsnLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRdQGLSILYISHYLQEIDsLCDEVTVLRNGRdvaVVE 223
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR-LADRIIVLDKGR---IVE 689
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-216 |
3.08e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 97.33 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 14 GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQfihqerllpasf 93
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQ------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFF---GHELRRGpfVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVA 170
Cdd:cd03226 79 DVDYQLFTdsvREELLLG--LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 171 LVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
268-473 |
3.20e-23 |
|
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: 97.59 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 268 YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaQGIALVPEERRsqgISPLLSV 347
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMVFQDYA---LFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLaGLGRfsrwGLLSQRKEQAESLRLIDELAIKTPGpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:cd03259 90 AENIAF-GLKL----RGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 428 GAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03259 164 KLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
4.12e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgV 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 161 ILVFDEPSVAL-VKREVdQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK09536 160 VLLLDEPTASLdINHQV-RTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-217 |
7.02e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPR------- 73
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrniamv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 74 -QVDALgvqFIHQerllpasfTVGEALFFGHELRRGP------FVDRrrqqreaerlLAEYFELQLPADALVGELNSAER 146
Cdd:COG3839 81 fQSYAL---YPHM--------TVYENIAFPLKLRKVPkaeidrRVRE----------AAELLGLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 147 QVLQITRALIRQPKILVFDEPSVALvkrevDQLLRI-----VKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNL-----DAKLRVemraeIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-472 |
1.01e-22 |
|
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: 101.30 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGA----TLALDDASLKVERGTIHGLVGENGAGKS----TLIKVLAGIHKADSGQVSIDGQPYAALSP 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 73 RQVDAL---GVQFIHQErllPAS-----FTVG----EALffghELRRGpfVDRRRQQREAERLLAeyfELQLP-----AD 135
Cdd:COG4172 84 RELRRIrgnRIAMIFQE---PMTslnplHTIGkqiaEVL----RLHRG--LSGAAARARALELLE---RVGIPdperrLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 136 ALVGELNSAERQVLQITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTV 212
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQILDLLKDLQ--RELGMALLLITHDLGVVRRFADRVAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 213 LRNGRdvaVVE----------PRHTSSAQ-IARLMVNRevqemyPKAQVELGEPLLQVRGLN---------LARRYRQ-- 270
Cdd:COG4172 230 MRQGE---IVEqgptaelfaaPQHPYTRKlLAAEPRGD------PRPVPPDAPPLLEARDLKvwfpikrglFRRTVGHvk 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 ----IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRAdSGSIHLEGR---------LLRLR--------------SP-- 321
Cdd:COG4172 301 avdgVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQdldglsrraLRPLRrrmqvvfqdpfgslSPrm 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 322 --GEAIAQG-----IALVPEERRSQgispllsVLENLTLAGLGRFSRWgllsqrkeqaeslRLIDElaiktpgpqaavsq 394
Cdd:COG4172 380 tvGQIIAEGlrvhgPGLSAAERRAR-------VAEALEEVGLDPAARH-------------RYPHE-------------- 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-226 |
1.19e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL---- 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GVqfIHQE-RLLPaSFTVGEALFFGHELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIR 157
Cdd:COG2884 82 GV--VFQDfRLLP-DRTVYENVALPLRVTG---KSRKEIRRRVREVL-DLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 158 QPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVEPRH 226
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR---LVRDEA 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-223 |
1.53e-22 |
|
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: 100.91 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAdSGQVSIDGQPYAALSPRQVDAL--GVQFIHQE 86
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRPLrrRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 87 rllP-ASF----TVGEALFFGHELRRgPFVDRRRQQREAERLLAeyfELQLPADAL---VGELNSAERQVLQITRALIRQ 158
Cdd:COG4172 371 ---PfGSLsprmTVGQIIAEGLRVHG-PGLSAAERRARVAEALE---EVGLDPAARhryPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 159 PKILVFDEPSVAL---VKREVDQLLRivkRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:COG4172 444 PKLLVLDEPTSALdvsVQAQILDLLR---DLqREHGLAYLFISHDLAVVRALAHRVMVMKDGK---VVE 506
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
1.88e-22 |
|
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: 96.31 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAG-IHKADSGQVSIDGQPYAALSPRQVDA-L 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKrI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GV--QFIHQErlLPASFTVGEAL---FFGHelrRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITR 153
Cdd:COG1119 81 GLvsPALQLR--FPRDETVLDVVlsgFFDS---IGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 154 ALIRQPKILVFDEPSVAL--VKREvdQLLRIVKRLRDQG-LSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:COG1119 156 ALVKDPELLILDEPTAGLdlGARE--LLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
269-475 |
1.96e-22 |
|
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: 95.51 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrLLRLRSPGEAiAQGIALVPEerrSQGISPLLSVL 348
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEA-RRRLGFVSD---STGLYDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLT-LAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTPGpqaavsqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:cd03266 97 ENLEyFAGLYGLKGDELTARLEELADRLGMEELLDRRVGG-------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 428 GAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
2.18e-22 |
|
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: 97.82 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKA---DSGQVSIDGQPYAALSPRQVD 76
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 AL---GVQFIHQErllPAS-----FTVGEALFFGHELRRGpfVDRRRQQREAERLLAEYfELQLPADALV---GELNSAE 145
Cdd:COG0444 82 KIrgrEIQMIFQD---PMTslnpvMTVGDQIAEPLRIHGG--LSKAEARERAIELLERV-GLPDPERRLDrypHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 146 RQVLQITRALIRQPKILVFDEPSVAL---VKREVDQLLrivKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaV 221
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALdvtIQAQILNLL---KDLQRElGLAILFITHDLGVVAEIADRVAVMYAGR---I 229
|
250
....*....|....*
gi 2545433469 222 VE----------PRH 226
Cdd:COG0444 230 VEegpveelfenPRH 244
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
3.62e-22 |
|
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: 93.22 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATL--ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGV 80
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 qfIHQERLLpASFTVGEALFFGhelrrGpfvdrrrqqreaerllaeyfelqlpadalvgelnsaERQVLQITRALIRQPK 160
Cdd:cd03228 81 --VPQDPFL-FSGTIRENILSG-----G------------------------------------QRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRdQGLSILYISHYLQEIDsLCDEVTVLRNGR 217
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
257-472 |
3.64e-22 |
|
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: 94.88 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlaRRY--------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIAQG 328
Cdd:cd03263 1 LQIRNLT--KTYkkgtkpavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERrsqGISPLLSVLENLTLaglgrFSR-WGlLSQRKEQAESLRLIDELAIKtpgPQA--AVSQLSGGNQQKVAL 405
Cdd:cd03263 77 LGYCPQFD---ALFDELTVREHLRF-----YARlKG-LPKSEIKEEVELLLRVLGLT---DKAnkRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 406 GKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVeEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-220 |
6.81e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 93.71 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPrqvDALGVQFIHQERLLPASFTVGEALFFG 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 103 HE--LRRGPfVDRRRQQREAERLLAEYFELQLPadalvGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLL 180
Cdd:cd03298 95 LSpgLKLTA-EDRQAIEVALARVGLAGLEKRLP-----GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2545433469 181 RIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03298 169 DLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
263-472 |
7.40e-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: 94.15 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaQGIALVPEER 336
Cdd:cd03218 5 NLSKRYGKrkvvngVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-------------QDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 RSQ-GISPL---------LSVLENLTLAGLGR-FSRWgllsQRKEQAESLrlIDELAIKTPGPQAAvSQLSGGNQQKVAL 405
Cdd:cd03218 72 RARlGIGYLpqeasifrkLTVEENILAVLEIRgLSKK----EREEKLEEL--LEEFHITHLRKSKA-SSLSGGERRRVEI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 406 GKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-220 |
7.47e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 7.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQFI 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-ARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGhelrRGPFVDRRRQQREAERLLA----EYFELQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYG----RSPWLSLWGRLSAEDNARVnqamEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 160 KILVFDEPSVAL-VKREVDqLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK11231 158 PVVLLDEPTTYLdINHQVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
8.01e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.18 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGhelrrGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG-----GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
258-472 |
3.50e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 90.96 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 258 QVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVP 333
Cdd:cd03214 1 EVENLSVGYGGRTVlddlSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 334 EerrsqgispllsVLENLTLAGLgrfsrwgllsqrkeqaeSLRLIDElaiktpgpqaavsqLSGGNQQKVALGKWLSRRS 413
Cdd:cd03214 80 Q------------ALELLGLAHL-----------------ADRPFNE--------------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 414 AVYLLDEPCVGVDVGAKVEIYRVIGRLV-EEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-245 |
4.15e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.26 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDD--LSAEQREDRANELMEE-FHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAvveprHTSSAQIarlMVNRE 240
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA-----HGTPTEI---LQDEH 229
|
....*
gi 2545433469 241 VQEMY 245
Cdd:PRK10895 230 VKRVY 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
255-469 |
6.04e-21 |
|
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: 91.00 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIAQGIA 330
Cdd:COG4133 1 MMLEAENLSCRRGERLLfsglSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE--PIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEErrsQGISPLLSVLENLTLAGlgrfsrwGLLSQRKEQAESLRLIDELAIkTPGPQAAVSQLSGGNQQKVALGKWLS 410
Cdd:COG4133 79 YLGHA---DGLKPELTVRENLRFWA-------ALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGicDRILVLHR 469
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
6.11e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDA-LGVqf 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASFTVGEALFFGHELRRGPFVDrrrqqreaerllaeyfELQLPADAL--VG----------ELNSAERQVLQ 150
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSSAAQ----------------DRQIVREALalVGlahlagrsyqTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 151 ITRALI-------RQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-225 |
7.36e-21 |
|
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: 92.32 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL-----GVQFI 83
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkiSMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQErLLPaSFTVGEALFFGHELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:cd03294 110 SFA-LLP-HRTVLENVAFGLEVQG---VPRAEREERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 164 FDEPSVAL---VKREV-DQLLRIVkrlRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:cd03294 184 MDEAFSALdplIRREMqDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-472 |
1.15e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQpyaalsprqvdaLGVQFIHQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEALFFGHE-----LRRgpFVDRRRQQREAERLLAEYFELQ--------------------------LPA 134
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAelralEAE--LEELEAKLAEPDEDLERLAELQeefealggweaearaeeilsglgfpeEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 135 DALVGELNSAERQVLQITRALIRQPKILVFDEP-------SVAlvkrevdqLLRivKRLRDQGLSILYISH--YLqeIDS 205
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPtnhldleSIE--------WLE--EFLKNYPGTVLVVSHdrYF--LDR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 206 LCDEVTVLRNGRdvavVEP--------------------------------------------RHTSSAQ--IARL--MV 237
Cdd:COG0488 215 VATRILELDRGK----LTLypgnysayleqraerleqeaaayakqqkkiakeeefirrfrakaRKAKQAQsrIKALekLE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 238 NREVQ------EMYPKAQVELGEPLLQVRGLNLA---RR-YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSG 307
Cdd:COG0488 291 REEPPrrdktvEIRFPPPERLGKKVLELEGLSKSygdKTlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 308 SIHLeGRLLRlrspgeaiaqgIALVPEERRSqgISPLLSVLENLTLAG-----------LGRFsrwgLLSQrkEQAESLr 376
Cdd:COG0488 371 TVKL-GETVK-----------IGYFDQHQEE--LDPDKTVLDELRDGApggteqevrgyLGRF----LFSG--DDAFKP- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 377 lidelaiktpgpqaaVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKvEIyrvigrLVE-----EGAAVLVlS 451
Cdd:COG0488 430 ---------------VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL-EA------LEEalddfPGTVLLV-S 486
|
570 580
....*....|....*....|..
gi 2545433469 452 SDlPELL-GICDRILVLHRGEI 472
Cdd:COG0488 487 HD-RYFLdRVATRILEFEDGGV 507
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
140-472 |
1.58e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 140 ELNSAERQVLQITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALdvsVQAQILQLLRELQ--QELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 217 RdvaVVEPRHT----SSAQIA--RLMVNREvQEMYPKAQVELGEPLLQVRGLNLARRYRQ---------------IDLEL 275
Cdd:PRK15134 234 R---CVEQNRAatlfSAPTHPytQKLLNSE-PSGDPVPLPEPASPLLDVEQLQVAFPIRKgilkrtvdhnvvvknISFTL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 276 RRGEIVGLTGLVGSGAKDLLKTLFGVVRAdSGSIHLEGRLLRLRSPGEaiaqgiaLVPEERRSQ--------GISPLLSV 347
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQ-------LLPVRHRIQvvfqdpnsSLNPRLNV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LEnLTLAGLGRFSRwgLLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:PRK15134 382 LQ-IIEEGLRVHQP--TLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2545433469 428 GAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK15134 459 TVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-219 |
1.60e-20 |
|
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: 90.71 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGA-TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQ- 81
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 -FIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLA----EYFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:cd03256 81 gMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRAlaalERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-217 |
1.63e-20 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 90.10 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQ--- 81
Cdd:TIGR02211 7 LGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKklg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGE----ALFFGHElrrgpfvDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIR 157
Cdd:TIGR02211 87 FIYQFHHLLPDFTALEnvamPLLIGKK-------SVKEAKERAYEML-EKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 158 QPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLcDEVTVLRNGR 217
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELAKKL-DRVLEMKDGQ 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
269-471 |
1.75e-20 |
|
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: 88.07 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlRSPGEAIAQGIALVPeerrsqgispllsvl 348
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 enltlaglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVG 428
Cdd:cd00267 80 ---------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545433469 429 AKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-466 |
2.35e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.49 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 26 VERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQ----VSIDG----------QPY-AALSPRQVD-ALGVQFIHQerlL 89
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeePSWDEvlkrfrgtelQNYfKKLYNGEIKvVHKPQYVDL---I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 90 PASF--TVGEALFFGHElrRGPFVDrrrqqreaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEP 167
Cdd:PRK13409 173 PKVFkgKVRELLKKVDE--RGKLDE-----------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 168 SVALvkrEVDQLLRIVKRLRD--QGLSILYISHYLQEIDSLCDEVTVL----------------RNG------------- 216
Cdd:PRK13409 240 TSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVLDYLADNVHIAygepgaygvvskpkgvRVGineylkgylpeen 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 217 ---RDVAVVEPRHTSSAQiarlmVNREVQEMYPKAQVELGEPLLQVRGLnlarryrqidlELRRGEIVGLTGLVGSGAKD 293
Cdd:PRK13409 317 mriRPEPIEFEERPPRDE-----SERETLVEYPDLTKKLGDFSLEVEGG-----------EIYEGEVIGIVGPNGIGKTT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 294 LLKTLFGVVRADSGSIHLEGRllrlrspgeaiaqgIALVPeerrsQGISP--LLSVLENLTLAGlGRF-SRWgllsQRKE 370
Cdd:PRK13409 381 FAKLLAGVLKPDEGEVDPELK--------------ISYKP-----QYIKPdyDGTVEDLLRSIT-DDLgSSY----YKSE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 371 QAESLRLIDELaiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLV 449
Cdd:PRK13409 437 IIKPLQLERLL-------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALV 509
|
490
....*....|....*..
gi 2545433469 450 LSSDLPELLGICDRILV 466
Cdd:PRK13409 510 VDHDIYMIDYISDRLMV 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-466 |
2.40e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 94.47 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 27 ERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG--------------QPY----------AALSPRQVDalgvqf 82
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfrgtelQDYfkklangeikVAHKPQYVD------ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 ihqerLLPASF--TVGEALFFGHElrRGPFVDrrrqqreaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:COG1245 171 -----LIPKVFkgTVRELLEKVDE--RGKLDE-----------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVALvkrEVDQLL---RIVKRLRDQGLSILYISHYLQEIDSLCDEVTVL----------------RNG----- 216
Cdd:COG1245 233 FYFFDEPSSYL---DIYQRLnvaRLIRELAEEGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksvRVGinqyl 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 217 -----------RDVAVVEPRHTSSAQiarlmVNREVQEMYPKAQVELGEPLLQVRGLnlarryrqidlELRRGEIVGLTG 285
Cdd:COG1245 310 dgylpeenvriRDEPIEFEVHAPRRE-----KEEETLVEYPDLTKSYGGFSLEVEGG-----------EIREGEVLGIVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 286 LVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeaiaqgIALVPeerrsQGISPL--LSVLENLTLAGLGRF-SRW 362
Cdd:COG1245 374 PNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKP-----QYISPDydGTVEEFLRSANTDDFgSSY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 363 gllsqrkEQAEslrLIDELAIKtPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVE 442
Cdd:COG1245 435 -------YKTE---IIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
490 500
....*....|....*....|....*
gi 2545433469 443 E-GAAVLVLSSDLPELLGICDRILV 466
Cdd:COG1245 504 NrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-226 |
2.53e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 91.72 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-----------GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 73 RQVDAL--GVQFIHQErllP-AS----FTVGEALFFG---HELrrgpfVDRRRQQREAERLLaeyfelqlpadALVG--- 139
Cdd:COG4608 88 RELRPLrrRMQMVFQD---PyASlnprMTVGDIIAEPlriHGL-----ASKAERRERVAELL-----------ELVGlrp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 140 --------ELNSAERQVLQITRALIRQPKILVFDEPSVALvkrevD-----QLLRIVKRLRDQ-GLSILYISHYLQEIDS 205
Cdd:COG4608 149 ehadryphEFSGGQRQRIGIARALALNPKLIVCDEPVSAL-----DvsiqaQVLNLLEDLQDElGLTYLFISHDLSVVRH 223
|
250 260 270
....*....|....*....|....*....|.
gi 2545433469 206 LCDEVTVLRNGRdvaVVE----------PRH 226
Cdd:COG4608 224 ISDRVAVMYLGK---IVEiaprdelyarPLH 251
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
263-471 |
3.17e-20 |
|
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: 88.01 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLlrlrspgeaIAQGIALVPEER 336
Cdd:cd03229 5 NVSKRYgqktvlNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED---------LTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 RSQGIS-------PLLSVLENLTLAglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavsqLSGGNQQKVALGKWL 409
Cdd:cd03229 76 RRIGMVfqdfalfPHLTVLENIALG----------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 410 SRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-220 |
3.21e-20 |
|
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: 89.19 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAlGVQFIHQErllpasftv 95
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQD--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 gEALFFGhELR-----RGPFVDRRRQQREAERLLAEYFELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVF 164
Cdd:cd03245 87 -VTLFYG-TLRdnitlGAPLADDERILRAAELAGVTDFVNKHPNglDLQIGErgrgLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 165 DEPSVALVKR-EVdqllRIVKRLRdQGLS---ILYISHYlQEIDSLCDEVTVLRNGRDVA 220
Cdd:cd03245 165 DEPTSAMDMNsEE----RLKERLR-QLLGdktLIIITHR-PSLLDLVDRIIVMDSGRIVA 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
254-472 |
3.44e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRglNLARRYRQ------IDLELRRGEIVGLTGLVGSGakdllK-TLF----GVVRADSGSIHLEGrllrlrspg 322
Cdd:COG1137 1 MMTLEAE--NLVKSYGKrtvvkdVSLEVNQGEIVGLLGPNGAG-----KtTTFymivGLVKPDSGRIFLDG--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 323 eaiaQGIALVPEERRSQ-GISPL---------LSVLEN----LTLAGLGRfsrwgllSQRKEQAESlrLIDELAI----K 384
Cdd:COG1137 65 ----EDITHLPMHKRARlGIGYLpqeasifrkLTVEDNilavLELRKLSK-------KEREERLEE--LLEEFGIthlrK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 385 TPGpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRI 464
Cdd:COG1137 132 SKA-----YSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRA 206
|
....*...
gi 2545433469 465 LVLHRGEI 472
Cdd:COG1137 207 YIISEGKV 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
263-472 |
3.44e-20 |
|
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: 88.88 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspGEAIAQGIALVPEER 336
Cdd:cd03269 5 NVTKRFGRvtalddISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsqGISPLLSVLENL----TLAGLGRfsrwgllsqRKEQAESLRLIDELAIkTPGPQAAVSQLSGGNQQKVALGKWLSRR 412
Cdd:cd03269 80 ---GLYPKMKVIDQLvylaQLKGLKK---------EEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
268-421 |
3.68e-20 |
|
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: 86.93 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 268 YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgEAIAQGIALVPEERRsqgISPLLSV 347
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDPQ---LFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 348 LENLTLAGLGRFsrwglLSQRKEQAESLRLIDELAI----KTPgPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEP 421
Cdd:pfam00005 77 RENLRLGLLLKG-----LSKREKDARAEEALEKLGLgdlaDRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-217 |
4.13e-20 |
|
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: 88.62 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 11 KRFGA-TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL----GVQFihQ 85
Cdd:cd03292 8 KTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkiGVVF--Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAeyfeLQLPADALVGELNSAERQVLQITRALIRQPKILVFD 165
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVG----LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 166 EPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-226 |
4.55e-20 |
|
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: 88.78 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKA-----DSGQVSIDGQPYAALSPRqVDAL-- 78
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVD-VLELrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GVQFIHQeRLLPASFTVGEALFFG---HELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGElnsaERQVLQITRAL 155
Cdd:cd03260 82 RVGMVFQ-KPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGG----QQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 156 IRQPKILVFDEPSVAL---VKREVDQLLRivkRLRDQgLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:cd03260 157 ANEPEVLLLDEPTSALdpiSTAKIEELIA---ELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-223 |
5.24e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.02 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--G 79
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQERLLPASFTVGEALFFGHELRRgpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAG---TPKAEIKARVTELL-ELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 160 KILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGR---LVE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
271-472 |
6.05e-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: 88.08 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL----RLRSPGeaiaqgiaLVPEERRSQGISPllS 346
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakeRRKSIG--------YVMQDVDYQLFTD--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTLaGLGRfsrwglLSQRKEQAES-LRLIDELAIKTPGPQAavsqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGV 425
Cdd:cd03226 89 VREELLL-GLKE------LDAGNEQAETvLKDLDLYALKERHPLS----LSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 426 DVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-224 |
6.93e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQFI 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFG--HELRRGPFvdrrrqqreaERLL-------AEYFELQLPADAL--VGELNSAERQV---- 148
Cdd:PRK11300 86 FQHVRLFREMTVIENLLVAqhQQLKTGLF----------SGLLktpafrrAESEALDRAATWLerVGLLEHANRQAgnla 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 149 ------LQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAV 221
Cdd:PRK11300 156 ygqqrrLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
...
gi 2545433469 222 VEP 224
Cdd:PRK11300 236 GTP 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
256-480 |
7.11e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 88.71 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 256 LLQVRGLNLARRY--------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGeAIAQ 327
Cdd:COG1124 1 MLEVRNLSVSYGQggrrvpvlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK-AFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 328 GIALVPEERRSqGISPLLSVLENLT--LAGLGRFSRWgllSQRKEQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVAL 405
Cdd:COG1124 80 RVQMVFQDPYA-SLHPRHTVDRILAepLRIHGLPDRE---ERIAELLEQVGLPPSFLDRYP------HQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 406 GKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGE 480
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
255-472 |
7.77e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.44 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSpGEAIAQGIA 330
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVldgvDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEERRSQGISPLLSVLENLTLAGLGRFSRWG-----LLSQRKEQAESLRLIDElaiktpgpqaAVSQLSGGNQQKVAL 405
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTetdraAVERAMERTGVAQFADR----------PVTSLSGGERQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 406 GKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
257-475 |
9.67e-20 |
|
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: 88.33 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIaqgialv 332
Cdd:cd03261 1 IELRGLTKSFGGRTVlkgvDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 pEERRSQGI----SPL---LSVLENLTLaglgrfsrwgLLsqRKEQAESLRLIDELAIKTPG----PQAA---VSQLSGG 398
Cdd:cd03261 74 -RLRRRMGMlfqsGALfdsLTVFENVAF----------PL--REHTRLSEEEIREIVLEKLEavglRGAEdlyPAELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 399 NQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-224 |
1.51e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.28 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFI 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLaeyfELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLV----HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 164 FDEPSVALVKREVDQL-LRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-220 |
1.89e-19 |
|
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: 89.77 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 8 HLRKRFGAtLALDdASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYA------ALSPRQvDALGVQ 81
Cdd:COG4148 6 DFRLRRGG-FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHR-RRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FihQE-RLLPAsFTVGEALFFGHelRRGPFVDRRRQQREAERLLAeyFE--LQLPADALVGelnsAERQVLQITRALIRQ 158
Cdd:COG4148 83 F--QEaRLFPH-LSVRGNLLYGR--KRAPRAERRISFDEVVELLG--IGhlLDRRPATLSG----GERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 159 PKILVFDEPSVAL---VKREvdqLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:COG4148 152 PRLLLMDEPLAALdlaRKAE---ILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
269-472 |
2.38e-19 |
|
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: 86.77 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaqgiaLVPEERRSQGIS------ 342
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-------LAAFRRRHIGFVfqsfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 -PLLSVLENLTLAGLGRFSRWgllSQRKEQAESL--RL-IDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:cd03255 94 lPDLTALENVELPLLLAGVPK---KERRERAEELleRVgLGDRLNHYP------SELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 419 DEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDlPELLGICDRILVLHRGEI 472
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
270-475 |
2.44e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIALVPEERRsqgISPLLSVLE 349
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 NLTLAGLgrFSRWGLLSQRKEQAESL--RLIDELAIKTpgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:PRK11614 100 NLAMGGF--FAERDQFQERIKWVYELfpRLHERRIQRA-------GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 428 GAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
270-474 |
3.16e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 86.19 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRrGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSpgeaiaQGIALVPEERR------SQGISP 343
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSR------KKINLPPQQRKiglvfqQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLSVLENLTLaGLGRFSRWGLLSQRKEQAESLRLiDELAiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03297 89 HLNVRENLAF-GLKRKRNREDRISVDELLDLLGL-DHLL------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAG 474
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
271-473 |
3.83e-19 |
|
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: 86.47 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG---------RLLRLRSPGEAIAQGIALVPEerrsqgi 341
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkALRQLRRQIGMIFQQFNLIER------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 342 splLSVLENLTLAGLGRFSRW-GLLSQ--RKEQAESLRLIDELAIKTPGPQAAvSQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:cd03256 93 ---LSVLENVLSGRLGRRSTWrSLFGLfpKEEKQRALAALERVGLLDKAYQRA-DQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 419 DEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-217 |
3.89e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG-QPYaalsPRQVDAL---GVQFIHQERL---LP 90
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPF----KRRKEFArriGVVFGQRSQLwwdLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 91 A--SFTVGEALF------FGHELRRgpfvdrrrqqreaerlLAEYFELQlpadalvGELNSAERQV-------LQITRAL 155
Cdd:COG4586 113 AidSFRLLKAIYripdaeYKKRLDE----------------LVELLDLG-------ELLDTPVRQLslgqrmrCELAAAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 156 IRQPKILVFDEPSVAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:COG4586 170 LHRPKILFLDEPTIGLdvvSKEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-219 |
3.89e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKaDSGQVSID-----GQPYAALS 71
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADrfrwnGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 72 P---RQVDALGVQFIHQE--RLLPASFTVGEAL--------FFGHELRRgpfvdrrrqqreaerllaeYFELQLPADAL- 137
Cdd:COG4170 80 PrerRKIIGREIAMIFQEpsSCLDPSAKIGDQLieaipswtFKGKWWQR-------------------FKWRKKRAIELl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 138 --VG-------------ELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQ 201
Cdd:COG4170 141 hrVGikdhkdimnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLE 220
|
250
....*....|....*...
gi 2545433469 202 EIDSLCDEVTVLRNGRDV 219
Cdd:COG4170 221 SISQWADTITVLYCGQTV 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-217 |
4.60e-19 |
|
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: 85.30 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAG--IHKADSGQVSIDGQPYAALSPRQVdalgVQFIHQERLLPASFTVG 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 97 EALFFGHELRRgpfvdrrrqqreaerllaeyfelqlpadalvgeLNSAERQVLQITRALIRQPKILVFDEPSVALVKREV 176
Cdd:cd03213 101 ETLMFAAKLRG---------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2545433469 177 DQLLRIVKRLRDQGLSILYISHYL-QEIDSLCDEVTVLRNGR 217
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
271-487 |
9.13e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 9.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRS-QGISpllsVLE 349
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQHHLTpEGIT----VRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 nltLAGLGR---FSRWGLLSQRK----EQAESLRLIDELAIKtpgpqaAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPC 422
Cdd:PRK11231 96 ---LVAYGRspwLSLWGRLSAEDnarvNQAMEQTRINHLADR------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 423 VGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGSDQLL 487
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
256-472 |
1.16e-18 |
|
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: 84.86 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 256 LLQVRGLNLARRYRQ--------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQ 327
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkalddVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 328 G--IALVPEERRSQgISPLLSVLENLTLAglgrfsrwgLLSQRKE--QAESLRLIDELAIKTPGPQAAV----SQLSGGN 399
Cdd:cd03257 81 RkeIQMVFQDPMSS-LNPRMTIGEQIAEP---------LRIHGKLskKEARKEAVLLLLVGVGLPEEVLnrypHELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 400 QQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
257-472 |
1.24e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlaRRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspGEAIAQGIA 330
Cdd:COG4152 2 LELKGLT--KRFgdktavDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEERrsqGISPLLSVLENLT-LAGLgrfsrWGLlSQRKEQAESLRLIDELAIKtPGPQAAVSQLSGGNQQKVALGKWL 409
Cdd:COG4152 75 YLPEER---GLYPKMKVGEQLVyLARL-----KGL-SKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 410 SRRSAVYLLDEPCVGVD-VGAKVeIYRVIGRLVEEGAAVLvLSS---DLPELLgiCDRILVLHRGEI 472
Cdd:COG4152 145 LHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAKGTTVI-FSShqmELVEEL--CDRIVIINKGRK 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-213 |
1.54e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP---RQvdalGV 80
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyRQ----QV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQErllPASF--TVGEALFFGHELRRgpfvdrrrQQREAERLLAEYFELQLPADAL---VGELNSAERQVLQITRAL 155
Cdd:PRK10247 84 SYCAQT---PTLFgdTVYDNLIFPWQIRN--------QQPDPAIFLDDLERFALPDTILtknIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 156 IRQPKILVFDEPSVAL---VKREVDQLlrIVKRLRDQGLSILYISHYLQEIDSlCDEVTVL 213
Cdd:PRK10247 153 QFMPKVLLLDEITSALdesNKHNVNEI--IHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
263-480 |
1.63e-18 |
|
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: 84.34 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrLLRLRSPGEaIAQGIALVPEER 336
Cdd:cd03265 5 NLVKKYgdfeavRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-HDVVREPRE-VRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsqGISPLLSVLENLT----LAGLGRFSRwgllsqRKEQAESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGKWLSRR 412
Cdd:cd03265 83 ---SVDDELTGWENLYiharLYGVPGAER------RERIDELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGE 480
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
254-475 |
2.07e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 83.94 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNlaRRYRQ----------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR--------- 314
Cdd:COG1136 2 SPLLELRNLT--KSYGTgegevtalrgVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 315 LLRLRspGEAIA---QGIALVPEerrsqgisplLSVLENLTLAG-LGRFSRwgllSQRKEQAESL--RL-IDELAIKTPg 387
Cdd:COG1136 80 LARLR--RRHIGfvfQFFNLLPE----------LTALENVALPLlLAGVSR----KERRERARELleRVgLGDRLDHRP- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 388 pqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDlPELLGICDRILV 466
Cdd:COG1136 143 -----SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIR 216
|
....*....
gi 2545433469 467 LHRGEIAGE 475
Cdd:COG1136 217 LRDGRIVSD 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
263-472 |
2.56e-18 |
|
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: 83.46 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaQGIALVPEer 336
Cdd:cd03301 5 NVTKRFgnvtalDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMVFQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rSQGISPLLSVLENLTLA-GLGRFSRWGLLSQRKEQAESLRlIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:cd03301 80 -NYALYPHMTVYDNIAFGlKLRKVPKDEIDERVREVAELLQ-IEHLLDRKP------KQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-220 |
3.27e-18 |
|
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: 87.51 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQ 81
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASfTVGEALFFGH------ELRR-------GPFVDrrrqqreaerllaeyfelQLPA--DALVGE----LN 142
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGRpdasdeELEAaleaaglDEFVA------------------ALPDglDTPLGEggrgLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 143 SAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRdQGLSILYISHYLQEIDsLCDEVTVLRNGRDVA 220
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLA-QADRILVLDDGRIVE 551
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-217 |
3.32e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 83.35 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAAlSPRQVDAL--GVQ 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRGpfVDRRRQQREAERLLAeyfELQLP--ADALVGELNSAERQVLQITRALIRQP 159
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLE---KVGLAdkADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 160 KILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
269-477 |
5.27e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 82.90 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIA---QGIALVPeerrsqgispLL 345
Cdd:cd03293 21 EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--PVTGPGPDRGyvfQQDALLP----------WL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLEN----LTLAGLGRfsrwgllSQRKEQAES-LRLI--DELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:cd03293 89 TVLDNvalgLELQGVPK-------AEARERAEElLELVglSGFENAYP------HQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 419 DEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVL--HRGEIAGEFH 477
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-228 |
5.50e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.88 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGaTLALDdASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP--RQVDALgvq 81
Cdd:COG3840 2 LRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeRPVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FihQERLLPASFTVGEALFFGheLRRGPFVDRRRQQREAERL----LAEYfelqlpADALVGELNSAERQVLQITRALIR 157
Cdd:COG3840 77 F--QENNLFPHLTVAQNIGLG--LRPGLKLTAEQRAQVEQALervgLAGL------LDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 158 QPKILVFDEPSVAL---VKREvdqLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVEPRHTS 228
Cdd:COG3840 147 KRPILLLDEPFSALdpaLRQE---MLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGR---IAADGPTA 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-217 |
6.79e-18 |
|
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: 82.66 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQERLLpASFTVGE 97
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQDTFL-FSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 98 ALFFGHelrrgPFVDRRRQQREAERLLAEYFELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEpSVAL 171
Cdd:cd03254 96 NIRLGR-----PNATDEEVIEAAKEAGAHDFIMKLPNgyDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDE-ATSN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 172 VKREVDQLL-RIVKRLRDQGLSILyISHYLQEI-DSlcDEVTVLRNGR 217
Cdd:cd03254 170 IDTETEKLIqEALEKLMKGRTSII-IAHRLSTIkNA--DKILVLDDGK 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-220 |
7.62e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDA-LGV 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 qfIHQERLLPASFTVGEALFFGhelrRGPFvdrRRQQREAERLLAEYFElQLPADALVG----ELNSAERQVLQITRALI 156
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMG----RAPH---GLSRAEDDALVAAALA-QVDLAHLAGrdypQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 157 R------QPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK13548 151 QlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
1.01e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 85.97 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRF--GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALg 79
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQErllPASF--TVGEALFFG------HELRR-------GPFVDrrrqqreaerllaeyfelQLPA--DALVGE-- 140
Cdd:COG4987 411 IAVVPQR---PHLFdtTLRENLRLArpdatdEELWAalervglGDWLA------------------ALPDglDTWLGEgg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 141 --LNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLrDQGLSILYISHYLQEIDsLCDEVTVLRNGRD 218
Cdd:COG4987 470 rrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLE-RMDRILVLEDGRI 547
|
..
gi 2545433469 219 VA 220
Cdd:COG4987 548 VE 549
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-219 |
2.34e-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: 81.38 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGA--TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP----RQVdalG 79
Cdd:cd03252 3 FEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrRQV---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VqfIHQERLLpASFTVGEALFFGHelrrgPFVDRRRQQREAERLLAEYFELQLPA--DALVGE----LNSAERQVLQITR 153
Cdd:cd03252 80 V--VLQENVL-FNRSIRDNIALAD-----PGMSMERVIEAAKLAGAHDFISELPEgyDTIVGEqgagLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDqGLSILYISHYLQEIDSlCDEVTVLRNGRDV 219
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
2.75e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGV-------QFIhqer 87
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKIGIifqnpdnQFI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 llpaSFTVGEALFFGHELRRGPF------VDRRRQQREAERLLAeyFELQlpadalvgELNSAERQVLQITRALIRQPKI 161
Cdd:PRK13632 98 ----GATVEDDIAFGLENKKVPPkkmkdiIDDLAKKVGMEDYLD--KEPQ--------NLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGL-SILYISHYLQEIdSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKE 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
269-467 |
3.77e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHlegrllrlRSPGEaiaqGIALVPEerRSQGISPL-LSV 347
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGA----RVAYVPQ--RSEVPDSLpLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LEnltLAGLGRFSRWGLL-----SQRKEQAESL-RL-IDELAiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:NF040873 75 RD---LVAMGRWARRGLWrrltrDDRAAVDDALeRVgLADLA------GRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 421 PCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDlPELLGICDRILVL 467
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-217 |
3.89e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI--HKADSGQVSIDGQPYAALSPRQVDALGVQFIHQErllPASF--- 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQY---PVEIpgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRRGPFVDRRRQQREAERLLAEyfeLQLPADALVGELNSA----ERQVLQITRALIRQPKILVFDEPSV 169
Cdd:COG0396 93 SVSNFLRTALNARRGEELSAREFLKLLKEKMKE---LGLDEDFLDRYVNEGfsggEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 170 ALvkrEVDQLlRIV----KRLRDQGLSILYISHY---LQEIDslCDEVTVLRNGR 217
Cdd:COG0396 170 GL---DIDAL-RIVaegvNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGR 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-236 |
4.25e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.46 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFI 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLL-AEYFElqlpaDALVGELNSAERQVLQITRALIRQPKIL 162
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdLAGFE-----DRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 163 VFDEPSVALvkrevDQLLRivKRLRD------QGLSI--LYISHYLQEIDSLCDEVTVLRNGRDVAVVEP----RHTSSA 230
Cdd:PRK11432 159 LFDEPLSNL-----DANLR--RSMREkirelqQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPqelyRQPASR 231
|
....*.
gi 2545433469 231 QIARLM 236
Cdd:PRK11432 232 FMASFM 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-223 |
4.98e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.06 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 14 GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVqfIHQERLLpAS 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLrRQIGV--VPQDTFL-FS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 93 FTVGEALFFGH------ELRR-------GPFVDrrrqqreaerllaeyfelQLPA--DALVGE----LNSAERQVLQITR 153
Cdd:COG1132 428 GTIRENIRYGRpdatdeEVEEaakaaqaHEFIE------------------ALPDgyDTVVGErgvnLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 154 ALIRQPKILVFDEPSVAL-VKREVdqllRIVKRLRD--QGLSILYISHYLQEIdSLCDEVTVLRNGRdvaVVE 223
Cdd:COG1132 490 ALLKDPPILILDEATSALdTETEA----LIQEALERlmKGRTTIVIAHRLSTI-RNADRILVLDDGR---IVE 554
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-243 |
7.98e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF---------GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALS 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 72 PRQVDAL--GVQFIHQERL--LPASFTVGEALffGHELRRGPFVDRRRQQREAERLLaEYFELQLP-ADALVGELNSAER 146
Cdd:PRK10419 81 RAQRKAFrrDIQMVFQDSIsaVNPRKTVREII--REPLRHLLSLDKAERLARASEML-RAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 147 QVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVEPR 225
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ---IVETQ 234
|
250
....*....|....*...
gi 2545433469 226 HTSSAQIARLMVNREVQE 243
Cdd:PRK10419 235 PVGDKLTFSSPAGRVLQN 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
253-475 |
8.08e-17 |
|
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: 79.64 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 253 GEPLLQVRGLNLARR----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQg 328
Cdd:COG1127 2 SEPMIEVRNLTKSFGdrvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 ialvpeeRRSQGI----SPL---LSVLENLTLaGLGRFSRwglLSQrkeqaeslRLIDELAI-------------KTPgp 388
Cdd:COG1127 81 -------RRRIGMlfqgGALfdsLTVFENVAF-PLREHTD---LSE--------AEIRELVLeklelvglpgaadKMP-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 389 qaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD-VGAKVeIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILV 466
Cdd:COG1127 140 ----SELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV 214
|
....*....
gi 2545433469 467 LHRGEIAGE 475
Cdd:COG1127 215 LADGKIIAE 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
271-492 |
8.39e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.95 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADS--GSIHLEGRLLRLRSPGEAIAQGIALVPEErrsQGISPLLSVL 348
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQE---LTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLAGL----GRFSRWGLLSQRKEQaeslrLIDELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:TIGR02633 97 ENIFLGNEitlpGGRMAYNAMYLRAKN-----LLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 425 VDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGSDQLLACATG 492
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
263-472 |
1.01e-16 |
|
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: 79.69 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEA----IAQGIALV 332
Cdd:cd03296 7 NVSKRFgdfvalDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERnvgfVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 PEerrsqgisplLSVLENLTLaGL---GRFSRWGLLSQRKEQAESLRLI--DELAIKTPgpqaavSQLSGGNQQKVALGK 407
Cdd:cd03296 87 RH----------MTVFDNVAF-GLrvkPRSERPPEAEIRAKVHELLKLVqlDWLADRYP------AQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 408 WLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
271-472 |
1.18e-16 |
|
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: 78.73 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrlLRLRSPGEAIAqgialvpEERRSQGIS-------P 343
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDG--LKLTDDKKNIN-------ELRQKVGMVfqqfnlfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLSVLENLTLAglgrfSRWGLLSQRKE-QAESLRLIDELAIKtpgPQAAV--SQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:cd03262 90 HLTVLENITLA-----PIKVKGMSKAEaEERALELLEKVGLA---DKADAypAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 421 PCVGVD---VGakvEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03262 162 PTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-198 |
1.78e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPY---AALSPRQVDAL- 78
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 ---GVQFiHQERLLPaSFTVGEALFFGHELRRGpfVDRRRQQREAERLLAeyfELQLP--ADALVGELNSAERQVLQITR 153
Cdd:PRK11124 82 rnvGMVF-QQYNLWP-HLTVQQNLIEAPCRVLG--LSKDQALARAEKLLE---RLRLKpyADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISH 198
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
269-472 |
2.17e-16 |
|
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: 78.53 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgeaIAQGIALVPEErrsQGISPLLSVL 348
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVPQN---YALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLA-GLGRFSRWGLLSQRKEQAESLRlIDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:cd03299 90 KNIAYGlKKRKVDKKEIERKVLEIAEMLG-IDHLLNRKPE------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 428 GAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03299 163 RTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
271-472 |
2.57e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 78.05 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRL---RSPGEAIAQGIALVPEerrsqgisplLS 346
Cdd:cd03300 19 VSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLpphKRPVNTVFQNYALFPH----------LT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLEN----LTLAGLGRfsrwglLSQRKEQAESLRLI--DELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:cd03300 89 VFENiafgLRLKKLPK------AEIKERVAEALDLVqlEGYANRKP------SQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 421 PCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-223 |
4.54e-16 |
|
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: 77.15 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVqfIHQER 87
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISI--IPQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 LLpasftvgealFFGhELR-----RGPFVDRRRQQREAERLLAEYFELQ---LPADALVGELN-SA-ERQVLQITRALIR 157
Cdd:cd03244 88 VL----------FSG-TIRsnldpFGEYSDEELWQALERVGLKEFVESLpggLDTVVEEGGENlSVgQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 158 QPKILVFDEPSvALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSlCDEVTVLRNGRdvaVVE 223
Cdd:cd03244 157 KSKILVLDEAT-ASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGR---VVE 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-198 |
4.94e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.44 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 11 KRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQpyAALSPRQVDAL-----GVQFiHQ 85
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL--KVNDPKVDERLirqeaGMVF-QQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPaSFTVGEALFFGHELRRGpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKILVFD 165
Cdd:PRK09493 86 FYLFP-HLTALENVMFGPLRVRG--ASKEEAEKQARELLAK-VGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2545433469 166 EPSVAL---VKREVdqlLRIVKRLRDQGLSILYISH 198
Cdd:PRK09493 162 EPTSALdpeLRHEV---LKVMQDLAEEGMTMVIVTH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
271-475 |
8.30e-16 |
|
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: 78.62 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspgEAIAQGIALVPEERR------SQGISPL 344
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL------FDSRKGIFLPPEKRRigyvfqEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 LSVLENLtLAGLgRFSRWGLLSQRKEQAESLRLIDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:TIGR02142 90 LSVRGNL-RYGM-KRARPSERRISFERVIELLGIGHLLGRLPG------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 425 VDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-217 |
9.52e-16 |
|
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: 76.32 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRF------GATL-ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI--DGQP--YAAL 70
Cdd:COG4778 3 TLLEVENLSKTFtlhlqgGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWvdLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 71 SPRQV-----DALG-V-QFIhqeRLLP---ASFTVGEALffgheLRRGpfVDRRRQQREAERLLAeyfELQLPAdalvgE 140
Cdd:COG4778 83 SPREIlalrrRTIGyVsQFL---RVIPrvsALDVVAEPL-----LERG--VDREEARARARELLA---RLNLPE-----R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 141 LNSA--------ERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTV 212
Cdd:COG4778 145 LWDLppatfsggEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVD 224
|
....*
gi 2545433469 213 LRNGR 217
Cdd:COG4778 225 VTPFS 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
263-472 |
1.27e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYR------QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIALVPEE- 335
Cdd:PRK10895 8 NLAKAYKgrrvveDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 336 ---RRSQGISPLLSVLE---NLTLaglgrfsrwgllSQRKEQAEslRLIDELAIKTPGPQAAVSqLSGGNQQKVALGKWL 409
Cdd:PRK10895 88 sifRRLSVYDNLMAVLQirdDLSA------------EQREDRAN--ELMEEFHIEHLRDSMGQS-LSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 410 SRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
255-487 |
1.59e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNLARRYRQ----IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlRSPGEAIAQGIA 330
Cdd:PRK13548 1 AMLEARNLSVRLGGRTllddVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEErrsqgiSPL---LSVLEnltLAGLGRfSRWGLLSQRKEQ--AESLRLID--ELAiktpgpQAAVSQLSGGNQQKV 403
Cdd:PRK13548 80 VLPQH------SSLsfpFTVEE---VVAMGR-APHGLSRAEDDAlvAAALAQVDlaHLA------GRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 404 AL-------------GKWLsrrsavyLLDEPCVGVDVGAKVEIYRVIGRLV-EEGAAVLVLSSDLPELLGICDRILVLHR 469
Cdd:PRK13548 144 QLarvlaqlwepdgpPRWL-------LLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250
....*....|....*...
gi 2545433469 470 GEIAGEFHAGEAGSDQLL 487
Cdd:PRK13548 217 GRLVADGTPAEVLTPETL 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-219 |
1.89e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALS----PRQVDALGvqfihQERLLpASFT 94
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylHRQVALVG-----QEPVL-FSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFGheLRRGPFVDRRRQQREAErllAEYFELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEPS 168
Cdd:TIGR00958 571 VRENIAYG--LTDTPDEEIMAAAKAAN---AHDFIMEFPNgyDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 169 VALvKREVDQLLRIVKRLrdQGLSILYISHYLQEIDSlCDEVTVLRNGRDV 219
Cdd:TIGR00958 646 SAL-DAECEQLLQESRSR--ASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-225 |
2.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQpyaALSPRQV----DALGVQFIHQERLLPASfT 94
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVwdirHKIGMVFQNPDNQFVGA-T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFGHELRRGPFVDRRRQQREAERLLA-EYFELQLPAdalvgELNSAERQVLQITRALIRQPKILVFDEPSVALVK 173
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGmQDFKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 174 REVDQLLRIVKRLRDQ-GLSILYISHYLQEIdSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13650 174 EGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPR 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-226 |
2.08e-15 |
|
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: 75.14 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATL--ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGV 80
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLrSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 qfIHQERLLpasftvgealfFGHELRRG--PFvdrrrqqreaerllAEYFELQLPADALVGE----LNSAERQVLQITRA 154
Cdd:cd03369 87 --IPQDPTL-----------FSGTIRSNldPF--------------DEYSDEEIYGALRVSEgglnLSQGQRQLLCLARA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 155 LIRQPKILVFDEpSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSlCDEVTVLRNGRdvaVVEPRH 226
Cdd:cd03369 140 LLKRPRVLVLDE-ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIID-YDKILVMDAGE---VKEYDH 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
266-472 |
2.22e-15 |
|
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: 75.45 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 266 RRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIALVPEERRSQ 339
Cdd:cd03267 29 RKYREvealkgISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 340 GISPLLSVLENLTLAGL--GRFSRwgllsQRKEQAESLRLIDELaiKTPgpqaaVSQLSGGNQQKVALGKWLSRRSAVYL 417
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLppARFKK-----RLDELSELLDLEELL--DTP-----VRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 418 LDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
257-476 |
2.92e-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: 74.56 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlaRRYR------QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRLRSPGEAIAqgi 329
Cdd:cd03268 1 LKTNDLT--KTYGkkrvldDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsYQKNIEALRRIG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 330 ALVpeerRSQGISPLLSVLENLTLAGLGRfsrwGLLSQRKEQaeslrLIDELAIKTPGPQaAVSQLSGGNQQKVALGKWL 409
Cdd:cd03268 76 ALI----EAPGFYPNLTARENLRLLARLL----GIRKKRIDE-----VLDVVGLKDSAKK-KVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 410 SRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEF 476
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
263-472 |
2.97e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.04 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaQGIALVPEer 336
Cdd:COG3839 8 NVSKSYggvealKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAMVFQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rSQGISPLLSVLEN----LTLAGLGRfsrwgllSQRKEQ----AESLRlIDELAIKTPgpqaavSQLSGGNQQKVALGKW 408
Cdd:COG3839 83 -SYALYPHMTVYENiafpLKLRKVPK-------AEIDRRvreaAELLG-LEDLLDRKP------KQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 409 LSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-217 |
3.15e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFI 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLaeyfELQLPADALVGELNSAERQVLQITRALIRQPKILV 163
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMV----QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 164 FDEPSVALvkrevDQLLRI-----VKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK09452 168 LDESLSAL-----DYKLRKqmqneLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-220 |
3.24e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQFIHQ 85
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL-AKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEALFFGhelrRGP------------FVDRRRqqreaerllaEYFELQLPADALVGELNSAERQvlqitR 153
Cdd:COG4604 83 ENHINSRLTVRELVAFG----RFPyskgrltaedreIIDEAI----------AYLDLEDLADRYLDELSGGQRQ-----R 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 154 ALI-----RQPKILVFDEPSVAL-VKREVdQLLRIVKRL-RDQGLSIL-------YISHYlqeidslCDEVTVLRNGRDV 219
Cdd:COG4604 144 AFIamvlaQDTDYVLLDEPLNNLdMKHSV-QMMKLLRRLaDELGKTVVivlhdinFASCY-------ADHIVAMKDGRVV 215
|
.
gi 2545433469 220 A 220
Cdd:COG4604 216 A 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
269-462 |
3.38e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrspgEAIAQG-IALVPEERRSQGISPLLsv 347
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNlVAYVPQSEEVDWSFPVL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLagLGRFSRWGLLSQRKEQ-----AESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPC 422
Cdd:PRK15056 97 VEDVVM--MGRYGHMGWLRRAKKRdrqivTAALARVDMVEFR----HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 423 VGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICD 462
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
3.40e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.92 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSID-GQPYAALSPRQVDA 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 LG-----VQFIHQERLLPASFTVGEALFFGHELRrgpFVDRRRQQREAERLLAEYFELQLPA---DALVGELNSAERQVL 149
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLTEAIGLE---LPDELARMKAVITLKMVGFDEEKAEeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 150 QITRALIRQPKILVFDEPSVAL---VKREVDQllRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMdpiTKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-472 |
4.25e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGAtlaLDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSpRQVDALGVQ-- 81
Cdd:PRK10261 20 IAFMQEQQKIAA---VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS-RQVIELSEQsa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 ------------FIHQERL--LPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQ 147
Cdd:PRK10261 96 aqmrhvrgadmaMIFQEPMtsLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 148 VLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAV--VE- 223
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETgsVEq 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 224 ----PRHTSS----AQIARL--MVNREVQEMYP----------KAQVEL-----GEPLLQVRGL-----------NLARR 267
Cdd:PRK10261 256 ifhaPQHPYTrallAAVPQLgaMKGLDYPRRFPlislehpakqEPPIEQdtvvdGEPILQVRNLvtrfplrsgllNRVTR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 268 ----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPG--EAIAQGIALVPEE------ 335
Cdd:PRK10261 336 evhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyasld 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 336 -RRSQGisplLSVLENLTLAGLGRfsrwGLLSQRK--EQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRR 412
Cdd:PRK10261 416 pRQTVG----DSIMEPLRVHGLLP----GKAAAARvaWLLERVGLLPEHAWRYP------HEFSGGQRQRICIARALALN 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK10261 482 PKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
254-477 |
4.97e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.13 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRglNLARRYRQ----------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGe 323
Cdd:COG1116 5 APALELR--GVSKRFPTggggvtalddVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 324 aiaqgIALVPEERRSQgisPLLSVLEN----LTLAGLGRfsrwgllSQRKEQAEslRLIDEL-----AIKTPgpqaavSQ 394
Cdd:COG1116 82 -----RGVVFQEPALL---PWLTVLDNvalgLELRGVPK-------AERRERAR--ELLELVglagfEDAYP------HQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHR--GE 471
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVLSArpGR 218
|
....*.
gi 2545433469 472 IAGEFH 477
Cdd:COG1116 219 IVEEID 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-224 |
5.44e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.90 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQvd 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 alGVQFIHqERLLPAsFTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:COG4525 79 --GVVFQK-DALLPW-LNVLDNVAFGLRLRG---VPKAERRARAEELLAL-VGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 157 RQPKILVFDEPSVAL--VKREVDQ--LLRIvkrLRDQGLSILYISHYLQEIDSLCDEVTVL--RNGRDVAVVEP 224
Cdd:COG4525 151 ADPRFLLMDEPFGALdaLTREQMQelLLDV---WQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLEL 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
263-473 |
5.95e-15 |
|
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: 73.77 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYR------QIDLELRRGeIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIAQGIALVPEEr 336
Cdd:cd03264 5 NLTKRYGkkraldGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIGYLPQE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsQGISPLLSVLENL-TLAGLGRfsrwglLSQRKEQAESLRLIDELAIKTPGPQAaVSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:cd03264 81 --FGVYPNFTVREFLdYIAWLKG------IPSKEVKARVDEVLELVNLGDRAKKK-IGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEEgaAVLVLSSDLPE-LLGICDRILVLHRGEIA 473
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-230 |
6.14e-15 |
|
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: 74.01 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDA 77
Cdd:COG4181 7 PIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 L---GVQFIHQERLLPASFTVGEALFFGHELRRGPfvdrrRQQREAERLLAEYfELQLPADALVGELNSAERQVLQITRA 154
Cdd:COG4181 87 LrarHVGFVFQSFQLLPTLTALENVMLPLELAGRR-----DARARARALLERV-GLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 155 LIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYlQEIDSLCDEVTVLRNGRdvaVVEPRHTSSA 230
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGR---LVEDTAATAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
269-480 |
6.55e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.93 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaqgialVPEERRSQGIS------ 342
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE--------IPYLRRRIGVVfqdfrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 -PLLSVLENLTLAglgrfsrwgLLSQRKEQAESLRLIDE------LAIKTpgpQAAVSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:COG2884 91 lPDRTVYENVALP---------LRVTGKSRKEIRRRVREvldlvgLSDKA---KALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLpELLGICD-RILVLHRGEIAGEFHAGE 480
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL-ELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-64 |
7.03e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 7.03e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 10 RKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG 64
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-223 |
7.56e-15 |
|
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: 73.80 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYaalspRQVD------ALGVqfIHQERLLpas 92
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-----REVTldslrrAIGV--VPQDTVL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 93 F--TVGEALFFGHelrrgpfVDRRRQQREAERLLAEYFE--LQLPA--DALVGE----LNSAERQVLQITRALIRQPKIL 162
Cdd:cd03253 87 FndTIGYNIRYGR-------PDATDEEVIEAAKAAQIHDkiMRFPDgyDTIVGErglkLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 163 VFDEPSVAL---VKREVDQLLRIVKRLRdqglSILYISHYLQEIDSlCDEVTVLRNGRdvaVVE 223
Cdd:cd03253 160 LLDEATSALdthTEREIQAALRDVSKGR----TTIVIAHRLSTIVN-ADKIIVLKDGR---IVE 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-236 |
8.00e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKaDSGQVSIDGQPY-----AALS 71
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFddidlLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 72 PRQVDAL---GVQFIHQE--RLLPASFTVGEALF---------------FGHELRRGpfvdrrrqqreaeRLLAEYFELQ 131
Cdd:PRK15093 80 PRERRKLvghNVSMIFQEpqSCLDPSERVGRQLMqnipgwtykgrwwqrFGWRKRRA-------------IELLHRVGIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 132 LPADALVG---ELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLC 207
Cdd:PRK15093 147 DHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWA 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 2545433469 208 DEVTVLRNGRDVA-------VVEPRHTSSAQIARLM 236
Cdd:PRK15093 227 DKINVLYCGQTVEtapskelVTTPHHPYTQALIRAI 262
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
255-473 |
8.50e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.52 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRglNLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspgeaiaqg 328
Cdd:COG3842 4 PALELE--NVSKRYgdvtalDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERrsqGIS---------PLLSVLEN----LTLAGLGRfsrwgllSQRKEQA-ESLRL--IDELAIKTPgpqaav 392
Cdd:COG3842 70 TGLPPEKR---NVGmvfqdyalfPHLTVAENvafgLRMRGVPK-------AEIRARVaELLELvgLEGLADRYP------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 393 SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGR 213
|
..
gi 2545433469 472 IA 473
Cdd:COG3842 214 IE 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
269-472 |
1.08e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 74.22 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIA---QGIALVPEerrSQGISPLL 345
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMVFQ---SFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLEN----LTLAGLGRfsrwgllSQRKEQA-ESLRLIDELAIKTPGPqaavSQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:cd03294 118 TVLENvafgLEVQGVPR-------AEREERAaEALELVGLEGWEHKYP----DELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 421 PCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
270-473 |
1.25e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.25 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE----------------AIAQGIALvp 333
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmlfqennlfphlTVAQNIGL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 334 eerrsqGISPLLsvleNLTLAglgrfsrwgllsQRKEQAESLRL--IDELAIKTPGpqaavsQLSGGNQQKVALGKWLSR 411
Cdd:COG3840 95 ------GLRPGL----KLTAE------------QRAQVEQALERvgLAGLLDRLPG------QLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 412 RSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-225 |
1.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI---HKADSGQVSIDGQPYAALSPRQV-DALGVQFIHQERLLPASf 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIrEKVGIVFQNPDNQFVGA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRRGPfvdRRRQQREAERLLAEYFELQLpADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVK 173
Cdd:PRK13640 101 TVGDDVAFGLENRAVP---RPEMIKIVRDVLADVGMLDY-IDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 174 REVDQLLRIVKRL-RDQGLSILYISHYLQEIdSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13640 177 AGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPV 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-223 |
1.73e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKST----LIKVLAGihkadSGQVSIDGQPYAALSPRQVDAL--GVQF 82
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVrhRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQE--RLLPASFTVGEALFFGHELRRgPFVDRRRQQREAERLLAEyfeLQLPADA---LVGELNSAERQVLQITRALIR 157
Cdd:PRK15134 367 VFQDpnSSLNPRLNVLQIIEEGLRVHQ-PTLSAAQREQQVIAVMEE---VGLDPETrhrYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 158 QPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGE---VVE 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
271-476 |
2.21e-14 |
|
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: 72.61 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE--AIAQGIALVpeerrSQGISpLLS-- 346
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKARRRIGMI-----FQHFN-LLSsr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 -VLEN----LTLAGLGRfsrwgllSQRKEQA-ESLRLIDeLAIKTpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:cd03258 98 tVFENvalpLEIAGVPK-------AEIEERVlELLELVG-LEDKA---DAYPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 421 PCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGEF 476
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
271-470 |
2.49e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.50 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGE---AIAQGIALVPeerrsqgispLLSV 347
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK--QITEPGPdrmVVFQNYSLLP----------WLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLAGLGRFSRWGLLSQRKEQAESLRLID--ELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGV 425
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIVEEHIALVGltEAADKRPG------QLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 426 DVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-216 |
2.51e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 8 HLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFIHQER 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 LLPASFTVGEALFFGHEL---RRGPfvDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVF 164
Cdd:PRK10851 84 ALFRHMTVFDNIAFGLTVlprRERP--NAAAIKAKVTQLL-EMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 165 DEPSVAL---VKREVDQLLRivkRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:PRK10851 161 DEPFGALdaqVRKELRRWLR---QLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-213 |
3.32e-14 |
|
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: 75.02 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 14 GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAlGVQFIHQERLLPASf 93
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGhelRRGPFVDRRRQQREAERLLAEYFELQLPADALVGE----LNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:TIGR02857 411 TIAENIRLA---RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545433469 170 ALVKREVDQLLRIVKRLRdQGLSILYISHYLqEIDSLCDEVTVL 213
Cdd:TIGR02857 488 HLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
241-471 |
3.87e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 241 VQEMYPKAQVELGE---PLLQVRglNLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHL 311
Cdd:PRK11607 1 MNDAIPRPQAKTRKaltPLLEIR--NLTKSFdgqhavDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 312 EGrllrlrspgeaiaQGIALVPEERR-------SQGISPLLSVLENLTLaGL--GRFSRwGLLSQRKEQAESLRLIDELA 382
Cdd:PRK11607 79 DG-------------VDLSHVPPYQRpinmmfqSYALFPHMTVEQNIAF-GLkqDKLPK-AEIASRVNEMLGLVHMQEFA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 383 IKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAK----VEIYRVIGRLveeGAAVLVLSSDLPELL 458
Cdd:PRK11607 144 KRKP------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqLEVVDILERV---GVTCVMVTHDQEEAM 214
|
250
....*....|...
gi 2545433469 459 GICDRILVLHRGE 471
Cdd:PRK11607 215 TMAGRIAIMNRGK 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
271-472 |
4.44e-14 |
|
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: 71.47 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEErrsqgisPLL---SV 347
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQD-------VTLfygTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLAGLGrfsrwgLLSQRKEQAESLRLIDELAIKTP-GPQAAVS----QLSGGNQQKVALGKWLSRRSAVYLLDEPC 422
Cdd:cd03245 95 RDNITLGAPL------ADDERILRAAELAGVTDFVNKHPnGLDLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 423 VGVDVGAKVeiyRVIGRLVEEGAA-VLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03245 169 SAMDMNSEE---RLKERLRQLLGDkTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-220 |
4.55e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 12 RFGATlALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdalgVQFIHQERLLPA 91
Cdd:PRK15056 17 RNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL----VAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 92 SFTV--------GEalfFGHE--LRRGPFVDRRRQQREAERL-LAEYFELQlpadalVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK15056 92 SFPVlvedvvmmGR---YGHMgwLRRAKKRDRQIVTAALARVdMVEFRHRQ------IGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 161 ILVFDEPSVAL-VKREVdQLLRIVKRLRDQGLSILYISHYLQEIDSLCDeVTVLRNGRDVA 220
Cdd:PRK15056 163 VILLDEPFTGVdVKTEA-RIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLA 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
4.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.42 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPY-----AALSPRQvdALGVQFIHQERLLP 90
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRK--TVGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 91 ASfTVGEALFFGhELRRGpFVDRRRQQREAERLLA---EYFELQLPAdalvgELNSAERQVLQITRALIRQPKILVFDEP 167
Cdd:PRK13639 93 AP-TVEEDVAFG-PLNLG-LSKEEVEKRVKEALKAvgmEGFENKPPH-----HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 168 SVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-217 |
4.61e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALG 79
Cdd:PRK11629 6 LQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQ---FIHQ-ERLLPaSFT----VGEALFFGHelrrgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQI 151
Cdd:PRK11629 86 NQklgFIYQfHHLLP-DFTalenVAMPLLIGK-------KKPAEINSRALEMLAA-VGLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 152 TRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTvLRNGR 217
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-219 |
4.89e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--GVQFIHQERL--LPASF 93
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEAL-----FFGHELRRGPFVDRRRQQREAERLLAEYFElQLPAdalvgELNSAERQVLQITRALIRQPKILVFDEPS 168
Cdd:PRK15079 116 TIGEIIaeplrTYHPKLSRQEVKDRVKAMMLKVGLLPNLIN-RYPH-----EFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 169 VAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK15079 190 SALdvsIQAQVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-226 |
5.05e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.07 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQ-----------------------PYAALSPRQ 74
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkadpeaqkllrqkiqivfqnPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 75 vdalgvqfihqerllPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYfelqlpADALVGELNSAERQVLQITRA 154
Cdd:PRK11308 110 ---------------KVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEH------YDRYPHMFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 155 LIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE---------- 223
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR---CVEkgtkeqifnn 245
|
...
gi 2545433469 224 PRH 226
Cdd:PRK11308 246 PRH 248
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-217 |
5.12e-14 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 70.03 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVqfIHQERLLPASfTV 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV--LNQRPYLFDT-TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 GEALffGHELRRGpfvdrrrqqreaerllaeyfelqlpadalvgelnsaERQVLQITRALIRQPKILVFDEPSVALVKRE 175
Cdd:cd03247 92 RNNL--GRRFSGG------------------------------------ERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545433469 176 VDQLLRIV-KRLRDQglSILYISHYLQEIDSLcDEVTVLRNGR 217
Cdd:cd03247 134 ERQLLSLIfEVLKDK--TLIWITHHLTGIEHM-DKILFLENGK 173
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-225 |
6.31e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD--------SGQVSIDGQPYAALSPRQV 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 DALGVQFIHQERllPA-SFTVGEALFFG---HELRRGPFVDRRRQQREAERLLAEyfelqlpADALVGE----LNSAERQ 147
Cdd:PRK13547 82 ARLRAVLPQAAQ--PAfAFSAREIVLLGrypHARRAGALTHRDGEIAWQALALAG-------ATALVGRdvttLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 148 VLQITRAL---------IRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
....*...
gi 2545433469 218 DVAVVEPR 225
Cdd:PRK13547 233 IVAHGAPA 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-256 |
7.88e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQ--VDALGVQFIHQERLLPASf 93
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgiRKLVGIVFQNPETQFVGR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHE-LRRGPFVDRRRQQREAERLLAEYFELQLPAdalvgELNSAERQVLQITRALIRQPKILVFDEPSVALV 172
Cdd:PRK13644 94 TVEEDLAFGPEnLCLPPIEIRKRVDRALAEIGLEKYRHRSPK-----TLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 173 KREVDQLLRIVKRLRDQGLSILYISHYLQEIDSlCDEVTVLRNGRDVAVVEPRHTSSAQIARLMvnrevqEMYPKAQVEL 252
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL------GLTPPSLIEL 241
|
....
gi 2545433469 253 GEPL 256
Cdd:PRK13644 242 AENL 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
9.02e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFG-ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP--YAA---LSPRQvdA 77
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRkglMKLRE--S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 LGVQFIHQERLLpASFTVGEALFFG--------HELRRGpfVDRRRQQREAERLLAEyfelqlPADAlvgeLNSAERQVL 149
Cdd:PRK13636 84 VGMVFQDPDNQL-FSASVYQDVSFGavnlklpeDEVRKR--VDNALKRTGIEHLKDK------PTHC----LSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 150 QITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-226 |
9.25e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVE-------------RGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP 72
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 73 RQVdALGVQFIHQErlLPAS--FTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQ 150
Cdd:PRK10575 81 KAF-ARKVAYLPQQ--LPAAegMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 151 ITRALIRQPKILVFDEPSVAL-VKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALdIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-66 |
9.88e-14 |
|
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: 70.64 E-value: 9.88e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP 66
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-224 |
1.17e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP---RQVDALG 79
Cdd:PRK10070 28 GLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAeyfeLQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVG----LENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 160 KILVFDEPSVALvkrevDQLLR------IVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK10070 184 DILLMDEAFSAL-----DPLIRtemqdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
269-473 |
1.31e-13 |
|
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: 70.25 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllRLRSPgeaIAQGIALVPEerrsqgisplLSVL 348
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL---LGLGGGFNPE----------LTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLagLGRFsrWGLlsQRKEQAESLRLIDELA-----IKTPgpqaaVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03220 103 ENIYL--NGRL--LGL--SRKEIDEKIDEIIEFSelgdfIDLP-----VKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
257-472 |
1.40e-13 |
|
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: 69.90 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARR----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVV-----RADSGSIHLEGRllrlrspgeAIAQ 327
Cdd:cd03260 1 IELRDLNVYYGdkhaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGK---------DIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 328 GIALVPEERRSQGI-----SPL-LSVLENLTLaglgrfsrwGLLSQRKEQAESLRLIDELAIKTPG------PQAAVSQL 395
Cdd:cd03260 72 LDVDVLELRRRVGMvfqkpNPFpGSIYDNVAY---------GLRLHGIKLKEELDERVEEALRKAAlwdevkDRLHALGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 396 SGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVlSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIV-THNMQQAARVADRTAFLLNGRL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
232-473 |
1.42e-13 |
|
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: 72.88 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 232 IARLM--VNREVQEMYPKAQVEL-GEPLLQVRGLNLarRY--------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFG 300
Cdd:COG4987 306 ARRLNelLDAPPAVTEPAEPAPApGGPSLELEDVSF--RYpgagrpvlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 301 VVRADSGSIHLEGRLLRlRSPGEAIAQGIALVPEErrsqgiSPLL--SVLENLTLAglgrfsrwgllsqrKEQA------ 372
Cdd:COG4987 384 FLDPQSGSITLGGVDLR-DLDEDDLRRRIAVVPQR------PHLFdtTLRENLRLA--------------RPDAtdeelw 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 373 ---ESLRLIDELAIKTPGPQAAV----SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVeEGA 445
Cdd:COG4987 443 aalERVGLGDWLAALPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGR 521
|
250 260
....*....|....*....|....*...
gi 2545433469 446 AVLVLSSDLPElLGICDRILVLHRGEIA 473
Cdd:COG4987 522 TVLLITHRLAG-LERMDRILVLEDGRIV 548
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
246-471 |
1.65e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 246 PKAQVELGEPLLQVRGLNLARRY--------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLR 317
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQeqqkiaavRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 318 LRSPgEAIAQGIALVPEERRSQG-------------ISPLLSVLENLTLA-----GLGRfsrwgllsqRKEQAESLRLID 379
Cdd:PRK10261 82 RRSR-QVIELSEQSAAQMRHVRGadmamifqepmtsLNPVFTVGEQIAESirlhqGASR---------EEAMVEAKRMLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 380 ELAIktPGPQAAVS----QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGA-AVLVLSSDL 454
Cdd:PRK10261 152 QVRI--PEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDM 229
|
250
....*....|....*..
gi 2545433469 455 PELLGICDRILVLHRGE 471
Cdd:PRK10261 230 GVVAEIADRVLVMYQGE 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
271-472 |
1.78e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSG----------SIHLEGRLLR----LRSPGEAIAQGIALVPEer 336
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARdirkSRANTGYIFQQFNLVNR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsqgisplLSVLENLTLAGLGRFSRWGLLSQ---RKEQAESLRLIDELAIKTPGPQAaVSQLSGGNQQKVALGKWLSRRS 413
Cdd:PRK09984 101 --------LSVLENVLIGALGSTPFWRTCFSwftREQKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 414 AVYLLDEPCVGVDVGAK---VEIYRVIGRlvEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK09984 172 KVILADEPIASLDPESArivMDTLRDINQ--NDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-223 |
1.87e-13 |
|
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: 69.95 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQERLLpASFTVGE 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFL-FNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 98 ALFFGhelRRGpfVDRRRQQREAERLLAEYFELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEPSVAL 171
Cdd:cd03251 95 NIAYG---RPG--ATREEVEEAARAANAHEFIMELPEgyDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 172 -------VKREVDQLLrivkrlrdQGLSILYISHYLQEIDSlCDEVTVLRNGRdvaVVE 223
Cdd:cd03251 170 dteserlVQAALERLM--------KNRTTFVIAHRLSTIEN-ADRIVVLEDGK---IVE 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
271-490 |
2.73e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE-AIAQGIALVPEERRSQGI-----SPL 344
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQDPEQQIFytdidSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 LSVLENLTLAGlgrfsrwGLLSQRKEQAesLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:PRK13638 100 AFSLRNLGVPE-------AEITRRVDEA--LTLVDAQHFR----HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 425 VDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIageFHAGEAGsdQLLACA 490
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI---LTHGAPG--EVFACT 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
269-473 |
3.67e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaQGIALVPEerrSQGISPLLSVL 348
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMVFQ---SYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 EN----LTLAGLGRFSRwgllSQRKEQ-AESLRLIDELAIKtpgPQAavsqLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:PRK11000 94 ENmsfgLKLAGAKKEEI----NQRVNQvAEVLQLAHLLDRK---PKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 424 GVD----VGAKVEIYRVIGRLveeGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:PRK11000 163 NLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
7-200 |
4.06e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 7 QHLRKRFgatlalddaSLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalgVQFIHQE 86
Cdd:PRK10771 12 HHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP---VSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 87 RLLPASFTVGEALFFGHE--LRRGPFVDRRRQQREAERLLAEYFElQLPadalvGELNSAERQVLQITRALIRQPKILVF 164
Cdd:PRK10771 80 NNLFSHLTVAQNIGLGLNpgLKLNAAQREKLHAIARQMGIEDLLA-RLP-----GQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2545433469 165 DEPSVAL---VKREVDQLLRIVkrLRDQGLSILYISHYL 200
Cdd:PRK10771 154 DEPFSALdpaLRQEMLTLVSQV--CQERQLTLLMVSHSL 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-219 |
4.68e-13 |
|
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: 68.45 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 17 LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAG---IHKADSGQVSIDGQPyaaLSPRQVD---ALGVQFihqERLLP 90
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQP---RKPDQFQkcvAYVRQD---DILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 91 aSFTVGEALFFGHELR-RGPFVDRRRQQREAERLLAEYFELQLpADALVGELNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:cd03234 95 -GLTVRETLTYTAILRlPRKSSDAIRKKRVEDVLLRDLALTRI-GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 170 ALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:cd03234 173 GLDSFTALNLVSTLSQLaRRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-225 |
5.60e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.42 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP----RQV-DALGVQFIHQERLLPAS 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVrKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 93 FTVGEALFfghelrrGP--F-VDRRRQQREAERLLaeyFELQLPADALVG---ELNSAERQVLQITRALIRQPKILVFDE 166
Cdd:PRK13646 102 TVEREIIF-------GPknFkMNLDEVKNYAHRLL---MDLGFSRDVMSQspfQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 167 PSVALVKREVDQLLRIVKRLR-DQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-225 |
6.49e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.31 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVD---ALGVQFIHQERLLpa 91
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkKVGLVFQYPEYQL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 92 sF--TVGEALFFGHE---LRRGPFVDRRRQQREAERLLAEYFELQLPAdalvgELNSAERQVLQITRALIRQPKILVFDE 166
Cdd:PRK13637 97 -FeeTIEKDIAFGPInlgLSEEEIENRVKRAMNIVGLDYEDYKDKSPF-----ELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 167 PSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-217 |
6.70e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.55 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIH--KADSGQVSIDGQPYAALSPRQVDALGVQFIHQErllPASFT-V 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQY---PPEIPgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 GEALFfgheLRrgpFVDrrrqqreaerllaeyfelqlpadalVGeLNSAERQVLQITRALIRQPKILVFDEPSVALVKRE 175
Cdd:cd03217 93 KNADF----LR---YVN-------------------------EG-FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545433469 176 VDQLLRIVKRLRDQGLSILYISHYLQEIDSL-CDEVTVLRNGR 217
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGR 182
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
271-487 |
1.00e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 67.71 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR------LLRLR-SPGEAIaQGIALVPEerrsqgisp 343
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdPVELRrKIGYVI-QQIGLFPH--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 lLSVLENLTLagLGRFSRWGLLSQRKEQAESLRLID----ELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:cd03295 90 -MTVEENIAL--VPKLLKWPKEKIRERADELLALVGldpaEFADRYP------HELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI-------------AGEFHAGEAGSDQ 485
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIvqvgtpdeilrspANDFVAEFVGADR 240
|
..
gi 2545433469 486 LL 487
Cdd:cd03295 241 LL 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-217 |
1.13e-12 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 66.09 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQERLLPASfTVGEA 98
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 99 LFFGhelrrgpfvdrrrqqreaerllaeyfelqlpadalvgelnsAERQVLQITRALIRQPKILVFDEPSVAL-VKREVd 177
Cdd:cd03246 96 ILSG-----------------------------------------GQRQRLGLARALYGNPRILVLDEPNSHLdVEGER- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 178 QLLRIVKRLRDQGLSILYISHYLQEIDSlCDEVTVLRNGR 217
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
257-455 |
1.16e-12 |
|
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: 66.75 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYR----QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgeAIAQGIALV 332
Cdd:cd03231 1 LEADELTCERDGRalfsGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 PEErrsQGISPLLSVLENLTLaglgrfsrWGLLSQRKEQAESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGK-WLSR 411
Cdd:cd03231 79 GHA---PGIKTTLSVLENLRF--------WHADHSDEQVEEALARVGLNGFE----DRPVAQLSAGQQRRVALARlLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 412 RSaVYLLDEPCVGVDVgAKVEIY--RVIGRLVEEGAAVLVLSSDLP 455
Cdd:cd03231 144 RP-LWILDEPTTALDK-AGVARFaeAMAGHCARGGMVVLTTHQDLG 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-62 |
1.23e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 1.23e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI 62
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
254-470 |
1.55e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLarRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlRSPGEAIA- 326
Cdd:PRK11300 3 QPLLSVSGLMM--RFggllavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 327 QGIAlvpeeRRSQGISPL--LSVLENLTLA-----GLGRFSrwGLL---SQRKEQAESLRL----IDELAIKTPGPQAAv 392
Cdd:PRK11300 80 MGVV-----RTFQHVRLFreMTVIENLLVAqhqqlKTGLFS--GLLktpAFRRAESEALDRaatwLERVGLLEHANRQA- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 393 SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
254-481 |
1.62e-12 |
|
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: 67.07 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLarRY----------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrspge 323
Cdd:COG4181 6 APIIELRGLTK--TVgtgageltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 324 aiaqgiALVPEER---RSQGIS---------PLLSVLEN----LTLAGLGrfsrwgllsQRKEQAESL--------RLid 379
Cdd:COG4181 78 ------ALDEDARarlRARHVGfvfqsfqllPTLTALENvmlpLELAGRR---------DARARARALlervglghRL-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 380 elaiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD--VGAKVEiyRVIGRLVEEGAAVLVLSSDLPEL 457
Cdd:COG4181 141 ---------DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQII--DLLFELNRERGTTLVLVTHDPAL 209
|
250 260
....*....|....*....|....
gi 2545433469 458 LGICDRILVLHRGEIAGEFHAGEA 481
Cdd:COG4181 210 AARCDRVLRLRAGRLVEDTAATAA 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-216 |
1.69e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.11 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD--SGQVSIDGQPYAALSPRQVDalgvqFIHQERLLPASFTVG 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRSTG-----YVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 97 EALFFGHELRrgpfvdrrrqqreaerllaeyfelqlpadalvgELNSAERQVLQITRALIRQPKILVFDEPSVALVKREV 176
Cdd:cd03232 98 EALRFSALLR---------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2545433469 177 DQLLRIVKRLRDQGLSIL-YISHYLQEIDSLCDEVTVLRNG 216
Cdd:cd03232 145 YNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-235 |
1.80e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVsIDGQpyAALSPRQVDalgVQFI 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEARED---TRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQE-RLLPASF---TVGEALffghelrRGPFVDRRRQQREAERLLAEYFElqLPAdALVGelnsAERQVLQITRALIRQP 159
Cdd:PRK11247 87 FQDaRLLPWKKvidNVGLGL-------KGQWRDAALQALAAVGLADRANE--WPA-ALSG----GQKQRVALARALIHRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 160 KILVFDEPSVALvkrevDQLLRI-----VKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGR---DVAV--VEPRHTS 228
Cdd:PRK11247 153 GLLLLDEPLGAL-----DALTRIemqdlIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKiglDLTVdlPRPRRRG 227
|
....*..
gi 2545433469 229 SAQIARL 235
Cdd:PRK11247 228 SARLAEL 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-206 |
2.44e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGihKADSGQVSID-----GQPYAALSPRQVDALGVQFIHqerlLPASf 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGdrlvnGRPLDSSFQRSIGYVQQQDLH----LPTS- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRRgP----------FVDRrrqqreaerlLAEYFELQLPADALVGE----LNSAERQVLQITRALIRQP 159
Cdd:TIGR00956 852 TVRESLRFSAYLRQ-PksvsksekmeYVEE----------VIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 160 KILVF-DEPSVALVKREVDQLLRIVKRLRDQGLSILYISH-----YLQEIDSL 206
Cdd:TIGR00956 921 KLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsaiLFEEFDRL 973
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-470 |
2.74e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgeAIAQGIALVPEerrSQGISPLLSVLEN 350
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR--HARQRVGVVPQ---FDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 LTLaglgrFSRWGLLSQRKEQAESLRLIdELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAK 430
Cdd:PRK13537 101 LLV-----FGRYFGLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 431 VEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
227-467 |
3.26e-12 |
|
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: 68.85 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 227 TSSAQIARLMVNREvQEMYPKAQVELGEPL-LQVRGLNLA-----RRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFG 300
Cdd:TIGR02857 292 AAAEALFAVLDAAP-RPLAGKAPVTAAPASsLEFSGVSVAypgrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 301 VVRADSGSIHLEGRLLRLRSPgEAIAQGIALVPEerrsqgiSPLL---SVLENLTLAGLGrfSRWGLLSQRKEQAESLRL 377
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLADADA-DSWRDQIAWVPQ-------HPFLfagTIAENIRLARPD--ASDAEIREALERAGLDEF 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 378 IDEL--AIKTP-GPQAAvsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVeEGAAVLVLSSDl 454
Cdd:TIGR02857 441 VAALpqGLDTPiGEGGA--GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR- 516
|
250
....*....|...
gi 2545433469 455 PELLGICDRILVL 467
Cdd:TIGR02857 517 LALAALADRIVVL 529
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-226 |
3.72e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF--GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyaaLSPRQV----DA 77
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVwdvrRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 LGVQFIHQERLLPASfTVGEALFFGHELRRGPFVDRRRQQREAERLLA-EYFELQLPAdalvgELNSAERQVLQITRALI 156
Cdd:PRK13635 83 VGMVFQNPDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGmEDFLNREPH-----RLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSlCDEVTVLRNGRDVAVVEPRH 226
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
257-455 |
4.02e-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: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYR----QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL-RLR-SPGEAIAQgIA 330
Cdd:TIGR01189 1 LAARNLACSRGERmlfeGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRdEPHENILY-LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPeerrsqGISPLLSVLENLtlaglgRFSRWGLLSQRKEQAESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGK-WL 409
Cdd:TIGR01189 80 HLP------GLKPELSALENL------HFWAAIHGGAQRTIEDALAAVGLTGFE----DLPAAQLSAGQQRRLALARlWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 410 SRRSaVYLLDEPCVGVDVgAKVEIY--RVIGRLVEEGAAVLVLSSDLP 455
Cdd:TIGR01189 144 SRRP-LWILDEPTTALDK-AGVALLagLLRAHLARGGIVLLTTHQDLG 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
255-473 |
4.50e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNlaRRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaQG 328
Cdd:PRK09452 13 PLVELRGIS--KSFdgkeviSNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-------------QD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERR-------SQGISPLLSVLENLTlaglgrfsrWGLLSQRKEQAE-------SLRLI--DELAIKTPgpqaav 392
Cdd:PRK09452 78 ITHVPAENRhvntvfqSYALFPHMTVFENVA---------FGLRMQKTPAAEitprvmeALRMVqlEEFAQRKP------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 393 SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:PRK09452 143 HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
..
gi 2545433469 472 IA 473
Cdd:PRK09452 223 IE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-226 |
4.72e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 65.78 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGA-TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQF 82
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPaSFTVGEALFFGHELRRGPFVDRRRQQREAERLL----AEYfelqlpADALVGELNSAERQVLQITRALIRQ 158
Cdd:cd03295 81 IQQIGLFP-HMTVEENIALVPKLLKWPKEKIRERADELLALVgldpAEF------ADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 159 PKILVFDEPSVAL--VKREV--DQLLRIVKRLrdqGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:cd03295 154 PPLLLMDEPFGALdpITRDQlqEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-223 |
4.93e-12 |
|
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: 65.64 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQErllPASF--TVG 96
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQE---PVLFdgTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 97 EALFFGHElrrgpfvDRRRQQREAERLLAEY--FELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEPS 168
Cdd:cd03249 95 ENIRYGKP-------DATDEEVEEAAKKANIhdFIMSLPDgyDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 169 VAL-------VKREVDQLLRivkrlrdqGLSILYISHYLQEIdSLCDEVTVLRNGRdvaVVE 223
Cdd:cd03249 168 SALdaeseklVQEALDRAMK--------GRTTIVIAHRLSTI-RNADLIAVLQNGQ---VVE 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
257-470 |
5.65e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRAdSGSIHLEGRLLRLRSPGEaIAQgialvpeeR 336
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAE-LAR--------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 R---SQGISPLLS--VLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAiktpgpqAAVSQLSGGNQQKVALGK---- 407
Cdd:PRK03695 71 RaylSQQQTPPFAmpVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLG-------RSVNQLSGGEWQRVRLAAvvlq 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 408 -W--LSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK03695 144 vWpdINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-202 |
6.49e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 7 QHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP-------------------- 66
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdagdiatrrrvgymsqafs 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 67 -YAALSPRQVDALgvqfiHQeRLlpasFTVGEAlffghelRRGPFVDRrrqqreaerlLAEYFELQLPADALVGELNSAE 145
Cdd:NF033858 350 lYGELTVRQNLEL-----HA-RL----FHLPAA-------EIAARVAE----------MLERFDLADVADALPDSLPLGI 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 146 RQVLQITRALIRQPKILVFDEPS--VALVKRevDQLLRIVKRL-RDQGLSIlYIS-HYLQE 202
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPTsgVDPVAR--DMFWRLLIELsREDGVTI-FIStHFMNE 460
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-63 |
6.82e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.24 E-value: 6.82e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSID 63
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-217 |
7.86e-12 |
|
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: 64.80 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQERLLPASfT 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFGheLRRGPFVDRRRQQREAErllAEYF--ELQLPADALVGE----LNSAERQVLQITRALIRQPKILVFDEPS 168
Cdd:cd03248 104 LQDNIAYG--LQSCSFECVKEAAQKAH---AHSFisELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 169 VAL---VKREVDQLLRIVKRLRdqglSILYISHYLQEIDSlCDEVTVLRNGR 217
Cdd:cd03248 179 SALdaeSEQQVQQALYDWPERR----TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-216 |
8.41e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQvdalGVQF 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHqERLLPASfTVGEALFFGHELRRgpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPKIL 162
Cdd:PRK11248 77 QN-EGLLPWR-NVQDNVAFGLQLAG---VEKMQRLEIAHQMLKK-VGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 163 VFDEPSVAL--VKREVDQLLrIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:PRK11248 151 LLDEPFGALdaFTREQMQTL-LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-201 |
8.70e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGA-----TLALDDASLKVERG---TIhglVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV 75
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGdfvTV---IGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 dalgVQFI---HQERLL--PASFTVGE--ALFFGHELRRG-----------PFVDrrrqqreaerLLAEyFELQLPA--D 135
Cdd:COG1101 79 ----AKYIgrvFQDPMMgtAPSMTIEEnlALAYRRGKRRGlrrgltkkrreLFRE----------LLAT-LGLGLENrlD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 136 ALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQ 201
Cdd:COG1101 144 TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNME 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
263-473 |
1.01e-11 |
|
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: 64.36 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRY--------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaQGIALVPE 334
Cdd:cd03369 11 NLSVRYapdlppvlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG-------------IDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 335 E--RRSQGISPLLSVLENLTL-AGLGRFSRWgllsQRKEQAESLRlidelaIKTPGpqaavSQLSGGNQQKVALGKWLSR 411
Cdd:cd03369 78 EdlRSSLTIIPQDPTLFSGTIrSNLDPFDEY----SDEEIYGALR------VSEGG-----LNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 412 RSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLHRGEIA 473
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTI-REEFTNSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-217 |
1.06e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALspRQVDA-LGVQF 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDGqLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASFTvgeaLFFGH-----------ELRRGPF----VDRRRQQREAERLLAEYFELQLPADALVGELNSAERQ 147
Cdd:PRK10619 84 KNQLRLLRTRLT----MVFQHfnlwshmtvleNVMEAPIqvlgLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 148 VLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
1.08e-11 |
|
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: 67.00 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQF 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 83 IHQERLLPASfTVGEALFFGhelrRGPFVDRRRQQREAERLLAEYFElQLP--ADALVGE----LNSAERQVLQITRALI 156
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLA----RPDATDEELWAALERVGLADWLR-ALPdgLDTVLGEggarLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVkRLRDQGLSILYISHYL 200
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
1.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVQFIHQERLLpASFTVG 96
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrKFVGLVFQNPDDQI-FSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 97 EALFFGhELRRGpfVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREV 176
Cdd:PRK13652 98 QDIAFG-PINLG--LDEETVAHRVSSAL-HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545433469 177 DQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK13652 174 KELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-225 |
1.14e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP-------RQVDALGVQF----IHQE 86
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqiRKKVGLVFQFpesqLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 87 RLL------PASFTVGEAlffghelrrgpfvdrrrqqreaerllaEYFELQLPADALVG-----------ELNSAERQVL 149
Cdd:PRK13649 102 TVLkdvafgPQNFGVSQE---------------------------EAEALAREKLALVGiseslfeknpfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 150 QITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-223 |
1.16e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.91 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAAL---SPRQvdALGVQFihQERLLPASfT 94
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVtraSLRR--NIAVVF--QDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFGHElrrgpfvDRRRQQREAERLLAEYFELQLPA----DALVGE----LNSAERQVLQITRALIRQPKILVFDE 166
Cdd:PRK13657 425 IEDNIRVGRP-------DATDEEMRAAAERAQAHDFIERKpdgyDTVVGErgrqLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 167 PSVAL-------VKREVDQLLrivkrlrdQGLSILYISHYLQEIDSlCDEVTVLRNGRdvaVVE 223
Cdd:PRK13657 498 ATSALdveteakVKAALDELM--------KGRTTFIIAHRLSTVRN-ADRILVFDNGR---VVE 549
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-212 |
1.30e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIH-----GLVGENGAGKSTLIKVLAGIHKADSGqvSIDGQPYAALSPrqvdalgvQFIHQErllpASF 93
Cdd:COG1245 351 YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKP--------QYISPD----YDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEAL-----------FFGHELRRGpfvdrrrqqreaerllaeyfeLQLPA--DALVGELNSAERQVLQITRALIRQPK 160
Cdd:COG1245 417 TVEEFLrsantddfgssYYKTEIIKP---------------------LGLEKllDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 161 ILVFDEPSVALvkrEVDQLL---RIVKRL-RDQGLSILYISHYLQEIDSLCDEVTV 212
Cdd:COG1245 476 LYLLDEPSAHL---DVEQRLavaKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
272-473 |
1.77e-11 |
|
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: 63.67 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 272 DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaQGIALVPEErrsQGISPLLSVLENL 351
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQE---NNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 352 tlaGLGRFSRWGLLSQRKEQAESLRL---IDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVG 428
Cdd:cd03298 92 ---GLGLSPGLKLTAEDRQAIEVALArvgLAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 429 AKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:cd03298 163 LRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
271-475 |
1.92e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRLRSPGEAI--AQGIALVPEerrSQGISPLLSV 347
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQpLHQMDEEARAKlrAKHVGFVFQ---SFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLAGLGRFSrwgllSQRKEQAESLRLIDELAIKTPGPQAAvSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:PRK10584 106 LENVELPALLRGE-----SSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 428 GAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-223 |
2.07e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.38 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVqfIHQERLLpasF--TV 95
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLrAAIGI--VPQDTVL---FndTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 GEALFFG------HELRR-------GPFVDrrrqqreaerllaeyfelQLP--ADALVGE----LNSAERQVLQITRALI 156
Cdd:COG5265 449 AYNIAYGrpdaseEEVEAaaraaqiHDFIE------------------SLPdgYDTRVGErglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 157 RQPKILVFDEPSVAL---VKREVDQLLRIVKRLRdqglSILYISHYLQEI-DslCDEVTVLRNGRdvaVVE 223
Cdd:COG5265 511 KNPPILIFDEATSALdsrTERAIQAALREVARGR----TTLVIAHRLSTIvD--ADEILVLEAGR---IVE 572
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
2.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI-----HKADSGQVSIDGQ-----PYAAL 70
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdifkmDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 71 SPRqvdalgVQFIHQERLLPASFTVGEALFFGHELRRgpFVDRRRQQREAERLLAE----YFELQLPADALVGELNSAER 146
Cdd:PRK14247 81 RRR------VQMVFQIPNPIPNLSIFENVALGLKLNR--LVKSKKELQERVRWALEkaqlWDEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 147 QVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQgLSILYISHYLQEIDSLCDEVTVLRNGRDVAV----- 221
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWgptre 231
|
....*..
gi 2545433469 222 --VEPRH 226
Cdd:PRK14247 232 vfTNPRH 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
265-472 |
2.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 265 ARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIA---QGIALVPEERRSQGI 341
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvrKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 342 SPllSVLENLTLAGlgrfSRWGLLSQRKEQ--AESLRLI---DELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVY 416
Cdd:PRK13643 99 EE--TVLKDVAFGP----QNFGIPKEKAEKiaAEKLEMVglaDEFWEKSP------FELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 417 LLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-217 |
2.28e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFG----ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL- 78
Cdd:PRK10584 7 VEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 --GVQFIHQERLLPASFTVGEALFFGHELRRgpfvDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALI 156
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRG----ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQeIDSLCDEVTVLRNGR 217
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ-LAARCDRRLRLVNGQ 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
269-488 |
2.52e-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: 66.01 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgEAIAQGIALVPEErrsqgisPLL--- 345
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP-ASLRRQIGVVLQD-------VFLfsg 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLTLAGLGrfsrwglLSQRK-----EQAESLRLIDELA--IKTP-GPQAavSQLSGGNQQKVALGKWLSRRSAVYL 417
Cdd:COG2274 564 TIRENITLGDPD-------ATDEEiieaaRLAGLHDFIEALPmgYDTVvGEGG--SNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 418 LDEPCVGVDVGAKVEIYRVIGRLVEeGAAVLVLSSDLpELLGICDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIV------EDGThEELLA 698
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-203 |
2.95e-11 |
|
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: 66.51 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQFIHQERL 88
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 89 LpasftvgealfFGHELRRG--PFVDRRRQQREAERLLAEY--FELQLPAD-----ALVGE-LNSAERQVLQITRALIRQ 158
Cdd:TIGR00957 1371 L-----------FSGSLRMNldPFSQYSDEEVWWALELAHLktFVSALPDKldhecAEGGEnLSVGQRQLVCLARALLRK 1439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545433469 159 PKILVFDEPSVAlVKREVDQLLRIVKRLRDQGLSILYISHYLQEI 203
Cdd:TIGR00957 1440 TKILVLDEATAA-VDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-224 |
3.07e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQvdaLGV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAerllAEYFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQV----AEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 161 ILVFDEPSVALvkrevDQLLRI-----VKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK11000 154 VFLLDEPLSNL-----DAALRVqmrieISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
253-472 |
3.13e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 253 GEPLLqVRGLnlARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSihlegrLLRLRSPGEAIA 326
Cdd:PRK11247 10 GTPLL-LNAV--SKRYgertvlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE------LLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 327 QGIALVPEERRsqgISPLLSVLENLtlaGLGRFSRWgllsqRKEQAESLRLIDeLAIKTPGPQAAvsqLSGGNQQKVALG 406
Cdd:PRK11247 81 EDTRLMFQDAR---LLPWKKVIDNV---GLGLKGQW-----RDAALQALAAVG-LADRANEWPAA---LSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 407 KWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-219 |
3.27e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD---SGQVSIDGQPYAALSPRQVDAlgvqFIHQERLLPASFTV 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA----YVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 GEALFFGHELRRGPFVDRRRQQREAERLLAEyFELQLPADALVGE------LNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQA-LGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 170 ALVKREVDQLLRIVKRLRDQGLSILYISHylQ---EIDSLCDEVTVLRNGRDV 219
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH--QpssELFELFDKIILMAEGRVA 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-212 |
3.28e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIH-----GLVGENGAGKSTLIKVLAGIHKADSGQVSIDgqpyaalsprqvdaLGVQFIHQeRLLPASF 93
Cdd:PRK13409 350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISYKPQ-YIKPDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 -TVGEAL----------FFGHELRRGpfvdrrrqqreaerllaeyfeLQLPA--DALVGELNSAERQVLQITRALIRQPK 160
Cdd:PRK13409 415 gTVEDLLrsitddlgssYYKSEIIKP---------------------LQLERllDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 161 ILVFDEPSVALvkrEVDQLL---RIVKRL-RDQGLSILYISHYLQEIDSLCDEVTV 212
Cdd:PRK13409 474 LYLLDEPSAHL---DVEQRLavaKAIRRIaEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
269-472 |
4.18e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR---LLRLrspgeaiaqGIALVPEerrsqgisplL 345
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLEL---------GAGFHPE----------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLTLAG--LGrfsrwglLSqRKEQAESLRLIDELA-----IKTPgpqaaVSQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:COG1134 104 TGRENIYLNGrlLG-------LS-RKEIDEKFDEIVEFAelgdfIDQP-----VKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 419 DEpcvGVDVG-----AKVeiYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG1134 171 DE---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
263-480 |
7.80e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaiaqGIALVPEER 336
Cdd:PRK10619 10 DLHKRYGEhevlkgVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKD----GQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 RSQGISPLLS-------------VLENLTLAGLGRFSrwglLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQQKV 403
Cdd:PRK10619 86 QLRLLRTRLTmvfqhfnlwshmtVLENVMEAPIQVLG----LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 404 ALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGE 480
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-220 |
8.06e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAdSGQVSIDGQPYAALSPRQvdaLGVQ--FIHQERLLPASFTVGEAL- 99
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAE---LARHraYLSQQQSPPFAMPVFQYLa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 100 FFGHELRRGPFVDRRRQQreaerlLAEYFELQLPADALVGELNSAERQ-------VLQITRALIRQPKILVFDEPSVALV 172
Cdd:COG4138 92 LHQPAGASSEAVEQLLAQ------LAEALGLEDKLSRPLTQLSGGEWQrvrlaavLLQVWPTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 173 KREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
269-471 |
8.60e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.33 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeaiaqgIALVPEErrsqgisPLL--- 345
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQE-------PWIqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLtLAGLgRFSrwgllSQRKEQA-ESLRLIDELAIKTPGPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:cd03250 81 TIRENI-LFGK-PFD-----EERYEKViKACALEPDLEILPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 421 PCVGVD--VGAKVeIYRVIGRLVEEGAAVlVLSSDLPELLGICDRILVLHRGE 471
Cdd:cd03250 154 PLSAVDahVGRHI-FENCILGLLLNNKTR-ILVTHQLQLLPHADQIVVLDNGR 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
269-421 |
9.30e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.19 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGE---AIAQGIALVPeerrsqgispLL 345
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--PVTGPGAdrgVVFQKDALLP----------WL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLEN----LTLAGLGRfsrwgllSQRKEQAES-LRLID--ELAiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:COG4525 92 NVLDNvafgLRLRGVPK-------AERRARAEElLALVGlaDFA------RRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
...
gi 2545433469 419 DEP 421
Cdd:COG4525 159 DEP 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-216 |
1.09e-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: 64.65 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATL--ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGV- 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 -QFIHQERLLpasfTVGEALFFGHELRRGPFVDRRRQQREAERLLAeyfeLQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:TIGR01257 2018 pQFDAIDDLL----TGREHLYLYARLRGVPAEEIEKVANWSIQSLG----LSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 160 KILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-216 |
1.29e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVQFIHQERLLPASf 93
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrKHIGIVFQNPDNQFVGS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRRGPFVDRRRQQREAErllaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVK 173
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEAL----KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545433469 174 REVDQLLRIVKRLR-DQGLSILYISHYLQE-IDSlcDEVTVLRNG 216
Cdd:PRK13648 176 DARQNLLDLVRKVKsEHNITIISITHDLSEaMEA--DHVIVMNKG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
1.33e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVQFIHQERLLPASfT 94
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrSKVGLVFQDPDDQVFSS-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFG---HELRRGPfVDRRRQQREAERLLAEYfelqlpADALVGELNSAERQVLQITRALIRQPKILVFDEPSVAL 171
Cdd:PRK13647 97 VWDDVAFGpvnMGLDKDE-VERRVEEALKAVRMWDF------RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 172 VKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIA 233
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-427 |
1.39e-10 |
|
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: 63.42 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 5 HLQHLRKRFGAT-LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQvsidgqpyAALSPrqvdALGVQFI 83
Cdd:TIGR03719 6 TMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQP----GIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALFFG-HELRR---------GPFVDrrrQQREAERLLAEYFELQ---------------------- 131
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGvAEIKDaldrfneisAKYAE---PDADFDKLAAEQAELQeiidaadawdldsqleiamdal 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 132 -LPA-DALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLR---------------------- 187
Cdd:TIGR03719 151 rCPPwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPgtvvavthdryfldnvagwile 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 188 -DQGLSILYISHYLQEID------------------SLCDEVTVLRNGrdvavVEPRHTSS-AQIARL--MVNREVQEMY 245
Cdd:TIGR03719 231 lDRGRGIPWEGNYSSWLEqkqkrleqeekeesarqkTLKRELEWVRQS-----PKGRQAKSkARLARYeeLLSQEFQKRN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 246 PKAQV------ELGEPLLQVRglNLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLeg 313
Cdd:TIGR03719 306 ETAEIyippgpRLGDKVIEAE--NLTKAFgdklliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 314 rllrlrspGEAIAqgIALVPEERRS--------QGISPLLSVL-----ENLTLAGLGRFSRWGLLSQRKeqaeslrlide 380
Cdd:TIGR03719 382 --------GETVK--LAYVDQSRDAldpnktvwEEISGGLDIIklgkrEIPSRAYVGRFNFKGSDQQKK----------- 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2545433469 381 laiktpgpqaaVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:TIGR03719 441 -----------VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-223 |
1.46e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP-----YAALSPRqvdalgVQFIHQE---RLL 89
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdYSYRSQR------IRMIFQDpstSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 90 PASfTVGEALFFghELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:PRK15112 102 PRQ-RISQILDF--PLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 170 ALVKREVDQLLRIVKRLRD-QGLSILYISHYLQEIDSLCDEVTVLRNGRdvaVVE 223
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGE---VVE 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-224 |
1.53e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 12 RFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPY-----AALSPRQVDALGVQFIHQE 86
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 87 RLLP-----ASFTVGEALFFGHELRRGpfVDRRRQQREaerllAEYFELQlPADALvgelNSAERQVLQITRALIRQPKI 161
Cdd:PRK13638 90 IFYTdidsdIAFSLRNLGVPEAEITRR--VDEALTLVD-----AQHFRHQ-PIQCL----SHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 162 LVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-212 |
1.73e-10 |
|
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: 61.27 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIH-----GLVGENGAGKSTLIKVLAGIHKADSGQVSIDGqPYAALSPRQVDAlgvQFIHQERLLPASF 93
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQYIKA---DYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 T--VGEALFFGHELRRgPfvdrrrqqreaerllaeyfeLQLPA--DALVGELNSAERQVLQITRALIRQPKILVFDEPSV 169
Cdd:cd03237 86 TkdFYTHPYFKTEIAK-P--------------------LQIEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 170 ALvkrEVDQLL---RIVKRLRDQGLS-ILYISHYLQEIDSLCDEVTV 212
Cdd:cd03237 145 YL---DVEQRLmasKVIRRFAENNEKtAFVVEHDIIMIDYLADRLIV 188
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-217 |
1.75e-10 |
|
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: 63.23 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 14 GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPrqvDALGvQFIH---QE-RLL 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELG-RHIGylpQDvELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 90 PAsfTVGE----------------ALFFG-HELRrgpfvdrrrqqreaerllaeyfeLQLPA--DALVGE----LNSAER 146
Cdd:COG4618 419 DG--TIAEniarfgdadpekvvaaAKLAGvHEMI-----------------------LRLPDgyDTRIGEggarLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 147 QVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIdSLCDEVTVLRNGR 217
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL-AAVDKLLVLRDGR 543
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
271-472 |
1.76e-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: 60.88 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlRSPGEAIaqgialvPEERRSQGIS-------P 343
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAI-------PYLRRKIGVVfqdfrllP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLSVLENLTLAGlgRFSRWGLLSQRKEQAESLRLIDeLAIKTpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03292 92 DRNVYENVAFAL--EVTGVPPREIRKRVPAALELVG-LSHKH---RALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
274-466 |
1.86e-10 |
|
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: 61.27 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 274 ELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaQGIALVPEERRSQGISPLLSVLENLTl 353
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-------------DTVSYKPQYIKADYEGTVRDLLSSIT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 354 AGLGRFSRWgllsqRKEQAESLRLIDELaiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEI 433
Cdd:cd03237 87 KDFYTHPYF-----KTEIAKPLQIEQIL-------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....
gi 2545433469 434 YRVIGRLVEEG-AAVLVLSSDLPELLGICDRILV 466
Cdd:cd03237 155 SKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIV 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-223 |
2.11e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQ-----PYAALSPRQVDAL 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 79 GVQ---FIHQE-----RL-LPASFTVGEALF------FGhELRRgpfvdrrrqqrEAERLLAeyfELQLPA---DALVGE 140
Cdd:PRK11701 87 LRTewgFVHQHprdglRMqVSAGGNIGERLMavgarhYG-DIRA-----------TAGDWLE---RVEIDAariDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 141 LNSAERQVLQITRALIRQPKILVFDEPS----VALVKREVDQLLRIVkrlRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTggldVSVQARLLDLLRGLV---RELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
....*..
gi 2545433469 217 RdvaVVE 223
Cdd:PRK11701 229 R---VVE 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
256-449 |
2.11e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 256 LLQVRGLNLAR--R--YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrspgeaiAQGial 331
Cdd:PRK13538 1 MLEARNLACERdeRilFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--------RQR--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 332 vpEERRSQ--------GISPLLSVLENLT----LAG-LGRFSRWGLLSQ----RKEqaeslrlidelaiktpgpQAAVSQ 394
Cdd:PRK13538 70 --DEYHQDllylghqpGIKTELTALENLRfyqrLHGpGDDEALWEALAQvglaGFE------------------DVPVRQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 395 LSGGNQQKVALGK-WLSRRsAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLV 449
Cdd:PRK13538 130 LSAGQQRRVALARlWLTRA-PLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
261-475 |
2.12e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 61.36 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 261 GLNLARRYRQ----IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRL-RSPGEAIAQGIALVPE 334
Cdd:TIGR02769 16 GLFGAKQRAPvltnVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdLYQLdRKQRRAFRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 335 ERRSqGISPLLSV-------LENLTLaglgrfsrwglLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQQKVALGK 407
Cdd:TIGR02769 96 DSPS-AVNPRMTVrqiigepLRHLTS-----------LDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 408 WLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-213 |
2.17e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 6 LQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPrqvdalgvQFIHQ 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVP--------QKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPasftvgeaLFFGHELRRGPFVDRRRQQREAERLLAEYFeLQLPADALVGelnsAERQVLQITRALIRQPKILVFD 165
Cdd:PRK09544 79 DTTLP--------LTVNRFLRLRPGTKKEDILPALKRVQAGHL-IDAPMQKLSG----GETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545433469 166 EPSVALVKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVL 213
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-217 |
2.17e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 8 HLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALgVQFIHQER 87
Cdd:PLN03232 1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 LL---PASFTVG-----------EALFFGH---ELRRGPFvdrrrqqreaeRLLAEYFElqlpadalVGE-LNSAERQVL 149
Cdd:PLN03232 1320 VLfsgTVRFNIDpfsehndadlwEALERAHikdVIDRNPF-----------GLDAEVSE--------GGEnFSVGQRQLL 1380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 150 QITRALIRQPKILVFDEpSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSlCDEVTVLRNGR 217
Cdd:PLN03232 1381 SLARALLRRSKILVLDE-ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
265-473 |
2.68e-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: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 265 ARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGvvRADSGSIhLEGRLL---RLRSPGEaIAQGIALVPEERR 337
Cdd:cd03234 16 WNKYARIlndvSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGT-TSGQILfngQPRKPDQ-FQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 338 sqgISPLLSVLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDeLAIKTPGpQAAVSQLSGGNQQKVALGKWLSRRSAVYL 417
Cdd:cd03234 92 ---LLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRD-LALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 418 LDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVL----SSDLPELLgicDRILVLHRGEIA 473
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTihqpRSDLFRLF---DRILLLSSGEIV 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
252-475 |
2.99e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 252 LGEPLLQVRGLNL----ARRY--RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrspgeai 325
Cdd:PRK13635 1 MKEEIIRVEHISFrypdAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 326 aqgIALVPEERRSQGIspllsVLENLTLAGLGRFSR----WGLLSQRKEQAESLRLIDElAIKTPGPQAAVSQ----LSG 397
Cdd:PRK13635 73 ---EETVWDVRRQVGM-----VFQNPDNQFVGATVQddvaFGLENIGVPREEMVERVDQ-ALRQVGMEDFLNRephrLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 398 GNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAA-VLVLSSDLPELLGiCDRILVLHRGEIAGE 475
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-198 |
3.00e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 17 LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYA---ALSPRQVDALGvqfiHQERLLPaSF 93
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlCTYQKQLCFVG----HRSGINP-YL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRRGPFvdrrrqqreAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVK 173
Cdd:PRK13540 90 TLRENCLYDIHFSPGAV---------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*
gi 2545433469 174 REVDQLLRIVKRLRDQGLSILYISH 198
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
271-473 |
3.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG--------RLLRLRSP-------------GEAIAQGI 329
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKvglvfqypeyqlfEETIEKDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 330 ALVPeerRSQGISP---LLSVLENLTLAGLGRfsrwgllsqrkeqaeslrliDELAIKTPgpqaavSQLSGGNQQKVALG 406
Cdd:PRK13637 106 AFGP---INLGLSEeeiENRVKRAMNIVGLDY--------------------EDYKDKSP------FELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 407 KWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSS-DLPELLGICDRILVLHRGEIA 473
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVShSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
278-475 |
3.73e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 278 GEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSpGEAIAQGIALVPEErrsqgisplLSVLENLT---LA 354
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQ---------LPAAEGMTvreLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 355 GLGRFSRWGLLSQ-----RKEQAESLRLIDelaiKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGA 429
Cdd:PRK10575 107 AIGRYPWHGALGRfgaadREKVEEAISLVG----LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 430 KVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK10575 183 QVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-62 |
3.78e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 3.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 7 QHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI 62
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-198 |
3.84e-10 |
|
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: 58.70 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIdgqpyaalsPRQVDALgvqFIHQERLLPASfTVGEA 98
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLL---FLPQRPYLPLG-TLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 99 LFFghelrrgPFVDrrrqqreaerllaeyfelqlpadalvgELNSAERQVLQITRALIRQPKILVFDEPSVALvkrEVDQ 178
Cdd:cd03223 84 LIY-------PWDD---------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSAL---DEES 126
|
170 180
....*....|....*....|
gi 2545433469 179 LLRIVKRLRDQGLSILYISH 198
Cdd:cd03223 127 EDRLYQLLKELGITVISVGH 146
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
257-476 |
4.11e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 59.81 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLarRYRQ--------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR------LLRLRSpg 322
Cdd:cd03244 3 IEFKNVSL--RYRPnlppvlknISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskigLHDLRS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 323 eaiaqGIALVPEErrsqgisPLL---SVLENltLAGLGRFS---RWGLLsqrkEQAESLRLIDELAIKTPGPQAAV-SQL 395
Cdd:cd03244 79 -----RISIIPQD-------PVLfsgTIRSN--LDPFGEYSdeeLWQAL----ERVGLKEFVESLPGGLDTVVEEGgENL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 396 SGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLHRGEIAgE 475
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV-E 217
|
.
gi 2545433469 476 F 476
Cdd:cd03244 218 F 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-472 |
4.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLrspGEAIAQGIALvpEERRSQGIS------ 342
Cdd:PRK14246 27 KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYF---GKDIFQIDAI--KLRKEVGMVfqqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 -PLLSVLENLTLAglgrFSRWGLLSQR---KEQAESLR---LIDELAIKTPGPqaaVSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:PRK14246 102 fPHLSIYDNIAYP----LKSHGIKEKReikKIVEECLRkvgLWKEVYDRLNSP---ASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVlSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIV-SHNPQQVARVADYVAFLYNGEL 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
275-470 |
4.27e-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: 62.72 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 275 LRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspgeaiaqgIALVPEERRSQGISPLLSVLENLtLA 354
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISDVHQNMGYCPQFDAIDDL-LT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 355 GLGRFSRWGLLsqRKEQAESLRLIDELAIKTPGPQAAVSQL----SGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAK 430
Cdd:TIGR01257 2029 GREHLYLYARL--RGVPAEEIEKVANWSIQSLGLSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 431 VEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
269-483 |
4.40e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRL-RSPGEAIAQGIALVPEERRSqGISPLLS 346
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLnRAQRKAFRRDIQMVFQDSIS-AVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLT--LAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:PRK10419 108 VREIIRepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPP------QLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 425 VDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGS 483
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
254-470 |
4.65e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLARR--------YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRAD---SGSIHLEGR-------- 314
Cdd:PRK09473 10 DALLDVKDLRVTFStpdgdvtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilnlpek 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 315 -LLRLRspgeaiAQGIALVPEERRSQgISPLLSVLENLTLA-----GLGrfsrwgllsqrKEQA--ESLRLIDelAIKTP 386
Cdd:PRK09473 90 eLNKLR------AEQISMIFQDPMTS-LNPYMRVGEQLMEVlmlhkGMS-----------KAEAfeESVRMLD--AVKMP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 387 GPQAAVS----QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGIC 461
Cdd:PRK09473 150 EARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGIC 229
|
....*....
gi 2545433469 462 DRILVLHRG 470
Cdd:PRK09473 230 DKVLVMYAG 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
271-472 |
5.35e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSpgeaIAQ-GIALVPEerrSQGISPLLSVLE 349
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS----IQQrDICMVFQ---SYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 N----LTLAGLGRfsrwgllSQRKEQ-AESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:PRK11432 98 NvgygLKMLGVPK-------EERKQRvKEALELVDLAGFE----DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545433469 425 VDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-231 |
6.42e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAA-LHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV 75
Cdd:PRK10535 1 MTAlLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 DALGVQ---FIHQERLLPASFTVGE-----ALFFGHELRRgpfvdrrrQQREAERLLAEyFELQLPADALVGELNSAERQ 147
Cdd:PRK10535 81 AQLRREhfgFIFQRYHLLSHLTAAQnvevpAVYAGLERKQ--------RLLRAQELLQR-LGLEDRVEYQPSQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 148 VLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQeIDSLCDEVTVLRNGRDVAVVEPRHT 227
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEK 230
|
....
gi 2545433469 228 SSAQ 231
Cdd:PRK10535 231 VNVA 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-470 |
6.45e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.61 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 277 RGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIhlegRLLRLRSPGEAIA--QGIALVPEERRsqgISPLLSVLENLTLa 354
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPDAGKI----TVLGVPVPARARLarARIGVVPQFDN---LDLEFTVRENLLV- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 355 glgrFSRWGLLSQRKEQAESLRLIdELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIY 434
Cdd:PRK13536 138 ----FGRYFGMSTREIEAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190
....*....|....*....|....*....|....*.
gi 2545433469 435 RVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK13536 213 ERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-224 |
6.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIdGQPYAALSPRQVD------ALGVQFIHQERL 88
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEikpvrkKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 89 LPASfTVGEALFFGHE---LRRGPFVDRRRQQREAERLLAEYFElQLPAdalvgELNSAERQVLQITRALIRQPKILVFD 165
Cdd:PRK13643 97 LFEE-TVLKDVAFGPQnfgIPKEKAEKIAAEKLEMVGLADEFWE-KSPF-----ELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 166 EPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
270-472 |
7.03e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspgEAIAQGIALVPEERRsqgIS------- 342
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------FDAEKGICLPPEKRR---IGyvfqdar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 --PLLSVLENLtlaglgrfsRWGLlsQRKEQAESLRLIDELAIKT-----PgpqaavSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:PRK11144 87 lfPHYKVRGNL---------RYGM--AKSMVAQFDKIVALLGIEPlldryP------GSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-217 |
7.67e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG---QPYAALSPRQVDALGVQFIH-------- 84
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVALVSQNVHlfndtian 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 85 -----------QERLLPASfTVGEALFFGHELRRGpfvdrrrqqreaerllaeyfelqlpADALVGE----LNSAERQVL 149
Cdd:PRK11176 436 niayarteqysREQIEEAA-RMAYAMDFINKMDNG-------------------------LDTVIGEngvlLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 150 QITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVKRLRdqglSILYISHYLQEIDSlCDEVTVLRNGR 217
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALdteSERAIQAALDELQKNR----TSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
270-473 |
8.00e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrlLRLRSPGeaiaqgiALVPEERRSQGIS------- 342
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK-------VDERLIRQEAGMVfqqfylf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 PLLSVLENLTlaglgrFSRWGLLSQRKEQAESLRLidELAIKTPGPQAA---VSQLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:PRK09493 90 PHLTALENVM------FGPLRVRGASKEEAEKQAR--ELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
271-469 |
9.76e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLrlrspgeaiaqgIALVPEERRSQGISPLLsvlen 350
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR------------IGYVPQKLYLDTTLPLT----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 ltlagLGRFSRWGLLSQRKEQAESLRLIDELAIKtpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAK 430
Cdd:PRK09544 86 -----VNRFLRLRPGTKKEDILPALKRVQAGHLI----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 431 VEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHR 469
Cdd:PRK09544 157 VALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-224 |
9.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.86 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI----------DGQPYAALSPRQVDalgvQFIHQER 87
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIK----NFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 LLPASFTVGEALFFGHELRR----GPfVDRRRQQREAERLLAEYFE-LQLPADALVG---ELNSAERQVLQITRALIRQP 159
Cdd:PRK13631 117 RVSMVFQFPEYQLFKDTIEKdimfGP-VALGVKKSEAKKLAKFYLNkMGLDDSYLERspfGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 160 KILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-219 |
1.05e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP-YAALSPRQVDALG----VQFIHQERLLPASF 93
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlYFGKDIFQIDAIKlrkeVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFF---GHELRRGPFVDRRRQQREAERLLAE--YFELQLPADALVGelnsAERQVLQITRALIRQPKILVFDEPS 168
Cdd:PRK14246 106 SIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWKevYDRLNSPASQLSG----GQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 169 VALVKREVDQLLRIVKRLRDQgLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
269-472 |
1.07e-09 |
|
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: 57.61 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRsqgispLL--S 346
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE-LGDHVGYLPQDDE------LFsgS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLtlaglgrfsrwgllsqrkeqaeslrlidelaiktpgpqaavsqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD 426
Cdd:cd03246 92 IAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 427 VGAKVEIYRVIGRLVEEGAAVLVLSSDlPELLGICDRILVLHRGEI 472
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-232 |
1.21e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVdALGVQ 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV-ARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 FIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKI 161
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 162 LVFDEPSVAL-VKREVDqLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRHTSSAQI 232
Cdd:PRK10253 165 MLLDEPTTWLdISHQID-LLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-224 |
1.24e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQvSIDGQ---PYAALSPRQVDALgvqfihqERLLPASFT 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaiPANLKKIKEVKRL-------RKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALFFGHELRR----GPfVDRRRQQREAERLLAEYFEL-QLPADALVG---ELNSAERQVLQITRALIRQPKILVFDE 166
Cdd:PRK13645 98 FPEYQLFQETIEKdiafGP-VNLGENKQEAYKKVPELLKLvQLPEDYVKRspfELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 167 PSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEP 224
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-468 |
1.24e-09 |
|
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: 58.92 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 364 LLSQRKEQAESLRLIDELAIKtPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE 443
Cdd:cd03236 110 LLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED 188
|
90 100
....*....|....*....|....*
gi 2545433469 444 GAAVLVLSSDLPELLGICDRILVLH 468
Cdd:cd03236 189 DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
271-472 |
1.32e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG----RL-LRLRSPGeAIAQGIALVPEerrsqgisplL 345
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsRLhARDRKVG-FVFQHYALFRH----------M 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLT--LAGLGRFSRWGLLSQRKEQAESLRLI--DELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEP 421
Cdd:PRK10851 90 TVFDNIAfgLTVLPRRERPNAAAIKAKVTQLLEMVqlAHLADRYP------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 422 CVGVDVGAKVEIYRVIGRLVEE--GAAVLVlSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElkFTSVFV-THDQEEAMEVADRVVVMSQGNI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
257-444 |
1.46e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYRQ----IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAiAQGIALv 332
Cdd:PRK11124 3 IQLNGINCFYGAHQalfdITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSD-KAIREL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 peeRRSQGIS-------PLLSVLENLTLA-----GLGRfsrwgllSQRKEQAESL--RL-IDELAIKTPgpqaavSQLSG 397
Cdd:PRK11124 81 ---RRNVGMVfqqynlwPHLTVQQNLIEApcrvlGLSK-------DQALARAEKLleRLrLKPYADRFP------LHLSG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 398 GNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEG 444
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-220 |
1.75e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 31 IHGLVGENGAGKSTLIKVLAGIHKADSGQVSI------DGQPYAALSPRQvdaLGVQFIHQE-RLLPaSFTVGEALFFGH 103
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEK---RRIGYVFQDaRLFP-HYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 104 ELRRGPFVDRRRQQREAERLLAEYfelqlPADalvgeLNSAERQVLQITRALIRQPKILVFDEPSVAL---VKREvdqLL 180
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEPLLDRY-----PGS-----LSGGEKQRVAIGRALLTAPELLLMDEPLASLdlpRKRE---LL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2545433469 181 RIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK11144 169 PYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
259-472 |
1.76e-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: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 259 VRGLnLARRYRQ------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRL-LRLRspgEAIAQGIAL 331
Cdd:COG4586 24 LKGL-FRREYREveavddISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRR---KEFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 332 VPEErRSQgispL---LSVLENLTLagLGRFsrWGLlsqrkEQAESLRLIDELA--------IKTPgpqaaVSQLSGGNQ 400
Cdd:COG4586 100 VFGQ-RSQ----LwwdLPAIDSFRL--LKAI--YRI-----PDAEYKKRLDELVelldlgelLDTP-----VRQLSLGQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 401 QKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-198 |
2.29e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 34 LVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPR-QVDALGvqfiHQERLLPAsFTVGEALFFGHELRRGPFVD 112
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeACHYLG----HRNAMKPA-LTVAENLEFWAAFLGGEELD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 113 RRRQqreaerllAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLS 192
Cdd:PRK13539 108 IAAA--------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI 179
|
....*.
gi 2545433469 193 ILYISH 198
Cdd:PRK13539 180 VIAATH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-60 |
3.27e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 3.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV 60
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
270-444 |
3.98e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRS-PGEAIAQgialvpEERRSQGIS------ 342
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQkPSEKAIR------LLRQKVGMVfqqynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 -PLLSVLENLTLAGLGrfsrwgLLSQRKEQA--ESLRLIDELAIkTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:COG4161 94 wPHLTVMENLIEAPCK------VLGLSKEQAreKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180
....*....|....*....|....*
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLVEEG 444
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTG 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
254-487 |
4.06e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLnlARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHL---EGRLLRLRSPGEA 324
Cdd:PRK11701 4 QPLLSVRGL--TKLYgprkgcRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 325 iaqgialvpeERR--------------SQGISPLLS----VLENLTLAG---LGRF----SRWgllSQRKEQAESlRlID 379
Cdd:PRK11701 82 ----------ERRrllrtewgfvhqhpRDGLRMQVSaggnIGERLMAVGarhYGDIrataGDW---LERVEIDAA-R-ID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 380 ELAiktpgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELL 458
Cdd:PRK11701 147 DLP----------TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVAR 216
|
250 260 270
....*....|....*....|....*....|
gi 2545433469 459 GICDRILVLHRGEIAgefhagEAG-SDQLL 487
Cdd:PRK11701 217 LLAHRLLVMKQGRVV------ESGlTDQVL 240
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-294 |
4.55e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 29 GTIHGLVGENGAGKSTLIKVLAGIHKAD--SGQVSIDGQP-----YAALSP--RQVDalgvqfIHQERLlpasfTVGEAL 99
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPkkqetFARISGycEQND------IHSPQV-----TVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 100 FFGHELR---------RGPFVDRrrqqreaerlLAEYFELQLPADALVG-----ELNSAERQVLQITRALIRQPKILVFD 165
Cdd:PLN03140 975 IYSAFLRlpkevskeeKMMFVDE----------VMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 166 EPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQ-EIDSLCDEVTVLRNGRDVAVVEPRHTSSAQIARLMVN----RE 240
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAipgvPK 1124
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 241 VQEMYPKA--QVELGEPLLQVR-GLNLARRYRQIDLELRRGEIVGLTGLVGSGAKDL 294
Cdd:PLN03140 1125 IKEKYNPAtwMLEVSSLAAEVKlGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDL 1181
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-226 |
5.30e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--GVQFIHQERL--LPASF 93
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrDIQFIFQDPYasLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFfgHELRRGPFVDRRRQQREAERLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVK 173
Cdd:PRK10261 419 TVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 174 REVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV------AVVE-PRH 226
Cdd:PRK10261 497 SIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVeigprrAVFEnPQH 557
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-217 |
6.21e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF----GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD---SGQVSIDGQPYAALSPR 73
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 74 QVDAL---GVQFIHQERL--LPASFTVGEALFFGHELRRGpfvdrrrqqreaeRLLAEYFE--------LQLP-ADALVG 139
Cdd:PRK09473 90 ELNKLraeQISMIFQDPMtsLNPYMRVGEQLMEVLMLHKG-------------MSKAEAFEesvrmldaVKMPeARKRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 140 ----ELNSAERQVLQITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTV 212
Cdd:PRK09473 157 myphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALdvtVQAQIMTLLNELK--REFNTAIIMITHDLGVVAGICDKVLV 234
|
....*
gi 2545433469 213 LRNGR 217
Cdd:PRK09473 235 MYAGR 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-224 |
6.68e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVQFIHQERLLPASfTVGE 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrRKIGMVFQNPDNQFVGA-TVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 98 ALFFGHE---LRRGPFVDRRRQQREAERLLAeyFELQLPAdalvgELNSAERQVLQITRALIRQPKILVFDEPSVALVKR 174
Cdd:PRK13642 102 DVAFGMEnqgIPREEMIKRVDEALLAVNMLD--FKTREPA-----RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 175 EVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSlCDEVTVLRNGRDVAVVEP 224
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
271-471 |
8.90e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgEAIAqgiALVPEERRSQ----GISPLL- 345
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG---------EDIS---TLKPEIYRQQvsycAQTPTLf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 --SVLENLTLAglgrfsrWGLlsqRKEQAESLRLIDELA-IKTPGP--QAAVSQLSGGNQQKVALGKWLSRRSAVYLLDE 420
Cdd:PRK10247 94 gdTVYDNLIFP-------WQI---RNQQPDPAIFLDDLErFALPDTilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 421 PCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPElLGICDRILVL--HRGE 471
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDE-INHADKVITLqpHAGE 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
1.04e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV-----SIDGQPYAALSPRQV 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 DAL--GVQFIHQERLLPASFTVGEALFFGHELRRGpfVDRRRQQREAERLLAEyFELQLPADALVGELNSAERQVLQITR 153
Cdd:PRK11264 81 RQLrqHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAK-VGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
257-472 |
1.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLA----RRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLfgvvradsgsihleGRLLRL----RSPGEAIAQG 328
Cdd:PRK14247 4 IEIRDLKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF--------------NRLIELypeaRVSGEVYLDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 -----IALVPEERRSQGI------SPLLSVLENLTLA-GLGRF--SRWGLLSQRKEQAESLRLIDELAIKTPGPQAavsQ 394
Cdd:PRK14247 70 qdifkMDVIELRRRVQMVfqipnpIPNLSIFENVALGlKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDAPAG---K 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVlSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
254-475 |
1.23e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLARRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlRSPGEAIAQ 327
Cdd:PRK10253 3 ESVARLRGEQLTLGYgkytvaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 328 GIALVPEERRSQGIsplLSVLEnltLAGLGR------FSRWgllsqRKEQAESL-RLIDELAIKTPGPQAaVSQLSGGNQ 400
Cdd:PRK10253 82 RIGLLAQNATTPGD---ITVQE---LVARGRyphqplFTRW-----RKEDEEAVtKAMQATGITHLADQS-VDTLSGGQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 401 QKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-223 |
1.35e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 33 GLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGVqfIHQERLLpASFTVG--------------- 96
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLrKVLGI--IPQAPVL-FSGTVRfnldpfnehndadlw 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 97 EALFFGH---ELRRGPFvdrrrqqreaeRLLAEYFElqlpadalVGELNS-AERQVLQITRALIRQPKILVFDEPSVAlV 172
Cdd:PLN03130 1346 ESLERAHlkdVIRRNSL-----------GLDAEVSE--------AGENFSvGQRQLLSLARALLRRSKILVLDEATAA-V 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 173 KREVDQLlrIVKRLRDQGLS--ILYISHYLQE-IDslCDEVTVLRNGRdvaVVE 223
Cdd:PLN03130 1406 DVRTDAL--IQKTIREEFKSctMLIIAHRLNTiID--CDRILVLDAGR---VVE 1452
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-198 |
1.40e-08 |
|
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: 54.67 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP---RQVDALGv 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephENILYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 qfiHQERLLPAsFTVGEALFFGHELRRGpfvdrrrQQREAERLLAEyFELQLPADALVGELNSAERQVLQITRALIRQPK 160
Cdd:TIGR01189 80 ---HLPGLKPE-LSALENLHFWAAIHGG-------AQRTIEDALAA-VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISH 198
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
270-472 |
1.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.89 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRSQGISPLLSV-- 347
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPDNQFVGATVEDdv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 ---LENLTLAglgrfsrwglLSQRKEQA-ESLRLIDELAIKTPGPqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:PRK13650 104 afgLENKGIP----------HEEMKERVnEALELVGMQDFKEREP----ARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPElLGICDRILVLHRGEI 472
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-217 |
1.52e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVQ- 81
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 -FIHQERLLPASFTVGEALFF--------GHELRRgpfvdRRRQQREAERLL--AEYFELQlpadalvgeLNSAERQVLQ 150
Cdd:PRK10908 82 gMIFQDHHLLMDRTVYDNVAIpliiagasGDDIRR-----RVSAALDKVGLLdkAKNFPIQ---------LSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 151 ITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
253-462 |
1.60e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 253 GEPLLQVRGLNLARRYR----QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG---------RLLRLR 319
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRcifdNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 320 SPGEAIAQGIALVPEerrsqgisplLSVLENLTlaglgrfsrWGLLSQRKEQAESLRLIDELAIKTPGPQAAV----SQL 395
Cdd:PRK11831 84 KRMSMLFQSGALFTD----------MNVFDNVA---------YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAklmpSEL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 396 SGGNQQKVALGKWLSRRSAVYLLDEPCVGVD---VGakveiyrVIGRLVEE-----GAAVLVLSSDLPELLGICD 462
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDpitMG-------VLVKLISElnsalGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
271-472 |
1.72e-08 |
|
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: 54.24 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrSPGEAIAQGIALVPEErrsqgisPLL---SV 347
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLISVLNQR-------PYLfdtTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLtlaglGRfsrwgllsqrkeqaeslrlidelaiktpgpqaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:cd03247 92 RNNL-----GR-----------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 428 GAKVEIYRVIGRLVEEGAAVLVLSsdlpELLGI--CDRILVLHRGEI 472
Cdd:cd03247 132 ITERQLLSLIFEVLKDKTLIWITH----HLTGIehMDKILFLENGKI 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-220 |
2.05e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLiKVLAGIHKADSGQVSIDGQPYAALSPRQVDALG--- 79
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 -VQFIHQErllpaSFTVGEALFFgheLRRGPFVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQ 158
Cdd:NF000106 92 pVR*GRRE-----SFSGRENLYM---IGR*LDLSRKDARARADELL-ERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 159 PKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
163-295 |
2.05e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.15 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 163 VFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIdSLCDEVT------------VLRNGRDVAVVEPRHTSSA 230
Cdd:PRK00635 501 ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIdigpgagifggeVLFNGSPREFLAKSDSLTA 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 231 QIARLMVNREVQEMYPKAQVELgePLLQVRGLNLarryRQIDLELRRGEIVGLTGLVGSGAKDLL 295
Cdd:PRK00635 580 KYLRQELTIPIPEKRTNSLGTL--TLSKATKHNL----KDLTISLPLGRLTVVTGVSGSGKSSLI 638
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-213 |
2.18e-08 |
|
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: 55.07 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 29 GTIHGLVGENGAGKSTLIKVLAGIHKADSGQVS------------------------IDGQPYAALSPRQVDalgvqfih 84
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqnyftklLEGDVKVIVKPQYVD-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 85 qerLLPASF--TVGEALFFGHElrRGPFvdrrrqqreaeRLLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKIL 162
Cdd:cd03236 98 ---LIPKAVkgKVGELLKKKDE--RGKL-----------DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 163 VFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVL 213
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
271-456 |
2.18e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.09 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAiaQGIALvpeerRSQGISPLLSVLEN 350
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAE--RGVVF-----QNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 ----LTLAGLGRfsrwgllSQRKEQA-ESLRLID-ELAIKTPgpqaaVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:PRK11248 91 vafgLQLAGVEK-------MQRLEIAhQMLKKVGlEGAEKRY-----IWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|...
gi 2545433469 425 VDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPE 456
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQEtGKQVLLITHDIEE 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
269-467 |
2.22e-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: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIhlegrllRLRSPGEAI--AQG-----IALvpeeRR---- 337
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-------LVRHDGGWVdlAQAspreiLAL----RRrtig 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 338 --SQ------GISPLLSVLENLTLAGLGRfsrwgllSQRKEQAEslRLIDELAIKTPGPQAAVSQLSGGNQQKVALGKWL 409
Cdd:COG4778 97 yvSQflrvipRVSALDVVAEPLLERGVDR-------EEARARAR--ELLARLNLPERLWDLPPATFSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 410 SRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVL 467
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
271-493 |
2.29e-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: 56.88 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaqGIALVPEERRSQGISpllsVLEN 350
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQAWIQNDS----LREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 LTLAGLGRFSRWgllsqrKEQAESLRLIDELAIKTPGPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD 426
Cdd:TIGR00957 719 ILFGKALNEKYY------QQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 427 VGAKVEIY-RVIGR--LVEEGAAVLVLS--SDLPELlgicDRILVLHRGEIAgefhagEAGSDQLLACATGA 493
Cdd:TIGR00957 793 AHVGKHIFeHVIGPegVLKNKTRILVTHgiSYLPQV----DVIIVMSGGKIS------EMGSYQELLQRDGA 854
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
255-487 |
2.84e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 55.68 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNL-----ARRYRQID---LELRRGEIVGLTGLVGSGaKDLL-KTLFGV------VRADsgSIHLEGR-LLRL 318
Cdd:COG4170 2 PLLDIRNLTIeidtpQGRVKAVDrvsLTLNEGEIRGLVGESGSG-KSLIaKAICGItkdnwhVTAD--RFRWNGIdLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 319 rSPGE---AIAQGIALVPEERR-----SQGISP-LLSVLENLTLAglGRFsrWGLLSQRKEQAesLRLIDELAIKTpgPQ 389
Cdd:COG4170 79 -SPRErrkIIGREIAMIFQEPSscldpSAKIGDqLIEAIPSWTFK--GKW--WQRFKWRKKRA--IELLHRVGIKD--HK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 390 AAVS----QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRI 464
Cdd:COG4170 150 DIMNsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTI 229
|
250 260
....*....|....*....|....
gi 2545433469 465 LVLHRGEIAgefhagEAGS-DQLL 487
Cdd:COG4170 230 TVLYCGQTV------ESGPtEQIL 247
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
255-449 |
3.42e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNLARR----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQgIA 330
Cdd:PRK13543 10 PLLAAHALAFSRNeepvFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-LG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPeerrsqGISPLLSVLENLTLAGlgrfsrwGLLSQRKEQAESlrliDELAIK--TPGPQAAVSQLSGGNQQKVALGK- 407
Cdd:PRK13543 89 HLP------GLKADLSTLENLHFLC-------GLHGRRAKQMPG----SALAIVglAGYEDTLVRQLSAGQKKRLALARl 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2545433469 408 WLSRrSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLV 449
Cdd:PRK13543 152 WLSP-APLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALV 192
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-236 |
3.53e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGiHKA---DSGQVSIDGQPYAALSPRQVDALGV 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 81 QFIHQERLLPASFTVGEALFFGHELRRG----PFVDRRrqqreaerllaEYFELQLPADALVG--------ELNS----A 144
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAYNSKRKfqglPELDPL-----------EFLEIINEKLKLVGmdpsflsrNVNEgfsgG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 145 ERQVLQITRALIRQPKILVFDEPSVALvkrEVDQLLRI---VKRLRDQGLSILYISHYLQEIDSLC-DEVTVLRNGRDVa 220
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGL---DIDALKIIaegINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKII- 231
|
250
....*....|....*.
gi 2545433469 221 vveprHTSSAQIARLM 236
Cdd:CHL00131 232 -----KTGDAELAKEL 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
269-472 |
3.55e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR---------LLRLRSPGEA-IAQGIALVPEerrs 338
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadaLAQLRREHFGfIFQRYHLLSH---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 339 qgisplLSVLENLTL----AGLGRfsrwgllSQRKEQAESL--RL-IDELAIKTPgpqaavSQLSGGNQQKVALGKWLSR 411
Cdd:PRK10535 101 ------LTAAQNVEVpavyAGLER-------KQRLLRAQELlqRLgLEDRVEYQP------SQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 412 RSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDlPELLGICDRILVLHRGEI 472
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
269-471 |
3.68e-08 |
|
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: 54.86 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeaiaqgIALVPEerrSQGISPLlSVL 348
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ---FSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLtLAGLG----RFSRWGLLSQRKEQAESLRLIDelaiKTPGPQAAVSqLSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:cd03291 116 ENI-IFGVSydeyRYKSVVKACQLEEDITKFPEKD----NTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 425 VDVGAKVEIY-RVIGRLVEEGAAVLVLSSdlPELLGICDRILVLHRGE 471
Cdd:cd03291 190 LDVFTEKEIFeSCVCKLMANKTRILVTSK--MEHLKKADKILILHEGS 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-198 |
3.82e-08 |
|
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: 53.65 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAalSPRQVDALGVQFIHQERLLPASFTVGEALFFG 102
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 103 HelrrgPFVDRRRQQREAERLLAEYFElqlpaDALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRI 182
Cdd:cd03231 98 H-----ADHSDEQVEEALARVGLNGFE-----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 2545433469 183 VKRLRDQGLSILYISH 198
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-225 |
4.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG-QPYAALSPRQVDAL----GVQFIHQERLLP 90
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNKNLKKLrkkvSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 91 ASfTVGEALFFGHelRRGPFVDRRRQQREAERLLAEYFELQLpADALVGELNSAERQVLQITRALIRQPKILVFDEPSVA 170
Cdd:PRK13641 100 EN-TVLKDVEFGP--KNFGFSEDEAKEKALKWLKKVGLSEDL-ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 171 LVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
269-475 |
4.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.61 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIALVPEERRSQGI-----SP 343
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQFVgrtveED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLSVLENLTLAGLGrfsrwglLSQRKEQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:PRK13644 99 LAFGPENLCLPPIE-------IRKRVDRALAEIGLEKYRHRSP------KTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 424 GVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPElLGICDRILVLHRGEIAGE 475
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
379-468 |
4.37e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 379 DELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGA-AVLVLSSDLPEL 457
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL 135
|
90
....*....|.
gi 2545433469 458 LGICDRILVLH 468
Cdd:cd03222 136 DYLSDRIHVFE 146
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
271-480 |
4.60e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRLRSpgeaiaqgiALVPEERRSQGI----SPLL 345
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKN---------REVPFLRRQIGMifqdHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 ---SVLENLTLAGLGRFSRWGLLSQRKEQA-ESLRLIDElAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEP 421
Cdd:PRK10908 92 mdrTVYDNVAIPLIIAGASGDDIRRRVSAAlDKVGLLDK-AKNFP------IQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 422 CVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEfHAGE 480
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG-VGGE 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
257-472 |
4.75e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlarryrQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEA---IAQGIALV- 332
Cdd:PRK13641 18 MEKKGLD------NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkkLRKKVSLVf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 333 --PEERRSQGispllSVLENLTLAGLGrfsrWGLLSQR-KEQA----ESLRLIDELAIKTPgpqaavSQLSGGNQQKVAL 405
Cdd:PRK13641 92 qfPEAQLFEN-----TVLKDVEFGPKN----FGFSEDEaKEKAlkwlKKVGLSEDLISKSP------FELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 406 GKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-219 |
5.23e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 10 RKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAD---SGQVSIDGQPYA-ALSPRQVDALgvqFIHQ 85
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKeFAEKYPGEII---YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 86 ERLLPASFTVGEALffghelrrgpfvdrrrqqreaerllaeYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFD 165
Cdd:cd03233 91 EDVHFPTLTVRETL---------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 166 EPSVALvkrEVDQLLRIVKRLRDQ----GLSILyISHYL--QEIDSLCDEVTVLRNGRDV 219
Cdd:cd03233 144 NSTRGL---DSSTALEILKCIRTMadvlKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
271-488 |
5.49e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 55.52 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEErrsqgisPLL---SV 347
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINYLPQE-------PYIfsgSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLAglgrfSRWGLLSQRKEQAESLRLIDELAIKTP-GPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYLLDEPC 422
Cdd:TIGR01193 565 LENLLLG-----AKENVSQDEIWAACEIAEIKDDIENMPlGYQTELSEegssISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 423 VGVDVgakVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:TIGR01193 640 SNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKII------EQGShDELLD 697
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
269-488 |
5.66e-08 |
|
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: 53.77 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGrllrlrspgeaiaQGIALVPEE--RRSQGISPLLS 346
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG-------------QDIREVTLDslRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTP-GPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYLLDEP 421
Cdd:cd03253 85 VLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPdGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 422 CVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:cd03253 165 TSALDTHTEREIQAAL-RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV------ERGThEELLA 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-219 |
6.29e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 17 LALDDASLKV-ERGTIhGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSpRQVDALGVQFIHQER-LLPASFT 94
Cdd:PRK10790 355 LVLQNINLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDPvVLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 VGEALffGHELRrgpfvDRRRQQREAERLLAEyFELQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEPS 168
Cdd:PRK10790 433 ANVTL--GRDIS-----EEQVWQALETVQLAE-LARSLPDglYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 169 VAL---VKREVDQLLRIVKrlrdQGLSILYISHYLQEIDSlCDEVTVLRNGRDV 219
Cdd:PRK10790 505 ANIdsgTEQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
271-484 |
6.34e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.93 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE-AIAQGIALVPEERRSQGISPllSVLE 349
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlEVRKTVGIVFQNPDDQLFAP--TVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 NLTLAGLGrfsrWGLLSQRKEQ--AESLRLIDELAIKTPGPQaavsQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDV 427
Cdd:PRK13639 99 DVAFGPLN----LGLSKEEVEKrvKEALKAVGMEGFENKPPH----HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 428 GAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGSD 484
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
269-475 |
6.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE---AIAQGIALVPEERRSQGISpll 345
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirPVRKRIGMVFQFPESQLFE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLTLAGLGRFSRwgLLSQRKEQAesLRLIDELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGV 425
Cdd:PRK13646 101 DTVEREIIFGPKNFKM--NLDEVKNYA--HRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 426 DVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK13646 177 DPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
255-475 |
9.93e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRglNLARRY----------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL-RLRSPGE 323
Cdd:PRK11629 4 ILLQCD--NLCKRYqegsvqtdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 324 A---------IAQGIALVPEerrsqgisplLSVLENLTLAGLgrfsrWGLLSQRKEQAESLRLIDELAIKTPGpQAAVSQ 394
Cdd:PRK11629 82 AelrnqklgfIYQFHHLLPD----------FTALENVAMPLL-----IGKKKPAEINSRALEMLAAVGLEHRA-NHRPSE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLpELLGICDRILVLHRGEIA 473
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLT 224
|
..
gi 2545433469 474 GE 475
Cdd:PRK11629 225 AE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-226 |
1.08e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI-DGQPYAALSPRQVDAL----GVQFIHQERLL 89
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLrkkvGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 90 ------------PASFTVGEAlffghelrrgpfvdrrrqqrEAERLLAEYFEL-QLPADALVG---ELNSAERQVLQITR 153
Cdd:PRK13634 99 feetvekdicfgPMNFGVSEE--------------------DAKQKAREMIELvGLPEELLARspfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 154 ALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVAVVEPRH 226
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-225 |
1.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 16 TLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSP----RQvdALGVQFIHQERLLPA 91
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdiRN--KAGMVFQNPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 92 SFtVGEALFFG--------HELRRGpfVDRRRQQreaerllAEYFELQLPADALvgeLNSAERQVLQITRALIRQPKILV 163
Cdd:PRK13633 101 TI-VEEDVAFGpenlgippEEIRER--VDESLKK-------VGMYEYRRHAPHL---LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 164 FDEPSVAL---VKREVdqlLRIVKRL-RDQGLSILYISHYLQEIDSlCDEVTVLRNGRDVAVVEPR 225
Cdd:PRK13633 168 FDEPTAMLdpsGRREV---VNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
271-495 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRSQGISpllSVLEN 350
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPDNQFVG---ATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 LTLAGLgrfSRWGLLSQR--KEQAESLRLIDELAIKTPGPqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVG 428
Cdd:PRK13642 102 DVAFGM---ENQGIPREEmiKRVDEALLAVNMLDFKTREP----ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 429 AKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGiCDRILVLHRGEIagefhAGEAGSDQLLACATGAVQ 495
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEI-----IKEAAPSELFATSEDMVE 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
271-472 |
1.68e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPG-EAIAQGIALVPEERRSQGISPllSVLE 349
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlMKLRESVGMVFQDPDNQLFSA--SVYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 NLTlaglgrfsrWGLLSQRKEQAESLRLIDELAIKT---PGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD 426
Cdd:PRK13636 103 DVS---------FGAVNLKLPEDEVRKRVDNALKRTgieHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 427 VGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
271-488 |
2.13e-07 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 51.84 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLR------LRSpgeaiaqGIALVPEErrsqgisPL 344
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisrksLRS-------MIGVVLQD-------TF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 L---SVLENLTLAGLgrfsrwglLSQRKEQAESLRL--IDELAIKTP-GPQAAVSQ----LSGGNQQKVALGKWLSRRSA 414
Cdd:cd03254 88 LfsgTIMENIRLGRP--------NATDEEVIEAAKEagAHDFIMKLPnGYDTVLGEnggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 415 VYLLDEPCVGVDVGAKVEIYRVIGRLVEeGAAVLVLSSDLPELLGiCDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKII------EEGThDELLA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-208 |
2.29e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADS-----GQVSIDGQpyaALSPRQV 75
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQ---NIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 DA----LGVQFIH-QERLLPASftVGEALFFGHEL---RRGPFVDRRRQQREAERLLAEYFELQLPADALvgELNSAERQ 147
Cdd:PRK14258 82 NLnrlrRQVSMVHpKPNLFPMS--VYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 148 VLQITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVkRLRDQgLSILYISHYLQEIDSLCD 208
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLdpiASMKVESLIQSL-RLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
269-501 |
2.33e-07 |
|
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: 51.72 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQgIALVPEErrsqgiSPLL--S 346
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQE------NVLFnrS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTLAglgrfsRWGLLSQRKEQAESLRLIDELAIKTP-------GPQAAvsQLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:cd03252 92 IRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivGEQGA--GLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLVeEGAAVLVLSSDLPELLGiCDRILVLHRGEIAgefhagEAGSDQLLACATGAVQSTVA 499
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV------EQGSHDELLAENGLYAYLYQ 235
|
..
gi 2545433469 500 VQ 501
Cdd:cd03252 236 LQ 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
271-472 |
2.34e-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: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE-AIA---QGIALVPEerrsqgisplLS 346
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrDIAmvfQNYALYPH----------MS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLEN----LTLAGLGRfsrwGLLSQRKEQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPC 422
Cdd:PRK11650 93 VRENmaygLKIRGMPK----AEIEERVAEAARILELEPLLDRKP------RELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 423 VGVD----VGAKVEIYRVIGRLveeGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK11650 163 SNLDaklrVQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
271-472 |
2.36e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHL--------------EGRLLRLRSPGEAIAQGIALVPEEr 336
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHVGFVFQNFNLFPHR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsqgispllSVLENLTlaglgrfsrWGLLSQRKE-QAESLRLIDELAIKT--PGPQAAV-SQLSGGNQQKVALGKWLSRR 412
Cdd:PRK11264 101 ---------TVLENII---------EGPVIVKGEpKEEATARARELLAKVglAGKETSYpRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-217 |
2.47e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRF-GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDalg 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 VQFIHQERLLPASFTVGEALFFGHELRRGPFVDRRRQQREAERLLaeyfELQLPADALVGELNSAERQVLQITRALIRQP 159
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARIL----ELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 160 KILVFDEPSVALvkrevDQLLRIVKRL------RDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK11650 154 AVFLFDEPLSNL-----DAKLRVQMRLeiqrlhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-198 |
2.76e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 13 FGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAAL----SPRQVD-------ALGVQ 81
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPPRNVEgtvydfvAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 82 fihqerllpasfTVGEALFFGHELRRGPFVDRRRQQREAERLLAEYFE-----------------LQLPADALVGELNSA 144
Cdd:PRK11147 93 ------------EQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDhhnlwqlenrinevlaqLGLDPDAALSSLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 145 ERQVLQITRALIRQPKILVFDEPSVALvkrEVDQLLRIVKRLRDQGLSILYISH 198
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHL---DIETIEWLEGFLKTFQGSIIFISH 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
349-475 |
2.98e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLAGlgrfsRWGLLSQRKEQAESLRLIDELAIKTPGPQAAvSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVG 428
Cdd:NF000106 105 ENLYMIG-----R*LDLSRKDARARADELLERFSLTEAAGRAA-AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2545433469 429 AKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
269-488 |
3.18e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.86 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPgEAIAQGIALVPEErrsqgisPLL--- 345
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL-ESLRRQIGVVPQD-------TFLfsg 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 SVLENLtlaglgrfsRWGLLSQRKEQAES-LRL--IDELAIKTP-GPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYL 417
Cdd:COG1132 429 TIRENI---------RYGRPDATDEEVEEaAKAaqAHEFIEALPdGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 418 LDEPCVGVDVGAKVEIYRVIGRLVEeGAAVLV----LSSdlpelLGICDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK-GRTTIViahrLST-----IRNADRILVLDDGRIV------EQGThEELLA 563
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
272-473 |
3.47e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.12 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 272 DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE----------------AIAQGIALvpee 335
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvsmlfqennlfshlTVAQNIGL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 336 rrsqGISPllsvleNLTLAGlgrfsrwgllSQRKEQAESLRL--IDELAIKTPGpqaavsQLSGGNQQKVALGKWLSRRS 413
Cdd:PRK10771 95 ----GLNP------GLKLNA----------AQREKLHAIARQmgIEDLLARLPG------QLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 414 AVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEIA 473
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
279-472 |
3.58e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 279 EIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG------RLLRLRSPGEAIAQGIALVPEERRSQgISP--------L 344
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfGLTDLRRVLSIIPQSPVLFSGTVRFN-IDPfsehndadL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 LSVLENLTLAGLGRFSRWGLLSQRKEQAESLrlidelaiktpgpqaavsqlSGGNQQKVALGKWLSRRSAVYLLDEPCVG 424
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENF--------------------SVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 425 VDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLHRGEI 472
Cdd:PLN03232 1402 VDVRTDSLIQRTI-REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
242-492 |
3.96e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 242 QEMYPKAQVELGEPLLQVRGLNLARR-----YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL 316
Cdd:PRK10790 326 RQQYGNDDRPLQSGRIDIDNVSFAYRddnlvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 317 RLRSPGeAIAQGIALVPEErrsqgisPLL---SVLENLTlagLGR-FSR---WGLLsQRKEQAESLRLIDElAIKTP-GP 388
Cdd:PRK10790 406 SSLSHS-VLRQGVAMVQQD-------PVVladTFLANVT---LGRdISEeqvWQAL-ETVQLAELARSLPD-GLYTPlGE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 389 QAavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLH 468
Cdd:PRK10790 473 QG--NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTIVE-ADTILVLH 548
|
250 260
....*....|....*....|....
gi 2545433469 469 RGEIAgefhagEAGSDQLLACATG 492
Cdd:PRK10790 549 RGQAV------EQGTHQQLLAAQG 566
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-201 |
4.05e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 13 FGATLA-LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV---SIDGQPYAALSPRQVDALGVQFIHQER- 87
Cdd:cd03290 10 WGSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 88 LLPAsfTVGEALFFGhelrrGPFvdrrrqQREAERLLAEYFELQLPADAL-------VGE----LNSAERQVLQITRALI 156
Cdd:cd03290 90 LLNA--TVEENITFG-----SPF------NKQRYKAVTDACSLQPDIDLLpfgdqteIGErginLSGGQRQRICVARALY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 157 RQPKILVFDEPSVALVKREVDQLLR--IVKRLRDQGLSILYISHYLQ 201
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
257-480 |
4.16e-07 |
|
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: 51.10 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlARRYRQIDLELRRGEIVGLTGLVGSGAKDLlktLFgvvradsGSIHLEGRLLRLRSPGEAIAQGIALV--PE 334
Cdd:cd03270 1 IIVRGAR-EHNLKNVDVDIPRNKLVVITGVSGSGKSSL---AF-------DTIYAEGQRRYVESLSAYARQFLGQMdkPD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 335 ERRSQGISPLLSVLENL----------TLAGLGRFSRwgLLSQRKEQAESLRLIDELAIKTPGPQAAVSQLSGGNQQKVA 404
Cdd:cd03270 70 VDSIEGLSPAIAIDQKTtsrnprstvgTVTEIYDYLR--LLFARVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 405 LGKWLSRR--SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDlPELLGICDRILVLhrGEIAGEfHAGE 480
Cdd:cd03270 148 LATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDI--GPGAGV-HGGE 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
257-473 |
5.36e-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: 50.22 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGV--VRADSGSIHLEGRLLrlrspgeaiaqgIA 330
Cdd:cd03217 1 LEIKDLHVSVGGKEIlkgvNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI------------TD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEERRSQGIspllsvlenltlaglgrfsrwGLLSQRKEQAESLRLIDELAIKTPGpqaavsqLSGGNQQKVALGKWLS 410
Cdd:cd03217 69 LPPEERARLGI---------------------FLAFQYPPEIPGVKNADFLRYVNEG-------FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSdLPELLG--ICDRILVLHRGEIA 473
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH-YQRLLDyiKPDRVHVLYDGRIV 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
269-488 |
5.43e-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: 50.69 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrspgeaiaqGIALvPEERRSQGISPLLSVL 348
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR----------DYTL-ASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLAGLGRFSRWGLLSQRKEQAESLRLIDELAIKTP-GPQAAV----SQLSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03251 88 FNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPeGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 424 GVDVGAKVEIYRVIGRLVeEGAAVLVLSSDLPELLGIcDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:cd03251 168 ALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDGKIV------ERGThEELLA 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-217 |
5.78e-07 |
|
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: 52.71 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDALGVqfIHQERLLPASFTVGE 97
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGM--CPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 98 ALFFGHELRRGPFVDRRRQQREaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVD 177
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 178 QLLRIVKRLRdQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:TIGR01257 1099 SIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
34-219 |
5.97e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 34 LVGENGAGKSTLIKVLAGIHKAdSGQVSIDGQPYAALSP----RQVDALGvqfihQERLLPASfTVGEALFFGHelrrgP 109
Cdd:PRK11174 381 LVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPeswrKHLSWVG-----QNPQLPHG-TLRDNVLLGN-----P 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 110 FVDRRRQQREAERLLAEYFELQLPA--DALVGELNS------AERqvLQITRALIRQPKILVFDEPSVALVKREVDQLLR 181
Cdd:PRK11174 449 DASDEQLQQALENAWVSEFLPLLPQglDTPIGDQAAglsvgqAQR--LALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190
....*....|....*....|....*....|....*...
gi 2545433469 182 IVKRLRdQGLSILYISHYLQEIDSlCDEVTVLRNGRDV 219
Cdd:PRK11174 527 ALNAAS-RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
254-472 |
6.58e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.57 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLArrYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGE---AIAQGIA 330
Cdd:PRK10070 32 EQILEKTGLSLG--VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElreVRRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 LVPEerrSQGISPLLSVLEN----LTLAGLGRfsrwgllSQRKEQA-ESLRLI--DELAIKTPgpqaavSQLSGGNQQKV 403
Cdd:PRK10070 110 MVFQ---SFALMPHMTVLDNtafgMELAGINA-------EERREKAlDALRQVglENYAHSYP------DELSGGMRQRV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 404 ALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
263-472 |
7.40e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ--------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeAIAQ-GIAlvp 333
Cdd:PLN03130 1242 DVVLRYRPelppvlhgLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC---------DISKfGLM--- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 334 EERRSQGISPLLSVLenltLAGLGRFSR-----------WgllsqrkEQAESLRLIDELAIKTPGPQAAVSQ----LSGG 398
Cdd:PLN03130 1310 DLRKVLGIIPQAPVL----FSGTVRFNLdpfnehndadlW-------ESLERAHLKDVIRRNSLGLDAEVSEagenFSVG 1378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545433469 399 NQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGiCDRILVLHRGEI 472
Cdd:PLN03130 1379 QRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTI-REEFKSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-217 |
9.56e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.36 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQV-DALGV--QFIH------QERL 88
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALrQAISVvsQRVHlfsatlRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 89 LPASFTVGEALfFGHELRRgpfVDrrrqqreaerlLAEYFELQLPADALVGE----LNSAERQVLQITRALIRQPKILVF 164
Cdd:PRK11160 435 LLAAPNASDEA-LIEVLQQ---VG-----------LEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 165 DEPSVALVKREVDQLLRIvkrLRD--QGLSILYISHYLQEIDSLcDEVTVLRNGR 217
Cdd:PRK11160 500 DEPTEGLDAETERQILEL---LAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
268-449 |
1.19e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 268 YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQ-GialvpeerRSQGISPLLS 346
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlG--------HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTLaglgrfsrW-GLLSQRKEQAES------LRLIDELAIKTpgpqaavsqLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:PRK13539 90 VAENLEF--------WaAFLGGEELDIAAaleavgLAPLAHLPFGY---------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLVEEGAAVLV 449
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-471 |
1.67e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 394 QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVI--GRLVEEGAAVLVlSSDLPELLGICDRILVLHRGE 471
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIV-SHNLHQVSRLSDFTAFFKGNE 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-220 |
1.68e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKAdSGQVSIDGQPYAALSPRQVdALGVQFIHQERLLPASFTVGEALffg 102
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAEL-ARHRAYLSQQQTPPFAMPVFQYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 103 hELRRGPFVDRRRQQREAERlLAEYFELQlpaDAL---VGELNSAERQ-------VLQITRALIRQPKILVFDEPSVALV 172
Cdd:PRK03695 91 -TLHQPDKTRTEAVASALNE-VAEALGLD---DKLgrsVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 173 KREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-60 |
1.80e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 1.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 3 ALHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV 60
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
269-470 |
1.98e-06 |
|
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: 50.68 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeaiaqgIALVPEerrSQGISPLlSVL 348
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ---TSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 349 ENLTLAGLGRFSRWGLLSQRKEQAESLRLIDElAIKTPGPQAAVSqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVG 428
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKACQLEEDIALFPE-KDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545433469 429 AKVEIY-RVIGRLVEEGAAVLVLSSdlPELLGICDRILVLHRG 470
Cdd:TIGR01271 583 TEKEIFeSCLCKLMSNKTRILVTSK--LEHLKKADKILLLHEG 623
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
254-480 |
2.11e-06 |
|
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: 48.93 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 254 EPLLQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSG-SIHLEGRLLrlrspgeaiaqG 328
Cdd:COG1119 1 DPLLELRNVTVRRGGKTIlddiSWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR-----------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERRSQGIS---------PLLSVLEnLTLAGL----GRFSRWGLlSQRKEQAESLRL--IDELAiktpgpQAAVS 393
Cdd:COG1119 70 GEDVWELRKRIGLVspalqlrfpRDETVLD-VVLSGFfdsiGLYREPTD-EQRERARELLELlgLAHLA------DRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 394 QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSS----DLPEllGIcDRILVLHR 469
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVThhveEIPP--GI-THVLLLKD 218
|
250
....*....|.
gi 2545433469 470 GEIageFHAGE 480
Cdd:COG1119 219 GRV---VAAGP 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
365-472 |
2.16e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 365 LSQRKEQAESL--RLIDELAIKTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVE 442
Cdd:PRK13631 145 LGVKKSEAKKLakFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA 224
|
90 100 110
....*....|....*....|....*....|
gi 2545433469 443 EGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13631 225 NNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
277-475 |
3.65e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.65 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 277 RGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEERRSQGISPllSVLENLTLAGL 356
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPDDQIFSP--TVEQDIAFGPI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 357 GRFSRWGLLSQRKEQAESLRLIDELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRV 436
Cdd:PRK13652 106 NLGLDEETVAHRVSSALHMLGLEELRDRVP------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545433469 437 IGRLVEEGAAVLVLSSDLPELLG-ICDRILVLHRGEIAGE 475
Cdd:PRK13652 180 LNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRIVAY 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
253-472 |
3.78e-06 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 49.33 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 253 GEPLLQVRGL----NLARRYR--------QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG---RLLR 317
Cdd:TIGR02203 321 TRAIERARGDvefrNVTFRYPgrdrpaldSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 318 LRSpgeaIAQGIALVpeerrSQGIspllsVLENLTLAGLGRFSRWGLLSQRK-----EQAESLRLIDEL--AIKTPGPQA 390
Cdd:TIGR02203 401 LAS----LRRQVALV-----SQDV-----VLFNDTIANNIAYGRTEQADRAEieralAAAYAQDFVDKLplGLDTPIGEN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 391 AvSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVeEGAAVLVLSSDLPELLGiCDRILVLHRG 470
Cdd:TIGR02203 467 G-VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDG 543
|
..
gi 2545433469 471 EI 472
Cdd:TIGR02203 544 RI 545
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
395-467 |
4.11e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.38 E-value: 4.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 395 LSGGNQQKVALGKWLSRRS---AVYLLDEPCVGV---DVGAKVEiyrVIGRLVEEGAAVLVLSSDLpELLGICDRILVL 467
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKKLLE---VLQRLVDKGNTVVVIEHNL-DVIKCADWIIDL 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-220 |
4.28e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.22 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 14 GATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPRQVDAL--GVQFIHQERLLPA 91
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 92 SFTVGEALFFghELRRGPFVDRRRQQREAERLLaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVAL 171
Cdd:PRK11831 98 DMNVFDNVAY--PLREHTQLPAPLLHSTVMMKL-EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545433469 172 VKREVDQLLRIVKRLRDQ-GLSILYISHYLQEIDSLCDEVTVLRNGRDVA 220
Cdd:PRK11831 175 DPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
248-454 |
5.52e-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: 48.90 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 248 AQVELGEPLLQVRGLNL-----ARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPG 322
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAgypgaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 323 EaIAQGIALVPEErrsqgisPLL---SVLENLtlaglgRFSRWGLLSQRKEQA-ESLRLIDELAIKTPGPQAAV----SQ 394
Cdd:TIGR02868 406 E-VRRRVSVCAQD-------AHLfdtTVRENL------RLARPDATDEELWAAlERVGLADWLRALPDGLDTVLgeggAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDL 454
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
377-480 |
6.00e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 377 LIDeLAIKTPGPQAAVSQLSGGNQQKVALGKWLSRR--SAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDl 454
Cdd:PRK00635 460 LID-LGLPYLTPERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90 100
....*....|....*....|....*.
gi 2545433469 455 PELLGICDRILVLhrGEIAGEFhAGE 480
Cdd:PRK00635 538 EQMISLADRIIDI--GPGAGIF-GGE 560
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-217 |
6.06e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPY-----AALSPRQVDALGVQFihqeRLLPAS 92
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSviaisAGLSGQLTGIENIEF----KMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 93 FTVGEALFFGHElrrgpfvdrrrqqreaerlLAEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALV 172
Cdd:PRK13546 115 FKRKEIKAMTPK-------------------IIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545433469 173 KREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-216 |
6.20e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSidgqpYAALSPRQVDALG---- 79
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGS-----HIELLGRTVQREGrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 80 --------VQFIHQERLLPASFTVGEALFFGhELRRGPF----------VDRRRQQREAERLLAEYFELQLpadalVGEL 141
Cdd:PRK09984 80 dirksranTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFwrtcfswftrEQKQRALQALTRVGMVHFAHQR-----VSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 142 NSAERQVLQITRALIRQPKILVFDEPSVAL---VKREVDQLLRIVKrlRDQGLSILYISHYLQEIDSLCDEVTVLRNG 216
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLdpeSARIVMDTLRDIN--QNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-219 |
6.31e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 24 LKVERGTIHGLVGENGAGKSTLIKVLAGI--HKADSGQVSIDGQPYAALSPRQVDALGVQFIHQERL-LPA---SFTVGE 97
Cdd:PRK09580 22 LEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeIPGvsnQFFLQT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 98 ALFFGHELRRGPFVDrrrqQREAERLLAEYFE-LQLPADALVGELN----SAERQVLQITRALIRQPKILVFDEPSVALv 172
Cdd:PRK09580 102 ALNAVRSYRGQEPLD----RFDFQDLMEEKIAlLKMPEDLLTRSVNvgfsGGEKKRNDILQMAVLEPELCILDESDSGL- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 173 krEVDQLLRI---VKRLRDQGLSILYISHYLQEIDSL-CDEVTVLRNGRDV 219
Cdd:PRK09580 177 --DIDALKIVadgVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIV 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-63 |
6.85e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 6.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 13 FGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSID 63
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
272-427 |
7.21e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 272 DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL--RLRS--PGEA-------IAQGIA---------- 330
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvaRLQQdpPRNVegtvydfVAEGIEeqaeylkryh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 331 ----LVPEERRSQGISPLLSVLENLTLAGLgrfsrWGLLSQRKEQAESLRLidelaiktpGPQAAVSQLSGGNQQKVALG 406
Cdd:PRK11147 103 dishLVETDPSEKNLNELAKLQEQLDHHNL-----WQLENRINEVLAQLGL---------DPDAALSSLSGGWLRKAALG 168
|
170 180
....*....|....*....|.
gi 2545433469 407 KWLSRRSAVYLLDEPCVGVDV 427
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-194 |
9.18e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 36 GENGAGKSTLIKVLAGIHKADSGQVSIDGQPyaalSPRQVDALGVQFIHQERLLPASFTVGEALFF-----GHELRRGPf 110
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKT----ATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMP- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 111 vdrrrQQREAERLLAEYfelqlpADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVK-RLRDQ 189
Cdd:PRK13543 119 -----GSALAIVGLAGY------EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGG 187
|
....*
gi 2545433469 190 GLSIL 194
Cdd:PRK13543 188 GAALV 192
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-217 |
1.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.00 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV---------------------SIDGQPYAALSPRQVD 76
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleKLVIQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 77 AL----GVQFIHQERLLPASfTVGEALFFGHelrrgpfVDRRRQQREAERLLAEYFEL-QLPADALVG---ELNSAERQV 148
Cdd:PRK13651 102 EIrrrvGVVFQFAEYQLFEQ-TIEKDIIFGP-------VSMGVSKEEAKKRAAKYIELvGLDESYLQRspfELSGGQKRR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 149 LQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDSLCDEVTVLRNGR 217
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
257-465 |
1.39e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNlARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFgvvrADSGSIHLEGrLLRLRSPGEAIAqgialvpeer 336
Cdd:cd03238 1 LTVSGAN-VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLIS-FLPKFSRNKLIF---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 337 rsqgisplLSVLENLTLAGLGRFSrwglLSQrkeqaeslrlidelaiktpgpqaAVSQLSGGNQQKVALGKWLSRRS--A 414
Cdd:cd03238 65 --------IDQLQFLIDVGLGYLT----LGQ-----------------------KLSTLSGGELQRVKLASELFSEPpgT 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 415 VYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDlPELLGICDRIL 465
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWII 159
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
257-472 |
1.41e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 257 LQVRGLNLARR---YRQIDLELRRGEIVGLTGLVGSGaKDL-----LKTLFGVVRADSGSIHLEGRLLrlrSPGEAIAQG 328
Cdd:PRK10418 5 IELRNIALQAAqplVHGVSLTLQRGRVLALVGGSGSG-KSLtcaaaLGILPAGVRQTAGRVLLDGKPV---APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 329 IALVPEERRSqGISPLLSVLENL--TLAGLGRFSRwgllsqrkeQAESLRLIDELAIKTPG--PQAAVSQLSGGNQQKVA 404
Cdd:PRK10418 81 IATIMQNPRS-AFNPLHTMHTHAreTCLALGKPAD---------DATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 405 LGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
255-488 |
1.47e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 255 PLLQVRGLNL--------ARRYRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGV------VRADSGSIHlEGRLLRL-- 318
Cdd:PRK15093 2 PLLDIRNLTIefktsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADRMRFD-DIDLLRLsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 319 RSPGEAIAQGIALVPEERRSqGISPLLSVLENLTLA-----GLGRFsrWGLLSQRKEQAesLRLIDELAIKTPGP--QAA 391
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQS-CLDPSERVGRQLMQNipgwtYKGRW--WQRFGWRKRRA--IELLHRVGIKDHKDamRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 392 VSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVE-EGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250
....*....|....*...
gi 2545433469 471 EIagefhAGEAGSDQLLA 488
Cdd:PRK15093 236 QT-----VETAPSKELVT 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
1.60e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQhlrKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKA-----DSGQVSIDGQpyAALSPRQV 75
Cdd:PRK14271 22 MAAVNLT---LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGR--SIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 76 ----DALGVQFihqERLLPASFTVGEALFFGheLRRGPFVDRRRQQREAERLLAEYFELQLPADALVG---ELNSAERQV 148
Cdd:PRK14271 97 lefrRRVGMLF---QRPNPFPMSIMDNVLAG--VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 149 LQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQgLSILYISHYLQEIDSLCDEVTVLRNGRDVA-------V 221
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEegpteqlF 250
|
250
....*....|
gi 2545433469 222 VEPRHTSSAQ 231
Cdd:PRK14271 251 SSPKHAETAR 260
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
395-472 |
1.67e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.62 E-value: 1.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 395 LSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
394-472 |
1.90e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 394 QLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
389-449 |
2.35e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 2.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 389 QAAVsQLSGGNQQKVALGKWLSRRS---AVYLLDEPCVGV---DVGAKVEiyrVIGRLVEEGAAVLV 449
Cdd:PRK00349 826 QPAT-TLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRKLLE---VLHRLVDKGNTVVV 888
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-63 |
2.73e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 2.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 13 FGATL------ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSID 63
Cdd:COG2401 34 FGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD 90
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-73 |
2.73e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALSPR 73
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-64 |
2.82e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 2.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG 64
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-219 |
3.84e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 34 LVGENGAGKSTLIKVLA----GIHKADSGQVSIDGQPYAALSPRQVDAlgVQFIHQERLLPASFTVGEALFFGHELR--- 106
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGD--VVYNAETDVHFPHLTVGETLDFAARCKtpq 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 107 -RGPFVDRRRQQREAERLLAEYFELQLPADALVGE-----LNSAERQVLQITRALIRQPKILVFDEPSVALvkrEVDQLL 180
Cdd:TIGR00956 170 nRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGL---DSATAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 181 RIVKRLRDQG--------LSILYIShylQEIDSLCDEVTVLRNGRDV 219
Cdd:TIGR00956 247 EFIRALKTSAnildttplVAIYQCS---QDAYELFDKVIVLYEGYQI 290
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
273-472 |
3.88e-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: 45.15 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 273 LELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSpGEAIAQGIALVPEErrsqgisPLL---SVLE 349
Cdd:cd03248 35 FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQE-------PVLfarSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 NLTLaGLGRFSrWGLLSQRKEQAESLRLIDELAIktpGPQAAV----SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGV 425
Cdd:cd03248 107 NIAY-GLQSCS-FECVKEAAQKAHAHSFISELAS---GYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 426 DVGAKVEIYRVIgRLVEEGAAVLVLSSDLpELLGICDRILVLHRGEI 472
Cdd:cd03248 182 DAESEQQVQQAL-YDWPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-205 |
4.10e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 4.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 132 LPADALVGELNSAERQVLQITRALIRQPK--ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEIDS 205
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-217 |
4.51e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 29 GTIHGLVGENGAGKSTLIKVLAGIHKADS--GQVSIDGQPYAALSPRQVDalgvqFIHQERLLPASFTVGEALFFGHELR 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTG-----FVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 107 RGPFVDRRRQQREAERLLAEY----FELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRI 182
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELgltkCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 2545433469 183 VKRLRDQGLSILYISHY-LQEIDSLCDEVTVLRNGR 217
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
372-472 |
4.85e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.13 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 372 AESLRLIDELAIKTPGPQAavsqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRL-VEEGAAVLVL 450
Cdd:PRK13648 124 SEALKQVDMLERADYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISI 199
|
90 100
....*....|....*....|..
gi 2545433469 451 SSDLPELLGiCDRILVLHRGEI 472
Cdd:PRK13648 200 THDLSEAME-ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
271-472 |
6.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.74 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQ---GIALVPEERRSQGISPllSV 347
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkKVGLVFQFPESQLFEE--TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLaGLGRFSrwglLSQRKEQA---ESLRLI---DELAIKTPgpqaavSQLSGGNQQKVALGKWLSRRSAVYLLDEP 421
Cdd:PRK13649 104 LKDVAF-GPQNFG----VSQEEAEAlarEKLALVgisESLFEKNP------FELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 422 CVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-62 |
7.53e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 7.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 4 LHLQHLRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSI 62
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-60 |
7.69e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 7.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQV 60
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
268-488 |
7.80e-05 |
|
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: 44.07 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 268 YRQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG---RLLRLRSpgeaIAQGIALVPEErrsqgisPL 344
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRW----LRSQIGLVSQE-------PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 L---SVLENLtlaGLGRFSRwgllsQRKEQAESLRL--IDELAIKTP-------GPQAavSQLSGGNQQKVALGKWLSRR 412
Cdd:cd03249 88 LfdgTIAENI---RYGKPDA-----TDEEVEEAAKKanIHDFIMSLPdgydtlvGERG--SQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 413 SAVYLLDEPCVGVDVGAKVEIYRVIGRLVeEGAAVLVLSSDLPELLGiCDRILVLHRGEIAgefhagEAGS-DQLLA 488
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV------EQGThDELMA 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
271-475 |
7.81e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEG-------RLLRLRSPGEAIAQG-----IALVPEERRS 338
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRNKAGMVFQNpdnqiVATIVEEDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 339 QGisPllsvlENLtlaglgrfsrwGLLSQ--RKEQAESLRLIDELAIKTPGPQAavsqLSGGNQQKVALGKWLSRRSAVY 416
Cdd:PRK13633 109 FG--P-----ENL-----------GIPPEeiRERVDESLKKVGMYEYRRHAPHL----LSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 417 LLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
263-475 |
7.96e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 44.34 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 263 NLARRYRQ-------IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEaIAQGIALVPEE 335
Cdd:PRK13647 9 DLHFRYKDgtkalkgLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 336 RRSQGISplLSVLENLTLAGLGRFSRWGLLSQRKEQAesLRLIDELAIKTPGPQaavsQLSGGNQQKVALGKWLSRRSAV 415
Cdd:PRK13647 88 PDDQVFS--STVWDDVAFGPVNMGLDKDEVERRVEEA--LKAVRMWDFRDKPPY----HLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
8.27e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 5 HLQHLRKRFGAT-LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQvsidgqpyAALSPrqvdALGVQFI 83
Cdd:PRK11819 8 TMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAP----GIKVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 84 HQERLLPASFTVGEALffghELRRGPFVDRR-----------RQQREAERLLAEYFELQ--------------------- 131
Cdd:PRK11819 76 PQEPQLDPEKTVRENV----EEGVAEVKAALdrfneiyaayaEPDADFDALAAEQGELQeiidaadawdldsqleiamda 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2545433469 132 L---PADALVGELNSAERQVLQITRALIRQPKILVFDEP 167
Cdd:PRK11819 152 LrcpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
392-471 |
9.35e-05 |
|
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: 42.44 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 392 VSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAkveIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGE 471
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
269-473 |
9.62e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 43.31 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFG--VVRADSGSIHLEGRLLRLRSPGEAIAqgiaLVPEErrsqgisplLS 346
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKIIG----YVPQD---------DI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 347 VLENLTLAglgrfsrwgllsqrkeqaESLRLidelaiktpgpQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVD 426
Cdd:cd03213 93 LHPTLTVR------------------ETLMF-----------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 427 VGAKVEIYRVIGRLVEEGAAVLV----LSSdlpELLGICDRILVLHRGEIA 473
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICsihqPSS---EIFELFDKLLLLSQGRVI 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
278-470 |
1.06e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 278 GEIVGLTGLVGSGAKDLLKTLFGVVRADS--GSIhlegrLLRLRSPGEAIAQGIALVPEErrsQGISPLLSVLENLTLAG 355
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTI-----LANNRKPTKQILKRTGFVTQD---DILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 356 LGRFSRwGLLSQRKEQ-AESLrlIDELAI----KTPGPQAAVSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAK 430
Cdd:PLN03211 166 LLRLPK-SLTKQEKILvAESV--ISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2545433469 431 VEIYRVIGRLVEEGAAVlVLSSDLP--ELLGICDRILVLHRG 470
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTI-VTSMHQPssRVYQMFDSVLVLSEG 283
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
269-472 |
1.12e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 44.30 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGR-LLRLRspgeaiaqGIALVpEERRSQGI----SP 343
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdLTALS--------ERELR-AARRKIGMifqhFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LLS---VLEN----LTLAGLGRfsrwgllSQRKEQ-AESLRLIDeLAIKTpgpQAAVSQLSGGNQQKVALGKWLSRRSAV 415
Cdd:COG1135 93 LLSsrtVAENvalpLEIAGVPK-------AEIRKRvAELLELVG-LSDKA---DAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 416 YLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
270-472 |
1.14e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllRLRSPGEAIAQGIALVPEERRsqgISPLLSVLE 349
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQHNI---LFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 350 NLTLaglgrFSRWGLLSQRKEQAESLRLIDELAIKTPGPQAAvSQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGA 429
Cdd:TIGR01257 1023 HILF-----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545433469 430 KVEIYRVIgrLVEEGAAVLVLSS---DLPELLGicDRILVLHRGEI 472
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSThhmDEADLLG--DRIAIISQGRL 1138
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
271-470 |
1.18e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.47 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRlrSPGEAIAQGIALVPEERRSQgiSPLL---SV 347
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNES--EPSFEATRSRNRYSVAYAAQ--KPWLlnaTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 348 LENLTLAGLGRFSRWgllsqrKEQAESLRLIDELAIKTPGPQAAVSQ----LSGGNQQKVALGKWLSRRSAVYLLDEPCV 423
Cdd:cd03290 96 EENITFGSPFNKQRY------KAVTDACSLQPDIDLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545433469 424 GVDVGAKVEIYRV-IGRLVEEGAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:cd03290 170 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-213 |
1.25e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 26 VERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPyAALSPRQVDalgvqfihqerllpasftvgealffghel 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-PVYKPQYID----------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 106 rrgpfvdrrrqqreaerllaeyfelqlpadalvgeLNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKR 185
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180
....*....|....*....|....*....
gi 2545433469 186 LRDQGL-SILYISHYLQEIDSLCDEVTVL 213
Cdd:cd03222 117 LSEEGKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
395-454 |
1.28e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 395 LSGGNQQKVALGKWLSRRS---AVYLLDEPCVGV---DVGAKVEiyrVIGRLVEEGAAVLVLSSDL 454
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKLLE---VLQRLVDKGNTVVVIEHNL 892
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
258-426 |
1.40e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 258 QVRGLNLarRY------RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLLRLRSPGEAIAQGIAL 331
Cdd:NF033858 3 RLEGVSH--RYgktvalDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 332 VPeerrsQGIS----PLLSVLENL----TLAGLGRfsrwgllsqrkeqAESLRLIDELAIKT---PGPQAAVSQLSGGNQ 400
Cdd:NF033858 81 MP-----QGLGknlyPTLSVFENLdffgRLFGQDA-------------AERRRRIDELLRATglaPFADRPAGKLSGGMK 142
|
170 180
....*....|....*....|....*.
gi 2545433469 401 QKVALGKWLSRRSAVYLLDEPCVGVD 426
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-64 |
1.76e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 9 LRKRFGATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDG 64
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
2.06e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 1 MAALHLQHLRKRFGAT----LALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGI----HKADSGQVSIDGQPYAALSP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 73 ---RQVDALGVQFIHQERL--LPASFTVG----EALFF----GHELRRGPFVDrrrqqreaerlLAEYFELQLPA---DA 136
Cdd:PRK11022 81 kerRNLVGAEVAMIFQDPMtsLNPCYTVGfqimEAIKVhqggNKKTRRQRAID-----------LLNQVGIPDPAsrlDV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 137 LVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRL-RDQGLSILYISHYLQEIDSLCDEVTVLRN 215
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYA 229
|
250 260
....*....|....*....|.
gi 2545433469 216 GRdvaVVE----------PRH 226
Cdd:PRK11022 230 GQ---VVEtgkahdifraPRH 247
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-198 |
2.74e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 43.64 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 2 AALHLQHLRKRF--GATLaLDDASLKVERGtiHGL--VGENGAGKSTLIKVLAGIHKADSGQVSIdgqpyaalsPRQVDA 77
Cdd:COG4178 361 GALALEDLTLRTpdGRPL-LEDLSLSLKPG--ERLliTGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 78 LgvqFIHQERLLPASfTVGEALFFghelrrgPFVDRRRQQREAERLLAeyfELQLPadALVGELNSA----------ERQ 147
Cdd:COG4178 429 L---FLPQRPYLPLG-TLREALLY-------PATAEAFSDAELREALE---AVGLG--HLAERLDEEadwdqvlslgEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545433469 148 VLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRlRDQGLSILYISH 198
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-66 |
2.80e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 2.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2545433469 23 SLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQP 66
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP 64
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-219 |
2.96e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 20 DDASLKVERGTIHGLVGENGAGKS----TLIKVLAGIHKADSGQVSIDGQPYAalsPRQVDALGVQFIHQErllPAS-FT 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGRKIATIMQN---PRSaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 95 --------VGEALffgheLRRGpfvdrrrQQREAERLLAEYFELQLPADALVGELNSAER-----QVLQITRALIRQPKI 161
Cdd:PRK10418 94 plhtmhthARETC-----LALG-------KPADDATLTAALEAVGLENAARVLKLYPFEMsggmlQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545433469 162 LVFDEPSV---ALVK-REVDQLLRIVkrlRDQGLSILYISHYLQEIDSLCDEVTVLRNGRDV 219
Cdd:PRK10418 162 IIADEPTTdldVVAQaRILDLLESIV---QKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
269-472 |
3.80e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDL--LKTLFGVVraDSGSIHLEGRLLR---LRSpgeaIAQGIALVpeerrSQGISp 343
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDI--DEGEILLDGHDLRdytLAS----LRNQVALV-----SQNVH- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 344 LL--SVLENLTLAGLGRFSRWGLlSQRKEQAESLRLIDEL--AIKTPGPQAAVSqLSGGNQQKVALGKWLSRRSAVYLLD 419
Cdd:PRK11176 428 LFndTIANNIAYARTEQYSREQI-EEAARMAYAMDFINKMdnGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545433469 420 EPCVGVDVGAKVEIYRVIGRLvEEGAAVLVLSSDLPELLGiCDRILVLHRGEI 472
Cdd:PRK11176 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
271-316 |
4.92e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.86 E-value: 4.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL 316
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-205 |
5.33e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 36 GENGAGKSTLIKVLAGIHKADSGQVSidgqpYAALSPRQVDALGVQFIHQERLLPASFTVGEALFFGHElrrgpFVDRRR 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSE-----IYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 116 QQREAErllaEYFELQLPADALVGELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILY 195
Cdd:PRK13541 103 TLYAAI----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLL 178
|
170
....*....|
gi 2545433469 196 ISHYLQEIDS 205
Cdd:PRK13541 179 SSHLESSIKS 188
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
270-475 |
5.56e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 270 QIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGsihlegrllrLRSPGEAIAQGIAL-----VPEERRSQGI--- 341
Cdd:PRK14271 39 QVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG----------YRYSGDVLLGGRSIfnyrdVLEFRRRVGMlfq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 342 --SPL-LSVLENLtLAGLgrfsRWGLLSQRKEqaesLRLIDELAIKTPGPQAAVS--------QLSGGNQQKVALGKWLS 410
Cdd:PRK14271 109 rpNPFpMSIMDNV-LAGV----RAHKLVPRKE----FRGVAQARLTEVGLWDAVKdrlsdspfRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 411 RRSAVYLLDEPCVGVDVGAKVEIYRVIgRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGE 475
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFI-RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
345-498 |
7.12e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 345 LSVLENLtlaglgRFSRWGLLSQRKEQAESLRLIDELAIKTP-------GPQAavSQLSGGNQQKVALGKWLSRRSAVYL 417
Cdd:PTZ00265 1310 MSIYENI------KFGKEDATREDVKRACKFAAIDEFIESLPnkydtnvGPYG--KSLSGGQKQRIAIARALLREPKILL 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 418 LDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSSDLPELLGICDRILVLHRGEIAGEFHAGEAGSDQLLACATGAVQST 497
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSFVQAHGTHEELLSVQDGVYKKY 1461
|
.
gi 2545433469 498 V 498
Cdd:PTZ00265 1462 V 1462
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
271-472 |
1.00e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 41.75 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVrADSGSIHLEGRLLRlrspgeaiaqgiALVPEERRSQ----GISPLL- 345
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR------------ELDPESWRKHlswvGQNPQLp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 346 --SVLENLTLAG--LGRFSRWGLLsqrkEQAESLRLIDELA--IKTP-GPQAAvsQLSGGNQQKVALGKWLSRRSAVYLL 418
Cdd:PRK11174 436 hgTLRDNVLLGNpdASDEQLQQAL----ENAWVSEFLPLLPqgLDTPiGDQAA--GLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 419 DEPCVGVDvgAKVEiYRVIGRLVE--EGAAVLVLSSDLPELLGiCDRILVLHRGEI 472
Cdd:PRK11174 510 DEPTASLD--AHSE-QLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
389-449 |
1.01e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545433469 389 QAAvSQLSGGNQQKVALGKWLSRRS---AVYLLDEPCVGV---DVgAKVeiYRVIGRLVEEGAAVLV 449
Cdd:COG0178 822 QPA-TTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDI-RKL--LEVLHRLVDKGNTVVV 884
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-217 |
1.08e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.62 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 18 ALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQPYAALsprQVDALGVQF--IHQERLLpASFTV 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLavVSQTPFL-FSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 96 GEALFFGHElrrgpfvDRRRQQREAERLLAEYFE--LQLPA--DALVGE----LNSAERQVLQITRALIRQPKILVFDEP 167
Cdd:PRK10789 406 ANNIALGRP-------DATQQEIEHVARLASVHDdiLRLPQgyDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545433469 168 SVALVKREVDQLLRIVKRLRdQGLSILYISHYLQEIdSLCDEVTVLRNGR 217
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSAL-TEASEILVMQHGH 526
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
161-198 |
1.10e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2545433469 161 ILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISH 198
Cdd:cd03270 160 LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
393-472 |
1.20e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.94 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 393 SQLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGiCDRILVLHRGE 471
Cdd:PRK13640 142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGK 220
|
.
gi 2545433469 472 I 472
Cdd:PRK13640 221 L 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-309 |
1.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 132 LPADALVGELNSAERQVLQITRALI---RQPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQeIDSLCD 208
Cdd:PRK00635 801 LPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVAD 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 209 EVTVL------RNGRDVAVVEPR-----HTSSAQIARLMVNREvQEMYPKAQVELGEPLLqvRGLNLARRY----RQIDL 273
Cdd:PRK00635 880 YVLELgpeggnLGGYLLASCSPEelihlHTPTAKALRPYLSSP-QELPYLPDPSPKPPVP--ADITIKNAYqhnlKHIDL 956
|
170 180 190
....*....|....*....|....*....|....*.
gi 2545433469 274 ELRRGEIVGLTGLVGSGAKDLlktLFGVVRAdSGSI 309
Cdd:PRK00635 957 SLPRNALTAVTGPSASGKHSL---VFDILYA-AGNI 988
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
256-472 |
1.22e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.97 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 256 LLQVRGLNLARRYRQI----DLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRAD--------SGSIHLEGRLLRlRSPGE 323
Cdd:PRK13547 1 MLTADHLHVARRHRAIlrdlSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLA-AIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 324 AIAQGIALVPEErrSQGISPlLSVLEnltLAGLGRF---SRWGLLSQRKEQAESLRLidELAIKTPGPQAAVSQLSGGNQ 400
Cdd:PRK13547 80 RLARLRAVLPQA--AQPAFA-FSARE---IVLLGRYphaRRAGALTHRDGEIAWQAL--ALAGATALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 401 QKVALGK-----WLSRRSAV----YLLDEPCVGVDVGAKVEIYRVIGRLVEE-GAAVLVLSSDLPELLGICDRILVLHRG 470
Cdd:PRK13547 152 ARVQFARvlaqlWPPHDAAQppryLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADG 231
|
..
gi 2545433469 471 EI 472
Cdd:PRK13547 232 AI 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-171 |
1.31e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 41.82 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 19 LDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADsGQVSIDGQPYAALSPRQ-VDALGVqfIHQER-LLPASFTVG 96
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGV--IPQKVfIFSGTFRKN 1311
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545433469 97 ---EALFFGHELRRgpfVDRRRQQREAERLLAEYFELQLPADALVgeLNSAERQVLQITRALIRQPKILVFDEPSVAL 171
Cdd:TIGR01271 1312 ldpYEQWSDEEIWK---VAEEVGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-217 |
1.44e-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: 40.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 15 ATLALDDASLKVERGTIHGLVGENGAGKSTLIKVLAGIHKADSGQVSIDGQ-PYAALSPrqvdalgvqFIHqerllpaSF 93
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVSQEP---------WIQ-------NG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 94 TVGEALFFGHELRrgpfvdrrrqqreaerllAEYFELQLPADAL--------------VGE----LNSAERQVLQITRAL 155
Cdd:cd03250 81 TIRENILFGKPFD------------------EERYEKVIKACALepdleilpdgdlteIGEkginLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 156 IRQPKILVFDEPSVAL----VKREVDQLLRivKRLRDQGLSILyISHYLQEIdSLCDEVTVLRNGR 217
Cdd:cd03250 143 YSDADIYLLDDPLSAVdahvGRHIFENCIL--GLLLNNKTRIL-VTHQLQLL-PHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-215 |
1.73e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 1.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545433469 141 LNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLRDQG-LSILYISHYLQEIDSlCDEVTVLRN 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-203 |
2.10e-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: 40.77 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 126 EYFELQLPADALVGelnsAERQVLQITRALIRQ---PKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQE 202
Cdd:TIGR00630 819 GYIRLGQPATTLSG----GEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDV 894
|
.
gi 2545433469 203 I 203
Cdd:TIGR00630 895 I 895
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
271-472 |
2.19e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRllrlrspgeaiAQGIALvpeerrSQGISPLLSVLEN 350
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAI------SSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 351 LTLAGLgrfsrwgLLSQRKEQAESL--RLIDELAIKTPGPQaAVSQLSGGNQQKVALGKWLSRRSAVYLLDEpcvGVDVG 428
Cdd:PRK13545 106 IELKGL-------MMGLTKEKIKEIipEIIEFADIGKFIYQ-PVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545433469 429 AKVEIYRVIGRL---VEEGAAVLVLSSDLPELLGICDRILVLHRGEI 472
Cdd:PRK13545 175 DQTFTKKCLDKMnefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-302 |
2.56e-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: 40.77 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 126 EYFELQLPADALVGelNSAERQVL--QITRALIrqPKILVFDEPSVALVKREVDQLLRIVKRLRDQGLSILYISHYLQEI 203
Cdd:TIGR00630 478 DYLSLSRAAGTLSG--GEAQRIRLatQIGSGLT--GVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 204 dSLCDEVT------------VLRNGRDVAVVEPRHTSSAQIARLMVNREVqemyPKAQVELGEPLLQVRGLNlARRYRQI 271
Cdd:TIGR00630 554 -RAADYVIdigpgagehggeVVASGTPEEILANPDSLTGQYLSGRKKIEV----PAERRPGNGKFLTLKGAR-ENNLKNI 627
|
170 180 190
....*....|....*....|....*....|..
gi 2545433469 272 DLELRRGEIVGLTGLVGSGAKDLL-KTLFGVV 302
Cdd:TIGR00630 628 TVSIPLGLFTCITGVSGSGKSTLInDTLYPAL 659
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
271-474 |
3.93e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 39.23 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 271 IDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSGSIHLEGRLL----------RLRSP-------------GEAIAQ 327
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknkklkPLRKKvgivfqfpehqlfEETVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 328 GIAL------VPEERrsqgisPLLSVLENLTLAGLGrfsrwgllsqrkeqaeslrliDELAIKTPgpqaavSQLSGGNQQ 401
Cdd:PRK13634 106 DICFgpmnfgVSEED------AKQKAREMIELVGLP---------------------EELLARSP------FELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545433469 402 KVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEG--AAVLVLSSdLPELLGICDRILVLHRGEIAG 474
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHS-MEDAARYADQIVVMHKGTVFL 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
374-449 |
4.45e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.99 E-value: 4.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545433469 374 SLR---LIDElaIKTPGPQAAVSqLSGGNQQKVALGKWLSRRSAVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLV 449
Cdd:PRK14243 131 SLRqaaLWDE--VKDKLKQSGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-215 |
6.04e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 135 DALVG----ELNSAERQVLQITRALIRQPKILVFDEPSVALVKREVDQLLRIVKRLR-DQGLSILYISHYLQEIdSLCDE 209
Cdd:PTZ00265 570 ETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI-RYANT 648
|
....*.
gi 2545433469 210 VTVLRN 215
Cdd:PTZ00265 649 IFVLSN 654
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-452 |
8.79e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 37.90 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 269 RQIDLELRRGEIVGLTGLVGSGAKDLLKTLFGVVRADSgSIHLEGRLlrlRSPGEAIAQGIALVPEERRSQGIS------ 342
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGEV---RLFGRNIYSPDVDPIEVRREVGMVfqypnp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545433469 343 -PLLSVLENLTLAglgrFSRWGLLSQRKEQAESLrlidELAIKTPGPQAAV--------SQLSGGNQQKVALGKWLSRRS 413
Cdd:PRK14267 97 fPHLTIYDNVAIG----VKLNGLVKSKKELDERV----EWALKKAALWDEVkdrlndypSNLSGGQRQRLVIARALAMKP 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 2545433469 414 AVYLLDEPCVGVDVGAKVEIYRVIGRLVEEGAAVLVLSS 452
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHS 207
|
|
| |
