|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-511 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 708.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANG 88
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENIFARREITRGILgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGL-IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGS 248
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 249 DAKDFAKSVDHAVGAEVFRAENISLPRptgglSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGK 328
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 329 HVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTS 408
Cdd:COG1129 315 PVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 409 MSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
490 500
....*....|....*....|...
gi 499968440 489 VFDRNEATEEAIIAASAKGHGHQ 511
Cdd:COG1129 475 ELDREEATEEAIMAAATGGAAAA 497
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-500 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 522.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGI 89
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIFARREITRGILgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGR-LDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSD 249
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 250 AKDFAKSVDHAVGAEVFRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKH 329
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 330 VRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGR--FTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVT 407
Cdd:COG3845 322 ITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRppFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
490
....*....|...
gi 499968440 488 AVFDRNEATEEAI 500
Cdd:COG3845 482 GEVPAAEATREEI 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-508 |
6.36e-174 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 499.84 E-value: 6.36e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGV------ErptlGRIILDGKPVSFDSPAHAQ 85
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyE----GEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 ANGIGMIFQELNLFANMSVAENIFARREITRGILgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGI-MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSM 245
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 246 IGSDAKDFAKSVDHAVGAEVFRAENISL--PRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGR-HTHSTGK 322
Cdd:PRK13549 240 VGRELTALYPREPHTIGEVILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 323 IFIDGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNP 402
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 403 DFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLS 482
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
490 500
....*....|....*....|....*.
gi 499968440 483 NGQLVAVFDRNEATEEAIIAASAKGH 508
Cdd:PRK13549 480 EGKLKGDLINHNLTQEQVMEAALRSE 505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-503 |
2.11e-164 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 475.26 E-value: 2.11e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGM 91
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSDAK 251
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 252 DFAKSVDHAVGAEVFRAENISlprptgGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR 331
Cdd:PRK10762 244 DQYPRLDKAPGEVRLKVDNLS------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 332 ARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRL-FHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSMS 410
Cdd:PRK10762 318 TRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAgGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 411 GGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVF 490
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
|
490
....*....|...
gi 499968440 491 DRNEATEEAIIAA 503
Cdd:PRK10762 478 TREQATQEKLMAA 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-503 |
1.75e-152 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 444.74 E-value: 1.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMI 92
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGILgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGGI-VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV--TGEAMvRDIDTRWIVRSMIGSDA 250
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYvaTFDDM-AQVDRDQLVQAMVGREI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 251 KDFAKSVDHAVGAEVFRAENISLPrptgGLSvNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV 330
Cdd:PRK11288 243 GDIYGYRPRPLGEVRLRLDGLKGP----GLR-EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 331 RARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRL-FHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSM 409
Cdd:PRK11288 318 DIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAgCLINNRWEAENADRFIRSLNIKTPSREQLIMNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 410 SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
490
....*....|....
gi 499968440 490 FDRNEATEEAIIAA 503
Cdd:PRK11288 478 LAREQATERQALSL 491
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-503 |
2.67e-142 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 418.81 E-value: 2.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGV------ErptlGRIILDGKPVSFDSPAHAQ 85
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRFKDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 ANGIGMIFQELNLFANMSVAENIFARREI-TRGIlgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:NF040905 77 ALGIVIIHQELALIPYLSIAENIFLGNERaKRGV--IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV--TGEAMVRDIDTRWIV 242
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTieTLDCRADEVTEDRII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 243 RSMIGSDAKDFAKSVDHAVGAEVFRAENISLPRPT--GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRH--TH 318
Cdd:NF040905 235 RGMVGRDLEDRYPERTPKIGEVVFEVKNWTVYHPLhpERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 319 STGKIFIDGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIK 398
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 399 APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRI 478
Cdd:NF040905 395 TPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRI 474
|
490 500
....*....|....*....|....*
gi 499968440 479 AVLSNGQLVAVFDRNEATEEAIIAA 503
Cdd:NF040905 475 YVMNEGRITGELPREEASQERIMRL 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-504 |
4.08e-142 |
|
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: 418.46 E-value: 4.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGV--ERPTLGRIILDGKPVSFDSPAHAQANGI 89
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTM-VEDLPIGQQQLVEIAKAMSLNA 168
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGS 248
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 249 DAKDFAKSVDHAVGAEVFRAENISLPRPTGG--LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHS-TGKIFI 325
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVINPhrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 326 DGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFE 405
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 406 VTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
490
....*....|....*....
gi 499968440 486 LVAVFDRNEATEEAIIAAS 504
Cdd:TIGR02633 481 LKGDFVNHALTQEQVLAAA 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-504 |
9.66e-139 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 410.33 E-value: 9.66e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMI 92
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGILG---IDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSD 249
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 250 AKD----FAKSVDHAVGAEVFRAENISlPRPTGglSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFI 325
Cdd:PRK09700 246 LQNrfnaMKENVSNLAHETVFEVRNVT-SRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 326 DGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLTLA---SLGRFTRLFHI-DRGAEKSAIRDAIRDLSIKAPN 401
Cdd:PRK09700 323 NGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLfHEVDEQRTAENQRELLALKCHS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 402 PDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVL 481
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
490 500
....*....|....*....|....
gi 499968440 482 SNGQLVAVFD-RNEATEEAIIAAS 504
Cdd:PRK09700 483 CEGRLTQILTnRDDMSEEEIMAWA 506
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-506 |
2.15e-124 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 372.91 E-value: 2.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 17 DVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMIFQEL 96
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 97 NLFANMSVAENIFARREITRGILgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEP 176
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMF-VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 177 TSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSDAKDFAKS 256
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 257 VDHAVGAEVFRAENI-SLPRPtgglSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDT 335
Cdd:PRK10982 242 KENKPGEVILEVRNLtSLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 336 TRRIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRF-TRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQ 414
Cdd:PRK10982 318 NEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 415 QKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 477
|
490
....*....|..
gi 499968440 495 ATEEAIIAASAK 506
Cdd:PRK10982 478 TTQNEILRLASL 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-512 |
8.46e-124 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 371.69 E-value: 8.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGM 91
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARreITRgilgidHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG--LPK------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMI-GSDA 250
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITpAARE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 251 KDFAKSVD-----------HAVGAEVFRAENISlprptgGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHS 319
Cdd:PRK15439 243 KSLSASQKlwlelpgnrrqQAAGAPVLTVEDLT------GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 320 TGKIFIDGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASNLtlASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKA 399
Cdd:PRK15439 317 GGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNV--CALTHNRRGFWIKPARENAVLERYRRALNIKF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 400 PNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIA 479
Cdd:PRK15439 395 NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
490 500 510
....*....|....*....|....*....|...
gi 499968440 480 VLSNGQLVAVFDRNEATEEAIIAASAKGHGHQG 512
Cdd:PRK15439 475 VMHQGEISGALTGAAINVDTIMRLAFGEHQAQE 507
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-230 |
2.43e-77 |
|
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: 240.02 E-value: 2.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMI 92
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQelnlfanmsvaenifarreitrgilgidhkaqvqkanaflkrldagieadtmvedLPIGQQQLVEIAKAMSLNARILI 172
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
262-486 |
7.40e-74 |
|
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: 231.55 E-value: 7.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 262 GAEVFRAENISLPRptgglSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRR 341
Cdd:cd03215 1 GEPVLEVRGLSVKG-----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 342 GLALIPEDRQREGLVQVLSIASNLTLASLgrftrlfhidrgaeksairdairdlsikapnpdfevtsMSGGNQQKVVIGK 421
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 422 ALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-494 |
3.66e-63 |
|
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: 214.38 E-value: 3.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTL---GRIILDGKPVSfDSPAHAQA 86
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLL-ELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQE-LNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:COG1123 83 RRIGMVFQDpMTQLNPVTVGDQIaEALE-----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR-WIV 242
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApQAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 243 RSMIGSDAKDFAKSVDHAVGAEVFRAENIS----LPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTH 318
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 319 STGKIFIDGKHVRA--RDTTRRIRRGLALIPED--RQregLVQVLSIAsnltlASLGRFTRLFHIDRGAEKSA-IRDAIR 393
Cdd:COG1123 318 TSGSILFDGKDLTKlsRRSLRELRRRVQMVFQDpySS---LNPRMTVG-----DIIAEPLRLHGLLSRAERRErVAELLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 394 DLSIkapNPDFE---VTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLE 469
Cdd:COG1123 390 RVGL---PPDLAdryPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLA 466
|
490 500
....*....|....*....|....*
gi 499968440 470 EVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:COG1123 467 VVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-227 |
2.21e-53 |
|
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: 180.33 E-value: 2.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN-GIGM 91
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-GLPPHEIARlGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENI-----FARREITRGILGIDHKAQV-QKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:cd03219 80 TFQIPRLFPELTVLENVmvaaqARTGSGLLLARARREEREArERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-227 |
3.38e-51 |
|
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: 175.23 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN- 87
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-GLPPHRIARl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFANMSVAENI------FARREITRGILGI-----DHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQ 156
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVlvaahaRLGRGLLAALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 157 LVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKA-QGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-227 |
6.80e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.71 E-value: 6.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMI 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:COG1131 79 PQEPALYPDLTVRENL----RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-227 |
2.26e-47 |
|
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: 163.46 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQanGIGMI 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERR--NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:cd03259 78 FQDYALFPHLTVAENIaFGLK-----LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-227 |
4.53e-45 |
|
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: 158.48 E-value: 4.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMI 92
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI--FARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:COG4555 80 PDERGLYDRLTVRENIryFAE------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-226 |
2.04e-44 |
|
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: 155.70 E-value: 2.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGM 91
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQ--ELNLFaNMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVaFGLE-----NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-227 |
4.39e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 156.41 E-value: 4.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQanG 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKR--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENI--------FARREItrgilgidhKAQVQKAnafLKRLdaGIE--ADTMVEDLPIGQQQLV 158
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVafglrmrgVPKAEI---------RARVAEL---LELV--GLEglADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 159 EIAKAMSLNARILIMDEPTSALSA---AEVEILFKVIaeLKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAklrEEMREELRRL--QRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-227 |
7.53e-43 |
|
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: 150.24 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMI 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarreitrgilgidhkaqvqkanaflkrldagieadtmveDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:cd03230 79 PEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-226 |
1.03e-41 |
|
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: 147.33 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPV---SFDSPAHAQAngI 89
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRR--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIfarreitrgilgidhkaqvqkanaflkrldagieadtmVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:cd03229 79 GMVFQDFALFPHLTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-230 |
3.26e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.50 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVY----SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSP---A 82
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQANGIGMIFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEI 160
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENV----ALPLLLAGVSRKERRERARELLERV--GLGdrLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 161 AKAMSLNARILIMDEPTSAL---SAAEV-EILFKVIAElkaQGVAIVYISHRlEELMRIGDYITVLRDGQVTGE 230
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLdskTGEEVlELLRELNRE---LGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-236 |
5.83e-41 |
|
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: 147.09 E-value: 5.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAqANGIGM 91
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQ--ELNLFAnMSVAENI-FARREitrgiLGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:COG1122 80 VFQnpDDQLFA-PTVEEDVaFGPEN-----LGLPREEIRERVEEALELV--GLEhlADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-227 |
9.04e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.13 E-value: 9.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA--NG 88
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENI----FARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 165 SLNARILIMDEPTSAL---SAAEVEILFKVIAElkAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG3638 162 VQEPKLILADEPVASLdpkTARQVMDLLRRIAR--EDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-227 |
1.63e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.45 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaqaNGIGMI 92
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI--------FARREITR------GILGIDHkaqvqkanaFLKRLdagieadtmVEDLPIGQQQLV 158
Cdd:COG3839 81 FQSYALYPHMTVYENIafplklrkVPKAEIDRrvreaaELLGLED---------LLDRK---------PKQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 159 EIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-227 |
2.72e-39 |
|
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: 142.19 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN-GIGM 91
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHERARaGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIfarrEITRGILGIDH-KAQVQKANAFLKRLDAgiEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03224 80 VPEGRRIFPELTVEENL----LLGAYARRRAKrKARLERVYELFPRLKE--RRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-227 |
3.26e-39 |
|
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: 141.62 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaqaNGIGMI 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI--------FARREITRG------ILGIDHkaqvqkanaFLKRLdagieadtmVEDLPIGQQQLV 158
Cdd:cd03301 78 FQNYALYPHMTVYDNIafglklrkVPKDEIDERvrevaeLLQIEH---------LLDRK---------PKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 159 EIAKAMSLNARILIMDEPTSALSAAeveILFKVIAELK----AQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAK---LRVQMRAELKrlqqRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-227 |
1.13e-38 |
|
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: 140.32 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSP---AHAQ 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 ANGIGMIFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENV----ELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRlEELMRIGDYITVLRDGQV 227
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-178 |
1.24e-38 |
|
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: 138.16 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMIFQELNLFANMSVAEN 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 108 IFarreITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPI----GQQQLVEIAKAMSLNARILIMDEPTS 178
Cdd:pfam00005 80 LR----LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-227 |
2.70e-38 |
|
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: 140.01 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA--HAQANGI 89
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENI----FARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 166 LNARILIMDEPTSAL---SAAEVEILFKVIAelKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03256 161 QQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
282-489 |
1.35e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDttRRIRRGLALIPEDRqreGLVQVLSI 361
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP--AEVRRRIGYVPQEP---ALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgrFTRLFHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:COG1131 91 RENLRF-----FARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 442 GAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:COG1131 165 EARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-226 |
1.93e-37 |
|
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: 135.06 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIF 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 QelnlfanMSVaenifarreitrgilgidhkaqvqkanaflkrldagieadtmvedlpiGQQQLVEIAKAMSLNARILIM 173
Cdd:cd00267 80 Q-------LSG------------------------------------------------GQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 174 DEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-236 |
2.22e-37 |
|
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: 137.33 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA---HA 84
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QANgIGMIFQELNLFANMSVAENIFARREitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLE----IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-508 |
4.64e-37 |
|
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: 143.67 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKS----TLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA---NGIGMIFQE---- 95
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgNRIAMIFQEpmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 96 LN-LfanMSVAENIfarREITRGILGIDHKAQVQKANAFLKRldAGI-EADTMVEDLPI----GQQQLVEIAKAMSLNAR 169
Cdd:COG4172 105 LNpL---HTIGKQI---AEVLRLHRGLSGAAARARALELLER--VGIpDPERRLDAYPHqlsgGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 170 ILIMDEPTSALsaaEV----EILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI-------D 237
Cdd:COG4172 177 LLIADEPTTAL---DVtvqaQIL-DLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELfaapqhpY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 238 TrwivRSMIGSDAKDFAKSVDHAvGAEVFRAENISL--PRPTGGLS--------VNDVSLSVKAGEILGIYGLMGAGRSE 307
Cdd:COG4172 253 T----RKLLAAEPRGDPRPVPPD-APPLLEARDLKVwfPIKRGLFRrtvghvkaVDGVSLTLRRGETLGLVGESGSGKST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 308 FFECVIgRHTHSTGKIFIDGKHVRARDTT--RRIRRGLALIPED-------RQR------EGLvQVLSIasnltlaslgr 372
Cdd:COG4172 328 LGLALL-RLIPSEGEIRFDGQDLDGLSRRalRPLRRRMQVVFQDpfgslspRMTvgqiiaEGL-RVHGP----------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 373 ftrlfHIDRGAEKSAIRDAIRDLSIKA------PNpDFevtsmSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKAD 446
Cdd:COG4172 395 -----GLSAAERRARVAEALEEVGLDPaarhryPH-EF-----SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 447 VFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLV------AVFD--RNEATeEAIIAASAKGH 508
Cdd:COG4172 464 ILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVeqgpteQVFDapQHPYT-RALLAAAPLLE 533
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-243 |
5.51e-37 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 136.66 E-value: 5.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdspahAQANG-- 88
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI-------TKLRGkk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 -------IGMIFQELNLFANMSVAENI----FARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQL 157
Cdd:TIGR02315 74 lrklrrrIGMIFQHYNLIERLTVLENVlhgrLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 158 VEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
....*..
gi 499968440 237 DTRWIVR 243
Cdd:TIGR02315 234 DDEVLRH 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-227 |
6.26e-37 |
|
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: 136.21 E-value: 6.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQanGIGMI 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:cd03300 78 FQNYALFPHLTVFENIaFGLR-----LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-227 |
6.73e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 137.93 E-value: 6.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdspaHAQANGIGM 91
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENI--FARREitrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvyLARLK------GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-236 |
1.63e-36 |
|
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: 141.58 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 3 TAEAQKDDVILRLDDVSKVY-----SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS 77
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 78 FDSPA--HAQANGIGMIFQ--ELNLFANMSVaenifaRREITRG--ILGIDHKAQV-QKANAFLKR--LDAGIeADTMVE 148
Cdd:COG1123 331 KLSRRslRELRRRVQMVFQdpYSSLNPRMTV------GDIIAEPlrLHGLLSRAERrERVAELLERvgLPPDL-ADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 149 DLPIGQQQLVEIAKAMSLNARILIMDEPTSAL---SAAEVeilFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRD 224
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALdvsVQAQI---LNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250
....*....|..
gi 499968440 225 GQVTGEAMVRDI 236
Cdd:COG1123 481 GRIVEDGPTEEV 492
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-228 |
3.47e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS----FDSPAHAQa 86
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 nGIGMIFQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:COG2884 80 -RIGVVFQDFRLLPDRTVYENVaLPLR-----VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-230 |
6.53e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 133.57 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGI 89
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIfarreitrgILGidhkaqvqkanAFLKRLDAGIEAD-TMVEDL-PI--------------G 153
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENL---------LLG-----------AYARRDRAEVRADlERVYELfPRlkerrrqragtlsgG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 154 QQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
282-488 |
7.11e-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: 132.94 E-value: 7.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPEDRQregLVQVLSI 361
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRR---IFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLASLGRftrlfhidRGAEKSAIRDAIRDL-SIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:cd03224 93 EENLLLGAYAR--------RRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 441 VGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-227 |
2.52e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 8 KDDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdspaHAQAN 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFAN--MSVAENIFARREITRGILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKA 163
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERV--GLEdlADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-238 |
3.19e-35 |
|
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: 131.47 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA--NGIG 90
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENI-FARREITRgilgIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLREHTR----LSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 170 ILIMDEPTSAL---SAAEVEILfkvIAELK-AQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDT 238
Cdd:cd03261 157 LLLYDEPTAGLdpiASGVIDDL---IRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-227 |
3.67e-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: 130.86 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdspahAQANGIGMI 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI--FARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03269 76 PEERGLYPKMKVIDQLvyLAQ------LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-228 |
6.83e-35 |
|
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: 129.68 E-value: 6.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdsPAHAQANGIGMI 92
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELN--LFANmSVaenifaRREITRGILGIDHKAQvqKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03226 77 MQDVDyqLFTD-SV------REELLLGLKELDAGNE--QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-227 |
8.93e-35 |
|
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: 130.32 E-value: 8.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAN 87
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 G--IGMIFQE----LNlfANMSVAENIfarREITRgILGIDHKAQVQKANAFLKrLDAGIEADTMVEDLPI----GQQQL 157
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGEQI---AEPLR-IHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRYPHelsgGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 158 VEIAKAMSLNARILIMDEPTSAL-SAAEVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALdVSVQAQIL-DLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-227 |
9.26e-35 |
|
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: 130.48 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA-- 86
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQELNLFANMSVAENI-FARREITRgilgIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKA 163
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVaFPLREHTD----LSEAEIRELVLEKLELV--GLPgaADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 164 MSLNARILIMDEPTSAL---SAAEVEILfkvIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1127 156 LALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-227 |
5.73e-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: 5.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGM 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 172 IMDEPTSALS-AAEVEILfKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1120 160 LLDEPTSHLDlAHQLEVL-ELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-218 |
6.97e-34 |
|
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: 127.21 E-value: 6.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMI 92
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgILGIDHKAqvQKANAFLKRLdaGIEAdtmVEDLPI-----GQQQLVEIAKAMSL 166
Cdd:COG4133 81 GHADGLKPELTVRENLrFWAA-----LYGLRADR--EAIDEALEAV--GLAG---LADLPVrqlsaGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEEL-----MRIGDY 218
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-230 |
7.31e-34 |
|
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: 127.59 E-value: 7.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAhaqang 88
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVaLGLE-----LQGVPKAEARERAEELLELV--GLSgfENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVL--RDGQVTGE 230
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
278-488 |
1.34e-33 |
|
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: 127.17 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLS-VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLAlipedR--QREG 354
Cdd:cd03219 11 GGLVaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-----RtfQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 LVQVLSIASNLTLASLGRFTRLFHIDRGA-EKSAIRDAIRD------LSIKApnpDFEVTSMSGGNQQKVVIGKALMTNP 427
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSGLLLARARrEEREARERAEEllervgLADLA---DRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
282-503 |
2.16e-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: 126.64 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPEDRqreGLVQVLSI 361
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslGRFTRlfhiDRGAEKSAIRDAIRDLsikapnpdFEV---------TSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:COG0410 96 EENLLL---GAYAR----RDRAEVRADLERVYEL--------FPRlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 433 DEPSRGIdvgakA-----DVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE-ATEEAIIAA 503
Cdd:COG0410 161 DEPSLGL-----ApliveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAElLADPEVREA 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-227 |
2.73e-33 |
|
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: 126.12 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN-GIGM 91
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARREITrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIR----GLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-227 |
3.10e-33 |
|
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: 134.19 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIG 90
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFaNMSVAENI-FARREITRgilgidhkAQVQKA------NAFLKRLDAGIeaDTMVED----LPIGQQQLVE 159
Cdd:COG2274 553 VVLQDVFLF-SGTIRENItLGDPDATD--------EEIIEAarlaglHDFIEALPMGY--DTVVGEggsnLSGGQRQRLA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 160 IAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLeELMRIGDYITVLRDGQV 227
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-227 |
3.63e-33 |
|
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: 126.99 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 16 DDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA---NGIGMI 92
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQ----GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 173 MDEPTSALSA---AEV-EILFKVIAELKAqgvAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03294 184 MDEAFSALDPlirREMqDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-227 |
4.93e-33 |
|
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: 124.95 E-value: 4.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA-HAQANGIGM 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIfarREITRGILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:cd03262 81 VFQQFNLFPHLTVLENI---TLAPIKVKGMSKAEAEERALELLEKV--GLAdkADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-226 |
9.95e-33 |
|
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: 122.88 E-value: 9.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIG 90
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFaNMSVAENIfarreitrgilgidhkaqvqkanaflkrldagieadtmvedLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLeELMRIGDYITVLRDGQ 226
Cdd:cd03228 118 LILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-227 |
1.11e-32 |
|
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: 124.60 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAG-----VERPTLGRIILDGKPV-SFDSPAHAQA 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQELNLFaNMSVAENI-FARReiTRGILGIDH-KAQVQKAnafLKR--LDAGIEADTMVEDLPIGQQQLVEIAK 162
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVaYGLR--LHGIKLKEElDERVEEA---LRKaaLWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 163 AMSLNARILIMDEPTSAL---SAAEVEilfKVIAELKAQgVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03260 155 ALANEPEVLLLDEPTSALdpiSTAKIE---ELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-227 |
1.34e-32 |
|
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: 123.94 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 38 GAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsFDS------PAHAQanGIGMIFQELNLFANMSVAENifar 111
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-FDSrkkinlPPQQR--KIGLVFQQYALFPHLNVREN---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 112 reITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKV 191
Cdd:cd03297 96 --LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 499968440 192 IAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-227 |
2.73e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.57 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQA--NGI 89
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIfarreiTRG---ILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAM 164
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENV------TLApikVKKMSKAEAEERAMELLERV--GLAdkADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 165 SLNARILIMDEPTSAL---SAAEVEilfKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1126 152 AMEPKVMLFDEPTSALdpeLVGEVL---DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-227 |
3.06e-32 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 123.00 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGI--VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDsPAHAQANgIG 90
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD-RKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAEN--IFARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:cd03263 79 YCPQFDALFDELTVREHlrFYAR------LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKaQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-251 |
3.99e-32 |
|
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: 123.56 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGI-VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGM 91
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLK--RLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:cd03295 80 VIQQIGLFPHMTVEENI----ALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV----TGEAMVRDIDTRWiVRS 244
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIvqvgTPDEILRSPANDF-VAE 234
|
....*..
gi 499968440 245 MIGSDAK 251
Cdd:cd03295 235 FVGADRL 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-222 |
5.83e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.87 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSpahaqaNGIGMIF 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 Q--ELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:cd03235 75 QrrSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVL 222
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
282-488 |
1.12e-31 |
|
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: 121.10 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRardttrrirrglalipEDRQREGLV-QVLS 360
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----------------KERKRIGYVpQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 I-----ASNLTLASLGRF--TRLFHIDRGAEKSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:cd03235 79 IdrdfpISVRDVVLMGLYghKGLFRRLSKADKAKVDEALERVGLS----ELAdrqIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 431 LMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLsNGQLVA 488
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-227 |
1.19e-31 |
|
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: 122.06 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdSPAHAQANGIGMI 92
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARREitRGILGIDHKAQV-QKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03296 80 FQHYALFRHMTVFDNVaFGLRV--KPRSERPPEAEIrAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 171 LIMDEPTSALSAaeveilfKVIAELKA--------QGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03296 158 LLLDEPFGALDA-------KVRKELRRwlrrlhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-227 |
1.30e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.87 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDspAHAQANGIGMI 92
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN--LPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:COG1118 81 FQHYALFPHMTVAENIaFGLR-----VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 172 IMDEPTSALSA---AEVEI-LFKVIAELkaqGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1118 156 LLDEPFGALDAkvrKELRRwLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
282-486 |
1.39e-31 |
|
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: 119.81 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDttRRIRRGLALIPEDRqreGLVQVLSI 361
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYLPEEP---SLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgrftrlfhidrgaeksairdairdlsikapnpdfevtsmSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03230 91 RENLKL------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 442 GAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
265-488 |
1.88e-31 |
|
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: 121.69 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 265 VFRAENISLPRPTGGLsVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRgLA 344
Cdd:COG1120 1 MLEAENLSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 345 LIPedrqreglvQVLSIASNLT---LASLGRF--TRLFHIDRGAEKSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQK 416
Cdd:COG1120 79 YVP---------QEPPAPFGLTvreLVALGRYphLGLFGRPSAEDREAVEEALERTGLE----HLAdrpVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
282-488 |
2.48e-31 |
|
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: 120.69 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRArdTTRRIRRGLALIPedrQREGLVQVLSI 361
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQSLGYCP---QFDALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgrFTRLFHIDRGAEKSAIRDAIRDLSIKAPNpDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03263 93 REHLRF-----YARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 442 GAKADVFRTMRRLAANgLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03263 167 ASRRAIWDLILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-231 |
5.35e-31 |
|
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: 126.41 E-value: 5.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGM 91
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFAnMSVAENI-FARREITRgilgidhkAQVQKA------NAFLKRLDAGIeaDTMVED----LPIGQQQLVEI 160
Cdd:COG4988 416 VPQNPYLFA-GTIRENLrLGRPDASD--------EELEAAleaaglDEFVAALPDGL--DTPLGEggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 161 AKAMSLNARILIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLeELMRIGDYITVLRDGQVTGEA 231
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQG 553
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
282-503 |
9.91e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdttrriRRGLALIPedrqreglvQVLSI 361
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRIGYVP---------QRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASN--LT---LASLGRFTR--LFHIDRGAEKSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVLL 431
Cdd:COG1121 87 DWDfpITvrdVVLMGRYGRrgLFRRPSRADREAVDEALERVGLE----DLAdrpIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLsNGQLVAVFDRNEA-TEEAIIAA 503
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVlTPENLSRA 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-231 |
3.12e-30 |
|
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: 116.93 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQangIGMI 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarrEITRGILGIDHKAQvqkaNAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:cd03268 78 IEAPGFYPNLTARENL----RLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEA 231
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
282-485 |
3.17e-30 |
|
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: 116.13 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV-RARDTTRRIRRGLALIpedRQREGLVQVLS 360
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGMV---FQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLAslgrftrlfhidrgaeksairdairdlsikapnpdfevtsMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:cd03229 93 VLENIALG----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499968440 441 VGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-227 |
4.58e-30 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 117.08 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY----SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN 87
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 gIGMIFQELNLFANMSVAENI--FARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:cd03266 80 -LGFVSDSTGLYDRLTARENLeyFAG------LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-227 |
1.13e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGivAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAhaqANGIGMI 92
Cdd:COG3840 2 LRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---ERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARREITRgiLGIDHKAQVQKAnafLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAMsLNAR 169
Cdd:COG3840 77 FQENNLFPHLTVAQNIgLGLRPGLK--LTAEQRAQVEQA---LERV--GLAglLDRLPGQLSGGQRQRVALARCL-VRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 170 -ILIMDEPTSALSAA-EVEILfKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG3840 149 pILLLDEPFSALDPAlRQEML-DLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-227 |
1.14e-29 |
|
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: 114.84 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSkvysGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGI 89
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMI----FQELnLFANMSVAENIfarreitrgilgidhkaqvqkanaFLKRLDAGieadtmvedlpiGQQQLVEIAKAMS 165
Cdd:cd03215 78 AYVpedrKREG-LVLDLSVAENI------------------------ALSSLLSG------------GNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-228 |
2.40e-29 |
|
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: 118.66 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 31 ANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsFDS------PAHAQAngIGMIFQELNLFANMSV 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSargiflPPHRRR--IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 AENI-FARREITRGilgiDHKAQVQKANAFLkrldaGIEA--DTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSAL- 180
Cdd:COG4148 95 RGNLlYGRKRAPRA----ERRISFDEVVELL-----GIGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALd 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 181 SAAEVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:COG4148 166 LARKAEIL-PYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-227 |
4.39e-29 |
|
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: 114.74 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVaVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPahaQANGIGMI 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI--------FARREITR------GILGIDHkaqvqkanaFLKRldagieadtMVEDLPIGQQQLV 158
Cdd:cd03299 77 PQNYALFPHMTVYKNIayglkkrkVDKKEIERkvleiaEMLGIDH---------LLNR---------KPETLSGGEQQRV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 159 EIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-225 |
8.22e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 114.70 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN-GIG 90
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIARmGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENIFA--RREITRGIL-GI--------DHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVE 159
Cdd:PRK11300 84 RTFQHVRLFREMTVIENLLVaqHQQLKTGLFsGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 160 IAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDG 225
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
282-489 |
1.34e-28 |
|
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: 112.76 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRrirrgLALIPEDRqreGLVQVLSI 361
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLT-LASLgrftrlfhidRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:cd03269 88 IDQLVyLAQL----------KGLKKEEARRRIDEWLERlelSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 438 GIDVgAKADVFRT-MRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03269 158 GLDP-VNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-227 |
1.71e-28 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 115.90 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPahaQANGIGMI 92
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPP---QKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfARREITRGIlgidHKAQV-QKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:TIGR03265 82 FQSYALFPNLTVADNI-AYGLKNRGM----GRAEVaERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
267-485 |
1.84e-28 |
|
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: 112.18 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRArDTTRRIRRGLAL 345
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 346 I---PEDrqreglvQVLS------IASNLtlaslgrftRLFHIDRGAEKSAIRDAIRDLSIKAPnPDFEVTSMSGGNQQK 416
Cdd:cd03225 80 VfqnPDD-------QFFGptveeeVAFGL---------ENLGLPEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-498 |
2.13e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 118.37 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVE--RPTLGRII----------------LDGK 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 75 P------------VSFDSPAHAQANG----IGMIFQE-LNLFANMSVAENIF-ARREItrgilGIDHKAQVQKANAFLKR 136
Cdd:TIGR03269 81 PcpvcggtlepeeVDFWNLSDKLRRRirkrIAIMLQRtFALYGDDTVLDNVLeALEEI-----GYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 137 LDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRI 215
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 216 GDYITVLRDGQVTGEAMVRDIDTRWIvrsmigSDAKDFAKSVDHAVGAEVFRAEN-----ISLPRptgGL--SVNDVSLS 288
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFM------EGVSEVEKECEVEVGEPIIKVRNvskryISVDR---GVvkAVDNVSLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 289 VKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKI-------FIDGKHvRARDTTRRIRRGLALIpedRQREGLVQVLSI 361
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTK-PGPDGRGRAKRYIGIL---HQEYDLYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLA-------SLGRFTRLFHIdrgaeKSAIRDAIRDLSIKAPNPDfevtSMSGGNQQKVVIGKALMTNPKVLLMDE 434
Cdd:TIGR03269 383 LDNLTEAiglelpdELARMKAVITL-----KMVGFDEEKAEEILDKYPD----ELSEGERHRVALAQVLIKEPRIVILDE 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 435 PSRGIDVGAKADVFRTM--RRLAANGLAILFStSDLEEVMALSDRIAVLSNGQLVAVFDRNEATEE 498
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSIlkAREEMEQTFIIVS-HDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
267-487 |
2.81e-28 |
|
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: 112.21 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLS---VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR--IRR 341
Cdd:cd03257 3 EVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 342 GLALIPEDrQREGLVQVLSIASNLTLAslgrftrLFHIDRGAEKSAIRDAIRDLSIKAPNPD-------FEvtsMSGGNQ 414
Cdd:cd03257 83 EIQMVFQD-PMSSLNPRMTIGEQIAEP-------LRIHGKLSKKEARKEAVLLLLVGVGLPEevlnrypHE---LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 415 QKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAA-NGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-230 |
3.58e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGM 91
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-IGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFaNMSVAENI-FARREITRgilgidhkAQV----QKANA--FLKRLDAGIeaDTMVED----LPIGQQQLVEI 160
Cdd:COG1132 419 VPQDTFLF-SGTIRENIrYGRPDATD--------EEVeeaaKAAQAheFIEALPDGY--DTVVGErgvnLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 161 AKAMSLNARILIMDEPTSAL-SAAEVEIlFKVIAELkAQGVAIVYISHRLEELMRiGDYITVLRDGQVTGE 230
Cdd:COG1132 488 ARALLKDPPILILDEATSALdTETEALI-QEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-227 |
3.75e-28 |
|
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: 111.73 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 17 DVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQA---NGIGMI 92
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:cd03292 84 FQDFRLLPDRNVYENVaFALE-----VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 172 IMDEPTSAL---SAAEVEILFKVIaelKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03292 159 IADEPTGNLdpdTTWEIMNLLKKI---NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-228 |
5.77e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIF 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-SLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 QELNLfanmsvaenifarreitrgiLGIDHKaqvqkanaflkrldagieADTMVEDLPIGQQQLVEIAKAMSLNARILIM 173
Cdd:cd03214 80 QALEL--------------------LGLAHL------------------ADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 174 DEPTSALSAA-EVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03214 122 DEPTSHLDIAhQIELL-ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-489 |
6.12e-28 |
|
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: 109.44 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISlPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLAL 345
Cdd:cd03216 1 LELRGIT-KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 346 IPEdrqreglvqvlsiasnltlaslgrftrlfhidrgaeksairdairdlsikapnpdfevtsMSGGNQQKVVIGKALMT 425
Cdd:cd03216 80 VYQ------------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-488 |
6.56e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrardtTRRIRRGLALIPEDRqreGLVQVLSI 361
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRIGYLPEER---GLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLT-LASLgrftrlfhidRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:COG4152 89 GEQLVyLARL----------KGLSKAEAKRRADEWLERlglGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 438 GID-VGAkaDVFRTM-RRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG4152 159 GLDpVNV--ELLKDViRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-227 |
2.03e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 112.11 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMI 92
Cdd:COG1125 3 EFENVTKRYPdGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR-DLDPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKR--LDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:COG1125 82 IQQIGLFPHMTVAENI----ATVPRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 171 LIMDEPTSAL-----SAAEVEILfkviaELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG1125 158 LLMDEPFGALdpitrEQLQDELL-----RLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
280-489 |
2.06e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 109.76 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhVRARDTTRRIRRGLALIPEDRqreGLVQVL 359
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSDST---GLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLtlaslGRFTRLFHIDRGAEKSAIRDAIRDLSIKaPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGI 439
Cdd:cd03266 94 TARENL-----EYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 440 DVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-247 |
2.41e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.12 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 4 AEAQKDDVILRLDDVS-KVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA 82
Cdd:COG3845 249 APAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQANGIGMIFQELN---LFANMSVAENI----FARREITRGILgIDHKAQVQKANAFLKRLD---AGIeaDTMVEDLPI 152
Cdd:COG3845 329 ERRRLGVAYIPEDRLgrgLVPDMSVAENLilgrYRRPPFSRGGF-LDRKAIRAFAEELIEEFDvrtPGP--DTPARSLSG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 153 GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAM 232
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVP 485
|
250
....*....|....*
gi 499968440 233 VRDIDTRWIVRSMIG 247
Cdd:COG3845 486 AAEATREEIGLLMAG 500
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-239 |
2.43e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.12 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQA-NGIG 90
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKRArLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENIFARREITrgilGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELR----KLSKKEREERLEELLEEF--GIThlRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 169 RILIMDEPTSA---LSAAEVEilfKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV----TGEAMVRDIDTR 239
Cdd:COG1137 156 KFILLDEPFAGvdpIAVADIQ---KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVlaegTPEEILNNPLVR 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-227 |
3.24e-27 |
|
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: 107.69 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVA--VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIG 90
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANmSVAENIFARreitrgilgidhkaqvqkanaflkrldagieadtmvedlpiGQQQLVEIAKAMSLNARI 170
Cdd:cd03246 80 YLPQDDELFSG-SIAENILSG-----------------------------------------GQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLeELMRIGDYITVLRDGQV 227
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-236 |
3.70e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA- 86
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 -NGIGMIFQELNLFANMSVAENI-FARReitrgILGIDHKAQVQKANAFLKRLdaGIE--ADTMVEDLPIGQQQLVEIAK 162
Cdd:COG1135 81 rRKIGMIFQHFNLLSSRTVAENVaLPLE-----IAGVPKAEIRKRVAELLELV--GLSdkADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 163 AMSLNARILIMDEPTSAL-SAAEVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:COG1135 154 ALANNPKVLLCDEATSALdPETTRSIL-DLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-227 |
4.98e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.33 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA-----N 87
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAirllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFANMSVAENIFarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLI---EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 168 ARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
272-494 |
6.73e-27 |
|
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: 108.58 E-value: 6.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 272 SLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKhvrarDTTRR--IRRGLALIPED 349
Cdd:cd03299 5 NLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITNLppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 RqreGLVQVLSIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKV 429
Cdd:cd03299 80 Y---ALFPHMTVYKNIAYG-----LKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 430 LLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-248 |
1.11e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 110.66 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSG----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPV-SFDSPAHAQA-N 87
Cdd:PRK11153 3 ELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSEKELRKArR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFANMSVAENIFARREITrgilGIDhKAQV-QKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELA----GTP-KAEIkARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR---WIV 242
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHpkhPLT 237
|
....*.
gi 499968440 243 RSMIGS 248
Cdd:PRK11153 238 REFIQS 243
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-494 |
1.89e-26 |
|
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: 107.58 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLS---VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGL 343
Cdd:COG1124 3 EVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRR-KAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALIPED-------RQRegLVQVLSiasnLTLASLGRFTRLFHIDRGAEKSAIRDAIRDlsiKAPNpdfevtSMSGGNQQK 416
Cdd:COG1124 82 QMVFQDpyaslhpRHT--VDRILA----EPLRIHGLPDREERIAELLEQVGLPPSFLD---RYPH------QLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-227 |
2.07e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 7 QKDDVILRldDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSpahAQA 86
Cdd:PRK11432 3 QKNFVVLK--NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQELNLFANMSVAENI--------FARREItrgilgidhKAQVQKAnafLKRLD-AGIEaDTMVEDLPIGQQQL 157
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVgyglkmlgVPKEER---------KQRVKEA---LELVDlAGFE-DRYVDQISGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 158 VEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
266-488 |
3.64e-26 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 106.26 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRaRDTTRRIRRGLAL 345
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-KKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 346 I---PEDrqreglvQVLS------IAsnLTLASLGrftrlfhIDRGAEKSAIRDAIRDLSIKAPnPDFEVTSMSGGNQQK 416
Cdd:COG1122 80 VfqnPDD-------QLFAptveedVA--FGPENLG-------LPREEIRERVEEALELVGLEHL-ADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-295 |
4.34e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.65 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 1 MTTAEAQKDDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDS 80
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 PAHAQANgigMIFQELNLFANMSVAENI-FARR-------EITRGILgiDHKAQVQkanafLKRLdagieADTMVEDLPI 152
Cdd:PRK09452 83 AENRHVN---TVFQSYALFPHMTVFENVaFGLRmqktpaaEITPRVM--EALRMVQ-----LEEF-----AQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 153 GQQQLVEIAKAMSLNARILIMDEPTSALSAAeveiLFKVI-AELKA-Q---GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYK----LRKQMqNELKAlQrklGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 228 TGEAMVRDI---DTRWIVRSMIGsDAKDFAKSVDHAVGAEVFRAEnislprPTGGLSVNDVSLSVKAGEIL 295
Cdd:PRK09452 224 EQDGTPREIyeePKNLFVARFIG-EINIFDATVIERLDEQRVRAN------VEGRECNIYVNFAVEPGQKL 287
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-227 |
6.48e-26 |
|
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: 105.78 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIG 90
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR-DYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFaNMSVAENI-FARREITRGilGIDHKAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMS 165
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIaYGRPGATRE--EVEEAARAANAHEFIMELPEGY--DTVIGErgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVyISHRLEELMRIgDYITVLRDGQV 227
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDGKI 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-488 |
1.08e-25 |
|
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: 103.67 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPtGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRgLALI 346
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PedrqreglvQVLsiasnltlASLGrftrlfhidrgaeksairdaIRDLSikapnpDFEVTSMSGGNQQKVVIGKALMTN 426
Cdd:cd03214 79 P---------QAL--------ELLG--------------------LAHLA------DRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 427 PKVLLMDEPSRGIDVGAKADVFRTMRRLAA-NGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-485 |
1.25e-25 |
|
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: 102.71 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPtGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALI 346
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-AKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PEdrqreglvqvlsiasnltlaslgrftrlfhidrgaeksairdairdlsikapnpdfevtsMSGGNQQKVVIGKALMTN 426
Cdd:cd00267 79 PQ------------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 427 PKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-266 |
2.05e-25 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 106.81 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQanGIGMIFQELNLFANMSVAENI-FARReitrgILGI 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-NVPPHLR--HINMVFQSYALFPHMTVEENVaFGLK-----MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 122 DHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GV 200
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 201 AIVYISHRLEELMRIGDYITVLRDGQV----TGEAMVRDIDTRWIVRsMIGSDAKDFAKSVDHAVGAEVF 266
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIaqigTPEEIYEEPANLFVAR-FIGEINVFEATVIERKSEQVVL 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
282-489 |
3.05e-25 |
|
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: 103.37 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtrrIRRGLALIPEDRqreGLVQVLSI 361
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP---ERRNIGMVFQDY---ALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLAslgrfTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03259 90 AENIAFG-----LKLRGVPKAEIRARVRELLELVGLEGLLNRY-PHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 442 GAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03259 164 KLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-227 |
3.46e-25 |
|
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: 103.46 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 23 SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANm 102
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 103 SVAENI-FARREITRGIlgIDHKAQVQKANAFLKRLDAGIeaDTMV----EDLPIGQQQLVEIAKAMSLNARILIMDEPT 177
Cdd:cd03254 92 TIMENIrLGRPNATDEE--VIEAAKEAGAHDFIMKLPNGY--DTVLgengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 178 SALSAAEVEILFKVIAELKAQGVAIVyISHRLEELmRIGDYITVLRDGQV 227
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKGRTSII-IAHRLSTI-KNADKILVLDDGKI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-227 |
3.74e-25 |
|
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: 102.96 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSgiVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAhaqANGIGMI 92
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGILGIDHKAqVQKANA------FLKRLDagieadtmvEDLPIGQQQLVEIAKAMSL 166
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQA-IEVALArvglagLEKRLP---------GELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-232 |
5.68e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 102.63 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAvkRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaqaNGIGMI 92
Cdd:TIGR01277 1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ---RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarreitrgILGID-----HKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:TIGR01277 76 FQENNLFAHLTVRQNI---------GLGLHpglklNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 168 ARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAM 232
Cdd:TIGR01277 147 NPILLLDEPFSALDPLLREEMLALVKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
12-227 |
1.05e-24 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 102.76 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMK-------IIAGVErpTLGRIILDGKPV--SFDSPA 82
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIydKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQANgIGMIFQELNLFAnMSVAENI-FARReitrgILGIDHKAQVQK-ANAFLKRldAGI------EADTMVEDLPIGQ 154
Cdd:TIGR00972 79 ELRRR-VGMVFQKPNPFP-MSIYDNIaYGPR-----LHGIKDKKELDEiVEESLKK--AALwdevkdRLHDSALGLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 155 QQLVEIAKAMSLNARILIMDEPTSAL---SAAEVEilfKVIAELKAQgVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALdpiATGKIE---ELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGEL 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
266-500 |
1.45e-24 |
|
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: 102.26 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT--RRIRRGL 343
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALIpedRQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIR-----DLSIKAPNPdfeVTSMSGGNQQKVV 418
Cdd:cd03256 81 GMI---FQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAalervGLLDKAYQR---ADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 419 IGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLvaVFD--RNEA 495
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI--VFDgpPAEL 232
|
....*
gi 499968440 496 TEEAI 500
Cdd:cd03256 233 TDEVL 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-245 |
2.02e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.45 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMI 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI----FARREITRGIlgIDHKAQ---VQKAnaFLKRLdAGieadtmveDLPIGQQQLVEIAKAMS 165
Cdd:TIGR03410 81 PQGREIFPRLTVEENLltglAALPRRSRKI--PDEIYElfpVLKE--MLGRR-GG--------DLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRS 244
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRY 227
|
.
gi 499968440 245 M 245
Cdd:TIGR03410 228 L 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-228 |
2.17e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.71 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 17 DVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGkpVSFDSPAhAQANGI----GMI 92
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK-VDERLIrqeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARREItRGIlgidHKAQVQK-ANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:PRK09493 83 FQQFYLFPHLTALENVmFGPLRV-RGA----SKEEAEKqARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-227 |
2.52e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA-----N 87
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAirelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFANMSVAENIFarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLI---EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 168 ARILIMDEPTSALsaaEVEI---LFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK11124 160 PQVLLFDEPTAAL---DPEItaqIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
267-487 |
2.53e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 100.41 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIrrglALI 346
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI----GYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PEDRQReglvqvlsiasNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAP---NPdfevTSMSGGNQQKVVIGKAL 423
Cdd:cd03226 77 MQDVDY-----------QLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALkerHP----LSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
4.42e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.27 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 1 MTTAeAQKDDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMK-------IIAGVErpTLGRIILDG 73
Cdd:COG1117 1 MTAP-ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 74 KPVsFDS---PAHAQANgIGMIFQELNLFAnMSVAENI-FARReitrgILGIDHKAQ----VQKAnafLKRldAGI--Ea 143
Cdd:COG1117 78 EDI-YDPdvdVVELRRR-VGMVFQKPNPFP-KSIYDNVaYGLR-----LHGIKSKSEldeiVEES---LRK--AALwdE- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 144 dtmVED--------LPIGQQQLVEIAKAMSLNARILIMDEPTSAL---SAAEVEILfkvIAELKAQgVAIVYISHRLEEL 212
Cdd:COG1117 144 ---VKDrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALdpiSTAKIEEL---ILELKKD-YTIVIVTHNMQQA 216
|
....*.
gi 499968440 213 MRIGDY 218
Cdd:COG1117 217 ARVSDY 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-237 |
5.43e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.32 E-value: 5.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKV-YSGIVAVKRA----NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdSPAHAQA 86
Cdd:COG1101 1 MLELKNLSKTfNPGTVNEKRAldglNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQE--LNLFANMSVAEN--IFARREITRGI-LGIDhKAQVQKANAFLKRLDAGIEA--DTMVEDLPIGQQQlve 159
Cdd:COG1101 80 KYIGRVFQDpmMGTAPSMTIEENlaLAYRRGKRRGLrRGLT-KKRRELFRELLATLGLGLENrlDTKVGLLSGGQRQ--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 160 iakAMSL------NARILIMDEPTSAL---SAAEV-EILFKVIAElkaQGVAIVYISHRLEELMRIGDYITVLRDGQVtg 229
Cdd:COG1101 156 ---ALSLlmatltKPKLLLLDEHTAALdpkTAALVlELTEKIVEE---NNLTTLMVTHNMEQALDYGNRLIMMHEGRI-- 227
|
....*...
gi 499968440 230 eamVRDID 237
Cdd:COG1101 228 ---ILDVS 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-236 |
6.84e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 102.05 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY---SGIV-AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTL---GRIILDGKPVSFDSPAHA 84
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QA---NGIGMIFQE----LNlfANMSVAENIfarREITRGILGIDHKAQVQKANAFLKRLdaGI-EADTMVEDLPI---- 152
Cdd:COG0444 81 RKirgREIQMIFQDpmtsLN--PVMTVGDQI---AEPLRIHGGLSKAEARERAIELLERV--GLpDPERRLDRYPHelsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 153 GQQQLVEIAKAMSLNARILIMDEPTSALSA-AEVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVtIQAQIL-NLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
....*.
gi 499968440 231 AMVRDI 236
Cdd:COG0444 233 GPVEEL 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-227 |
7.43e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLG-RIILDGKP---VS-FDSPAHa 84
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDvWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 qangIGMIFQELNLF--ANMSVAE--------NIFARREITrgilgidhKAQVQKANAFLKRLDAGIEADTMVEDLPIGQ 154
Cdd:COG1119 80 ----IGLVSPALQLRfpRDETVLDvvlsgffdSIGLYREPT--------DEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 155 QQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQG-VAIVYISHRLEElmrIGDYIT---VLRDGQV 227
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE---IPPGIThvlLLKDGRV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-228 |
7.74e-24 |
|
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: 99.19 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGaVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANgIGMI 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAE--NIFARreiTRGILGIDHKAQVQKAnafLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03264 78 PQEFGVYPNFTVREflDYIAW---LKGIPSKEVKARVDEV---LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-245 |
9.28e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdSPAHAQANGIGMIFQ 94
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 95 ELNLFANMSVAENI------FARREITrgilgiDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:PRK10851 82 HYALFRHMTVFDNIafgltvLPRRERP------NAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 169 RILIMDEPTSALSA-AEVEI---LFKVIAELKAQGvaiVYISHRLEELMRIGDYITVLRDG---QV-TGEAMVRDIDTRW 240
Cdd:PRK10851 156 QILLLDEPFGALDAqVRKELrrwLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGnieQAgTPDQVWREPATRF 232
|
....*
gi 499968440 241 IVRSM 245
Cdd:PRK10851 233 VLEFM 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
280-489 |
1.34e-23 |
|
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: 98.98 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdtTRRIRRGLALIPEDRQREGlvqVL 359
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE--PREVRRRIGIVFQDLSVDD---EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLaslgrFTRLFHIDRGAEKSAIRDAIR--DLSIKApnpDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:cd03265 89 TGWENLYI-----HARLYGVPGAERRERIDELLDfvGLLEAA---DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 438 GIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
282-487 |
2.63e-23 |
|
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: 98.42 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV--RARDTTRRIRRGLALIpedRQREGLVQVL 359
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGKELRKARRRIGMI---FQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIR--DLSIKApnpDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:cd03258 98 TVFENVALP-----LEIAGVPKAEIEERVLELLElvGLEDKA---DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 438 GIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03258 170 ALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-230 |
3.69e-23 |
|
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: 97.83 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 16 DDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDsPAHAQANgIGMIFQE 95
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRR-IGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 96 LNLFANMSVAEN--IFARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIM 173
Cdd:cd03265 82 LSVDDELTGWENlyIHAR------LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 174 DEPTSALSAAEVEILFKVIAELKA-QGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
282-488 |
4.92e-23 |
|
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: 97.61 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPedrQREGLVQVLSI 361
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLP---QEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLtLASLgrftRLFHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03218 93 EENI-LAVL----EIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 442 GAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-227 |
5.07e-23 |
|
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: 97.28 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMI 92
Cdd:cd03245 5 FRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN-IGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANmSVAENI-FARREIT-RGILGIdhkAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSL 166
Cdd:cd03245 84 PQDVTLFYG-TLRDNItLGAPLADdERILRA---AELAGVTDFVNKHPNGL--DLQIGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVyISHRLeELMRIGDYITVLRDGQV 227
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLII-ITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
281-505 |
6.31e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.64 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPEDRQregLVQVLS 360
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLASlgrftrlFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK11614 97 VEENLAMGG-------FFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 441 VGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAvfdrnEATEEAIIAASA 505
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVL-----EDTGDALLANEA 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-226 |
6.54e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgigM 91
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN---M 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENI--------FARREITRGI---LGIDHKAQvqkanaFLKRldagieadtMVEDLPIGQQQLVEI 160
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIafglkqdkLPKAEIASRVnemLGLVHMQE------FAKR---------KPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 161 AKAMSLNARILIMDEPTSALSAAEVEIL-FKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
282-435 |
7.15e-23 |
|
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: 94.64 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRaRDTTRRIRRGLALIPEDRQregLVQVLSI 361
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQ---LFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 362 ASNLTLASlgrftRLFHIDRGAEKSAIRDAIRDLSIKAPN---PDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:pfam00005 77 RENLRLGL-----LLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
282-505 |
7.86e-23 |
|
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: 98.10 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRA--RDTTRRIRR--------GLALIPedrQ 351
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsRKELRELRRkkismvfqSFALLP---H 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 352 ReglvQVLS-IASNLTLASLGRFTRLfhidRGAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:cd03294 117 R----TVLEnVAFGLEVQGVPRAERE----ERAAEALELVGLEGWEHKYPD------ELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 431 LMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAVfdrneATEEAIIAASA 505
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQV-----GTPEEILTNPA 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-494 |
1.02e-22 |
|
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: 96.48 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLPRptGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECV-----IGRHTHSTGKIFIDGKHVRARDTTR-R 338
Cdd:cd03260 1 IELRDLNVYY--GDKHAlKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 339 IRRGLALIpedRQREGLVQvLSIASNLTLAslgrfTRLFHIDRGAEKSAI-RDAIRdlsiKAPNPDfEV------TSMSG 411
Cdd:cd03260 79 LRRRVGMV---FQKPNPFP-GSIYDNVAYG-----LRLHGIKLKEELDERvEEALR----KAALWD-EVkdrlhaLGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 412 GNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANgLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFD 491
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
...
gi 499968440 492 RNE 494
Cdd:cd03260 224 TEQ 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
282-489 |
1.57e-22 |
|
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: 95.78 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR----IRRGLALIPEDRQREglvq 357
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRdiamVFQNYALYPHMTVYD---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 vlSIASNLTLASLGRFTrlfhIDRGaeksaIRDAIRDLSIKApNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:cd03301 92 --NIAFGLKLRKVPKDE----IDER-----VREVAELLQIEH-LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 438 GID----VGAKADVFRTMRRLaanGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03301 160 NLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-230 |
1.77e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.71 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSF--DSPAHAQANG 88
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlkNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENIfARREITRGILGIDHKAQVQKANAFLKRLDagiEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-227 |
1.90e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY----------------------SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRI 69
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 70 ILDGKpVSfdSPAhaqanGIGMIFQelnlfANMSVAENIF--ARreitrgILGIDhKAQVQkanaflKRLD-----AGIE 142
Cdd:COG1134 84 EVNGR-VS--ALL-----ELGAGFH-----PELTGRENIYlnGR------LLGLS-RKEID------EKFDeivefAELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 143 AdtmVEDLPI-----GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGD 217
Cdd:COG1134 138 D---FIDQPVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|
gi 499968440 218 YITVLRDGQV 227
Cdd:COG1134 215 RAIWLEKGRL 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-227 |
2.02e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRldDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaqaNGI 89
Cdd:PRK11000 3 SVTLR--NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENI--------FARREITRgilGIDHKAQVQKANAFLKRLDagieadtmvEDLPIGQQQLVEIA 161
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMsfglklagAKKEEINQ---RVNQVAEVLQLAHLLDRKP---------KALSGGQRQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 162 KAMSLNARILIMDEPTSALSAA-EVEILFKvIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAAlRVQMRIE-ISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-236 |
2.66e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.36 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVA--VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgI 89
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQEL-NLFANMSVAENIFARREITrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:PRK13648 86 GIVFQNPdNQFVGSIVKYDVAFGLENH----AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKA-QGVAIVYISHRLEELMRiGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-233 |
2.70e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.72 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 11 VILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIG 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENI-----FARREitrgilgiDHKAQVQKANAFLKRLDA--GIEADTMVEdlpiGQQQLVEIAKA 163
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLamggfFAERD--------QFQERIKWVYELFPRLHErrIQRAGTMSG----GEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV----TGEAMV 233
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVvledTGDALL 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
282-488 |
2.77e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPedrQREGLVQVLSI 361
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP---QEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNL--TLASLGRFTRLFHIDRGAEK------SAIRDAIRDlsikapnpdfevtSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:PRK10895 96 YDNLmaVLQIRDDLSAEQREDRANELmeefhiEHLRDSMGQ-------------SLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 434 EPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
282-488 |
2.87e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.98 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdtTRRIRRGLALIPedrQREGLVQVLSI 361
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARARIGVVP---QFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLasLGRFTRLFHIDRGAEKSAIRDAIRdLSIKApnpDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:PRK13536 132 RENLLV--FGRYFGMSTREIEAVIPSLLEFAR-LESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 442 GAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIA 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
282-506 |
3.02e-22 |
|
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: 99.98 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIG---RHTHSTGKIFIDGKHVRARDTTRRIRRgLALIPEDrqreglvqv 358
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRR-IGMVFQD--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 lsIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFE---VTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:COG1123 92 --PMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLdryPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 436 SRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAvfdrnEATEEAIIAASAK 506
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVE-----DGPPEEILAAPQA 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-227 |
5.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIV--AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA 86
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NgIGMIFQEL-NLFANMSVAENI--------FARREITRGILGIDHKAQVQKanaFLKRldagiEAdtmvEDLPIGQQQL 157
Cdd:PRK13632 84 K-IGIIFQNPdNQFIGATVEDDIafglenkkVPPKKMKDIIDDLAKKVGMED---YLDK-----EP----QNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 158 VEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGV-AIVYISHRLEELMrIGDYITVLRDGQV 227
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
284-488 |
6.34e-22 |
|
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: 97.10 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKhvrardTTRRIRRGLALIPEDR------QREGLVQ 357
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR------TLFDSRKGIFLPPEKRrigyvfQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLtlaslgRFTRLFhiDRGAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:TIGR02142 89 HLSVRGNL------RYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 438 GIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-250 |
8.93e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 8.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGM 91
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS-MLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELnlfanmSVAENIFARREITR---------GILGIDHKAQVQKANAflkrlDAGIE--ADTMVEDLPIGQQQLVEI 160
Cdd:PRK11231 81 LPQHH------LTPEGITVRELVAYgrspwlslwGRLSAEDNARVNQAME-----QTRINhlADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 161 AKAMSLNARILIMDEPTSALSAA-EVEiLFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR 239
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINhQVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
250
....*....|.
gi 499968440 240 WIVRSMIGSDA 250
Cdd:PRK11231 229 GLLRTVFDVEA 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-230 |
9.60e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 9.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQ------- 85
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 -----ANGIGMIFQELNLFANMSVAENIFarrEITRGILGIDHKAQVQKANAFLKRLdaGIEADTMVE---DLPIGQQQL 157
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVM---EAPIQVLGLSKQEARERAVKYLAKV--GIDERAQGKypvHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 158 VEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
278-489 |
1.19e-21 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 93.84 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR----IRRGLALIPEdrqre 353
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRpvntVFQNYALFPH----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 glvqvLSIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIR-----DLSIKAPNpdfevtSMSGGNQQKVVIGKALMTNPK 428
Cdd:cd03300 87 -----LTVFENIAFG-----LRLKKLPKAEIKERVAEALDlvqleGYANRKPS------QLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 429 VLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-222 |
1.23e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.13 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG-IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAnGIGM 91
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANmSVAENI-FARREITRgiLGIDHKAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSL 166
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIrLARPDASD--AEIREALERAGLDEFVAALPQGL--DTPIGEggagLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLeELMRIGDYITVL 222
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-227 |
1.69e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAH-AQANGIGMIFQ--ELNLFANMSV 104
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlALRQQVATVFQdpEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 AENIFARREitrgiLGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAE 184
Cdd:PRK13638 97 SDIAFSLRN-----LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 185 VEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
278-487 |
1.71e-21 |
|
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: 92.67 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVraRDTTRRIRRGLALIpedrQREGLVQ 357
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALI----EAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTLASLGrftrlfhidRGAEKSAIRDAIRDLSIKApNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:cd03268 86 NLTARENLRLLARL---------LGIRKKRIDEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 438 GIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
282-491 |
1.90e-21 |
|
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: 92.53 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRardttrRIRRGLALIPedrQREGLVQVLSI 361
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPDRGYVF---QQDALLPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLASLGRFtrlfhIDRGAEKSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRG 438
Cdd:cd03293 91 LDNVALGLELQG-----VPKAEARERAEELLELVGLS----GFEnayPHQLSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 439 IDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSN--GQLVAVFD 491
Cdd:cd03293 162 LDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-227 |
2.01e-21 |
|
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: 92.20 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVE--RPTLGRIILDGKPVSFDSPAHAQANGIGMIFQELNLFANMSVA 105
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 106 EnifarreitrgilgidhkaqvqkanaFLKRLDAGIEAdtmvedlpiGQQQLVEIAKAMSLNARILIMDEPTSALSAAEV 185
Cdd:cd03217 96 D--------------------------FLRYVNEGFSG---------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 186 EILFKVIAELKAQGVAIVYISHRLEELMRI-GDYITVLRDGQV 227
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
269-505 |
2.67e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 92.75 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRR-GLALip 347
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKiGYVI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 348 edrQREGLVQVLSIASNLTLASlgrftRLFHIDRGAEKSAIRDAIRDLSIKAPN-----PDfevtSMSGGNQQKVVIGKA 422
Cdd:cd03295 82 ---QQIGLFPHMTVEENIALVP-----KLLKWPKEKIRERADELLALVGLDPAEfadryPH----ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 423 LMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAVfdrneATEEAII 501
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV-----GTPDEIL 224
|
....
gi 499968440 502 AASA 505
Cdd:cd03295 225 RSPA 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-227 |
2.88e-21 |
|
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: 92.53 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY---SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSP-AHAQa 86
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqYEHKyLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 ngIGMIFQELNLFANmSVAENifarreITRGILGIDH---KAQVQKANA--FLKRLDAGI--EADTMVEDLPIGQQQLVE 159
Cdd:cd03248 90 --VSLVGQEPVLFAR-SLQDN------IAYGLQSCSFecvKEAAQKAHAhsFISELASGYdtEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 160 IAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVyISHRLEELMRiGDYITVLRDGQV 227
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLV-IAHRLSTVER-ADQILVLDGGRI 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-207 |
2.93e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.33 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 1 MTTAEAQKddviLRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDS 80
Cdd:COG4598 1 MTDTAPPA----LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 PAH--------AQANGI----GMIFQELNLFANMSVAENIFarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVE 148
Cdd:COG4598 77 DRDgelvpadrRQLQRIrtrlGMVFQSFNLWSHMTVLENVI---EAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 149 DLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEV-EILfKVIAELKAQGVAIVYISH 207
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVgEVL-KVMRDLAEEGRTMLVVTH 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
32-227 |
3.11e-21 |
|
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: 92.60 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIagvER---PTLGRIILDGKPVSFDSPAHAQANgIGMIFQELNLFaNMSVAENI 108
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLF-DGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 -FARREITRgilgIDHKAQVQKANA--FLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSLNARILIMDEPTSALS 181
Cdd:cd03249 98 rYGKPDATD----EEVEEAAKKANIhdFIMSLPDGY--DTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499968440 182 aAEVEILFKVIAELKAQGVAIVYISHRLEELMRiGDYITVLRDGQV 227
Cdd:cd03249 172 -AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-236 |
3.40e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdSPAHAQA-NGIG 90
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARArRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENIFARREITRGIlgiDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDL---SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
263-488 |
3.69e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 263 AEVFRAENISLPRPTGGLSV---NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV-----RARD 334
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslseRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 335 TTRRirRGLALIPedrQREGLVQVLSIASNLTLASLgrftrLFHIDRGAEKSAIRDAIRDLSIKA-----PNpdfevtSM 409
Cdd:COG1136 82 RLRR--RHIGFVF---QFFNLLPELTALENVALPLL-----LAGVSRKERRERARELLERVGLGDrldhrPS------QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 410 SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDlEEVMALSDRIAVLSNGQLVA 488
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-487 |
3.73e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKS----TLMKIIAG--VERPTlGRIILDGKPVSFDSPA---HAQANGIGMIFQE--- 95
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPS-GDIRFHGESLLHASEQtlrGVRGNKIAMIFQEpmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 96 -LN--------LFANMSVAENIfaRREITRG-IL------GIDHKAqvQKANAFLKRLDAgieadtmvedlpiGQQQLVE 159
Cdd:PRK15134 104 sLNplhtlekqLYEVLSLHRGM--RREAARGeILncldrvGIRQAA--KRLTDYPHQLSG-------------GERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 160 IAKAMSLNARILIMDEPTSALSAA-EVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV----TGEAMV 233
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSvQAQIL-QLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCveqnRAATLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 234 RDIDTRWiVRSMIGSDAKDFAKSVDhAVGAEVFRAENISLPRPT-GGL---------SVNDVSLSVKAGEILGIYGLMGA 303
Cdd:PRK15134 246 SAPTHPY-TQKLLNSEPSGDPVPLP-EPASPLLDVEQLQVAFPIrKGIlkrtvdhnvVVKNISFTLRPGETLGLVGESGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 304 GRSEFFECVIgRHTHSTGKIFIDGK--HVRARDTTRRIRRGLALIPED-----RQREGLVQVlsIASNLtlaslgrftRL 376
Cdd:PRK15134 324 GKSTTGLALL-RLINSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDpnsslNPRLNVLQI--IEEGL---------RV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 377 FHIDRGAEK--SAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL 454
Cdd:PRK15134 392 HQPTLSAAQreQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
490 500 510
....*....|....*....|....*....|....
gi 499968440 455 -AANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK15134 472 qQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
267-486 |
3.79e-21 |
|
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: 91.78 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSV---NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRI---R 340
Cdd:cd03255 2 ELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 341 RGLALIPedrQREGLVQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIG 420
Cdd:cd03255 82 RHIGFVF---QSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPS------ELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 421 KALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDlEEVMALSDRIAVLSNGQL 486
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
267-488 |
5.26e-21 |
|
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: 96.37 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRrIRRGLALI 346
Cdd:COG4988 338 ELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS-WRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PedrQREGLVQvLSIASNLTLAslgrftrlfhiDRGAEKSAIRDAIRDLSIKA-----PN-PDFEVTS----MSGGNQQK 416
Cdd:COG4988 417 P---QNPYLFA-GTIRENLRLG-----------RPDASDEELEAALEAAGLDEfvaalPDgLDTPLGEggrgLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAnGLAILFSTSDLeEVMALSDRIAVLSNGQLVA 488
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVE 551
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
282-492 |
5.75e-21 |
|
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: 93.58 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSeffecVIGR--------HTHSTGKIFIDGKHVRA--RDTTRRIR-RGLALIPEDr 350
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKS-----TLARailgllppPGITSGEILFDGEDLLKlsEKELRKIRgREIQMIFQD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 351 qreglvqvlsiasnlTLASL------GR-FTRLFHIDRGAEKSAIRDAIRDL--SIKAPNPD-------FEvtsMSGGNQ 414
Cdd:COG0444 95 ---------------PMTSLnpvmtvGDqIAEPLRIHGGLSKAEARERAIELleRVGLPDPErrldrypHE---LSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 415 QKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV------ 487
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVeegpve 236
|
....*
gi 499968440 488 AVFDR 492
Cdd:COG0444 237 ELFEN 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
267-491 |
6.24e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.07 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISL--PRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtrriRRGL 343
Cdd:COG1116 9 ELRGVSKrfPTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP----DRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALipedrQREGLVQVLSIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIR--DLSikapnpDFE---VTSMSGGNQQKVV 418
Cdd:COG1116 85 VF-----QEPALLPWLTVLDNVALG-----LELRGVPKAERRERARELLElvGLA------GFEdayPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 419 IGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSN--GQLVAVFD 491
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEID 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
13-227 |
6.26e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAvkRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaqaNGIGMI 92
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIfarreitrgILGID-----HKAQVQKANAFLKRLdaGIEAdtMVEDLPI----GQQQLVEIAKA 163
Cdd:PRK10771 77 FQENNLFSHLTVAQNI---------GLGLNpglklNAAQREKLHAIARQM--GIED--LLARLPGqlsgGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 164 MSLNARILIMDEPTSALSAA-EVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPAlRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-227 |
6.60e-21 |
|
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: 91.78 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 24 GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMIFQElNLFANMS 103
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 104 VAENIFARREiTRGILGIDHKAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSLNARILIMDEPTSA 179
Cdd:cd03252 92 IRDNIALADP-GMSMERVIEAAKLAGAHDFISELPEGY--DTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 180 LSAAEVEILFKVIAELKAQGVAIVyISHRLEELMRiGDYITVLRDGQV 227
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVII-IAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-230 |
7.41e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPV-SFDSPAHAQAng 88
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFARK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENIFARREITRGILG---IDHKAQVQKANAF--LKRLdagieADTMVEDLPIGQQQLVEIAKA 163
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGRYPWHGALGrfgAADREKVEEAISLvgLKPL-----AHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 164 MSLNARILIMDEPTSALSAA-EVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAhQVDVL-ALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
7.58e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 7.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 1 MTTAEAQKDDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfds 80
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 PAHAQA--NGIGMIFQELNLFANMSVAEN--IFAR------REITRGILGIDHKAQVQKanaflkrldagiEADTMVEDL 150
Cdd:PRK13536 106 PARARLarARIGVVPQFDNLDLEFTVRENllVFGRyfgmstREIEAVIPSLLEFARLES------------KADARVSDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 151 PIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-228 |
1.35e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 95.20 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAhAQANGIG 90
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE-ELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANmSVAENIfARreitrgiLGIDHKAQVQKAnAflkRLdAGIEA---------DTMVED----LPIGQQQL 157
Cdd:COG4618 410 YLPQDVELFDG-TIAENI-AR-------FGDADPEKVVAA-A---KL-AGVHEmilrlpdgyDTRIGEggarLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 158 VEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLeELMRIGDYITVLRDGQVT 228
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQ 545
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-226 |
1.38e-20 |
|
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: 90.57 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYS-------GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIL--DGKPVSFdspA 82
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL---A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQA--------NGIGMIFQELNLFANMS----VAENIFARreitrgilGIDHKAQVQKANAFLKRLdaGIEadtmvEDL 150
Cdd:COG4778 81 QASPreilalrrRTIGYVSQFLRVIPRVSaldvVAEPLLER--------GVDREEARARARELLARL--NLP-----ERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 151 ----PI----GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVL 222
Cdd:COG4778 146 wdlpPAtfsgGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
....
gi 499968440 223 RDGQ 226
Cdd:COG4778 226 TPFS 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
278-486 |
1.73e-20 |
|
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: 89.90 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT-RRIRRGLALIpedRQREGL 355
Cdd:cd03262 11 GDFHVlKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGMV---FQQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASNLTLASlgrfTRLFHIDRG-AEKSAiRDAIRD--LSIKApnpDFEVTSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:cd03262 88 FPHLTVLENITLAP----IKVKGMSKAeAEERA-LELLEKvgLADKA---DAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499968440 433 DEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-239 |
1.83e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 20 KVYSGIVAVKRA-NLELRRGAVNVLVGENGAGKSTLMKIIAGV-----ERPTLGRIILDGKPVsFDSPAHAQANGIGMIF 93
Cdd:PRK14247 10 KVSFGQVEVLDGvNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDI-FKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 QELNLFANMSVAENIF----------ARREITRGILGIDHKAQVQkaNAFLKRLDAGieadtmVEDLPIGQQQLVEIAKA 163
Cdd:PRK14247 89 QIPNPIPNLSIFENVAlglklnrlvkSKKELQERVRWALEKAQLW--DEVKDRLDAP------AGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 164 MSLNARILIMDEPTSAL---SAAEVEILFkviAELKAQgVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR 239
Cdd:PRK14247 161 LAFQPEVLLADEPTANLdpeNTAKIESLF---LELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-278 |
1.89e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 26 VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA---HAQANGIGMIFQELNLFANM 102
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrEVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 103 SVAENIFARREITrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA 182
Cdd:PRK10070 122 TVLDNTAFGMELA----GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 183 AEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIdtrwivrsmIGSDAKDFAKSVDHAV 261
Cdd:PRK10070 198 LIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI---------LNNPANDYVRTFFRGV 268
|
250
....*....|....*...
gi 499968440 262 G-AEVFRAENISLPRPTG 278
Cdd:PRK10070 269 DiSQVFSAKDIARRTPNG 286
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-275 |
2.44e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQ-A 86
Cdd:PRK13636 2 EDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 NGIGMIFQEL-NLFANMSVAEnifarrEITRGI--LGIDHKAQVQKANAFLKRldAGIE--ADTMVEDLPIGQQQLVEIA 161
Cdd:PRK13636 82 ESVGMVFQDPdNQLFSASVYQ------DVSFGAvnLKLPEDEVRKRVDNALKR--TGIEhlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 162 KAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIdtrw 240
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---- 229
|
250 260 270
....*....|....*....|....*....|....*
gi 499968440 241 ivrsmigsdakdFAKSvdhavgaEVFRAENISLPR 275
Cdd:PRK13636 230 ------------FAEK-------EMLRKVNLRLPR 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
282-487 |
3.66e-20 |
|
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: 89.25 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGR-HTHST--GKIFIDGKHVRARDTTRRIRRGlalipedRQREGLVQV 358
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvEGGGTtsGQILFNGQPRKPDQFQKCVAYV-------RQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 LSIASNLTLASLGRFTRLFHiDRGAEKSAIRDAIRDLSIKAPNPDFeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRG 438
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSS-DAIRKKRVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 439 IDVGAKADVFRTMRRLAANGLAILFS----TSDLEEvmaLSDRIAVLSNGQLV 487
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTihqpRSDLFR---LFDRILLLSSGEIV 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-228 |
7.28e-20 |
|
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: 88.36 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 25 IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdspahaqaNGIGMIFQElnlfaNMSV 104
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGGGFNP-----ELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 AENIFarreITRGILGIDhKAQVQKANAFLKRLdAGIEADTmveDLPI-----GQQQLVEIAKAMSLNARILIMDEPTSA 179
Cdd:cd03220 102 RENIY----LNGRLLGLS-RKEIDEKIDEIIEF-SELGDFI---DLPVktyssGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 180 LSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
278-502 |
7.61e-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: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRA--RDTTRRIRRGLALIpedRQREG 354
Cdd:cd03261 11 GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMGML---FQSGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 LVQVLSIASNLTLAsLGRFTRLfhidrgaEKSAIRDAIRD------LSIKApnpDFEVTSMSGGNQQKVVIGKALMTNPK 428
Cdd:cd03261 88 LFDSLTVFENVAFP-LREHTRL-------SEEEIREIVLEkleavgLRGAE---DLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 429 VLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAvfdrnEATEEAIIA 502
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA-----EGTPEELRA 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-435 |
8.01e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdspahaqangIGMIFQ 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 95 ELNLFANMSVAENIFA----RREITRGILGIDHK-----------AQVQ-------------KANAFLKRLD-AGIEADT 145
Cdd:COG0488 69 EPPLDDDLTVLDTVLDgdaeLRALEAELEELEAKlaepdedlerlAELQeefealggweaeaRAEEILSGLGfPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 146 MVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILfkviaE--LKAQGVAIVYISHRLEELMRIGDYITVLR 223
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWL-----EefLKNYPGTVLVVSHDRYFLDRVATRILELD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 224 DGQVT---G-------------EAMVRDIDTR---------WIVR-------------------SMIGSDAKDFAKSV-- 257
Cdd:COG0488 224 RGKLTlypGnysayleqraerlEQEAAAYAKQqkkiakeeeFIRRfrakarkakqaqsrikaleKLEREEPPRRDKTVei 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 258 ----DHAVGAEVFRAENISLPRptGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIdGKHVR- 331
Cdd:COG0488 304 rfppPERLGKKVLELEGLSKSY--GDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKi 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 332 -----ARDTtrrirrglaLIPEDRQREGLVQVLSIASNLTLAS-LGRFtrLFHIDRgAEKSairdairdlsikapnpdfe 405
Cdd:COG0488 381 gyfdqHQEE---------LDPDKTVLDELRDGAPGGTEQEVRGyLGRF--LFSGDD-AFKP------------------- 429
|
490 500 510
....*....|....*....|....*....|
gi 499968440 406 VTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:COG0488 430 VGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-249 |
1.09e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPaHAQANgIGM 91
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQR-VGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAEN--IFARreiTRGILGIDHKAQVQKANAFlKRLDAgiEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:PRK13537 85 VPQFDNLDPDFTVRENllVFGR---YFGLSAAAARALVPPLLEF-AKLEN--KADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDidtrwIVRSMIGSD 249
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA-----LIESEIGCD 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
282-488 |
1.37e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGLALIPEDRqreglvqvlSI 361
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-RAASRRVASVPQDT---------SL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLASLGRFTRLFHIDR-----GAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHRSRfdtwtETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 437 RGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
266-486 |
1.71e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.79 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLpRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRrIRRGLAL 345
Cdd:COG4619 1 LELEGLSF-RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 346 IPedrQREGLVQVlSIASNLTLASLGRftrlfhiDRGAEKSAIRDAIRDLSIkapNPDF---EVTSMSGGNQQKVVIGKA 422
Cdd:COG4619 79 VP---QEPALWGG-TVRDNLPFPFQLR-------ERKFDRERALELLERLGL---PPDIldkPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 423 LMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-236 |
1.96e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA-NGI 89
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELN--LFANmSVAENI-FARREitrgiLGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:PRK13639 81 GIVFQNPDdqLFAP-TVEEDVaFGPLN-----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-211 |
2.04e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfDSPAHAQangiGM 91
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPGAER----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARREITrgilGIDHKAQVQKANAFLKRLD-AGIEAdTMVEDLPIGQQQLVEIAKAMSLNARI 170
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLA----GVEKMQRLEIAHQMLKKVGlEGAEK-RYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 171 LIMDEPTSALSAAEVE----ILFKVIAElkaQGVAIVYISHRLEE 211
Cdd:PRK11248 150 LLLDEPFGALDAFTREqmqtLLLKLWQE---TGKQVLLITHDIEE 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
284-488 |
3.35e-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: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKaGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhVRARDTtrriRRGLALIPEDR------QREGLVQ 357
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDS----RKKINLPPQQRkiglvfQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTLASlgrftrlfhidRGAEKSAIRDAIRDLSI--------KAPnpdfeVTSMSGGNQQKVVIGKALMTNPKV 429
Cdd:cd03297 89 HLNVRENLAFGL-----------KRKRNREDRISVDELLDllgldhllNRY-----PAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 430 LLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-228 |
6.47e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 31 ANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKpVSFDS------PAHAQanGIGMIFQELNLFANMSV 104
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAekgiclPPEKR--RIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 AENI-----------FARreITRgILGIDHkaqvqkanaFLKRLDAgieadtmveDLPIGQQQLVEIAKAMSLNARILIM 173
Cdd:PRK11144 94 RGNLrygmaksmvaqFDK--IVA-LLGIEP---------LLDRYPG---------SLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 174 DEPTSALS--------------AAEVEIlfkviaelkaqgvAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:PRK11144 153 DEPLASLDlprkrellpylerlAREINI-------------PILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
284-488 |
6.59e-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: 88.23 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRarDTTRRI-----RRGLALIP-EDRqregLVQ 357
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ--DSARGIflpphRRRIGYVFqEAR----LFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTLAslgrftrLFHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:COG4148 91 HLSVRGNLLYG-------RKRAPRAERRISFDEVVELLGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 438 GIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG4148 163 ALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-227 |
6.75e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 17 DVSKVYSGI---VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSP-----AHAQANG 88
Cdd:PRK14246 12 NISRLYLYIndkAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqidAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELNLFANMSVAENIFARREITrgilGIDHKAQVQK-ANAFLKRLDAGIEA----DTMVEDLPIGQQQLVEIAKA 163
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSH----GIKEKREIKKiVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAELKAQgVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-227 |
9.69e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMI 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNL-FAnmsvaeniFARREITR-GIL--GIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM---- 164
Cdd:COG4559 81 PQHSSLaFP--------FTVEEVVAlGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlw 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 165 ---SLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4559 153 epvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-488 |
9.69e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdtTRRIRRGLALIPedrQREGLVQVL 359
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARQRVGVVP---QFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLaslgrFTRLFhidrGAEKSAIRDAIRDLSIKA---PNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK13537 96 TVRENLLV-----FGRYF----GLSAAAARALVPPLLEFAkleNKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 437 RGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-207 |
1.45e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SG---IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSPAHAQ- 85
Cdd:PRK10535 4 LLELKDIRRSYpSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtLDADALAQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 -ANGIGMIFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISH 207
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
281-489 |
2.53e-18 |
|
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: 84.31 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRiRRGLALipedrQREGLVQVLS 360
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFVF-----QHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLAslgrfTRLFHIDRGAEKSAIRDAIRDL---------SIKAPNpdfevtSMSGGNQQKVVIGKALMTNPKVLL 431
Cdd:cd03296 91 VFDNVAFG-----LRVKPRSERPPEAEIRAKVHELlklvqldwlADRYPA------QLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-231 |
2.56e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGI--VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgI 89
Cdd:PRK13635 5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQEL-NLFANMSVAENI-FARREItrgilGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVaFGLENI-----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 168 ARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRiGDYITVLRDGQVTGEA 231
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-236 |
2.60e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.22 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG-----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSF---DSPAHA 84
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QANGIGMIFQ--ELNLFANmSVaenifaRREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMvEDLPI----GQQQLV 158
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TV------EREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVM-SQSPFqmsgGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 159 EIAKAMSLNARILIMDEPTSAL---SAAEVEILFKVIAElkAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRD 235
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLdpqSKRQVMRLLKSLQT--DENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
.
gi 499968440 236 I 236
Cdd:PRK13646 233 L 233
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
32-225 |
2.86e-18 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 83.61 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPV---SFDSPAHAQANGIGMIFQELNLFANMSVAENI 108
Cdd:NF038007 25 NFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlSYSQKIILRRELIGYIFQSFNLIPHLSIFDNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 farrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEIL 188
Cdd:NF038007 105 ----ALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARAV 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 499968440 189 FKVIAELKAQGVAIVYISHRlEELMRIGDYITVLRDG 225
Cdd:NF038007 181 LQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-227 |
3.05e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSPA-HAQangIGMIFQELNLFANmSVAENIf 109
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDHHYlHRQ---VALVGQEPVLFSG-SVRENI- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 110 arreitrgILGIDHK------AQVQKANA--FLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSLNARILIMDEPT 177
Cdd:TIGR00958 576 --------AYGLTDTpdeeimAAAKAANAhdFIMEFPNGY--DTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 178 SALSaAEVEILFKviAELKAQGVAIVYISHRLeELMRIGDYITVLRDGQV 227
Cdd:TIGR00958 646 SALD-AECEQLLQ--ESRSRASRTVLLIAHRL-STVERADQILVLKKGSV 691
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
282-488 |
3.52e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALIPedrqreglvQVLSI 361
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSSRQLARRLALLP---------QHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLT---LASLGRFTRLFHIDR--GAEKSAIRDAIRDLSIKAPnPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK11231 88 PEGITvreLVAYGRSPWLSLWGRlsAEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 437 RGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-227 |
4.20e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMK----IIAGVERPT-----LGRIILDGKPVSFD--- 79
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGshielLGRTVQREGRLARDirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 80 SPAHAqangiGMIFQELNLFANMSVAENIF----ARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQ 155
Cdd:PRK09984 84 SRANT-----GYIFQQFNLVNRLSVLENVLigalGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 156 QLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-241 |
4.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIG 90
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNL-FANMSVAENI-FARREITrgILGIDHKAQVQKANAflkrlDAGIEA--DTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLaFGPENLC--LPPIEIRKRVDRALA-----EIGLEKyrHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELmRIGDYITVLRDGQV----TGEAMVRDIDTRWI 241
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIvlegEPENVLSDVSLQTL 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
265-487 |
4.73e-18 |
|
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: 82.21 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 265 VFRAENISLPRPTGGLS---VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHT--HSTGKIFIDGKHVRARdttrRI 339
Cdd:cd03213 5 SFRNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKR----SF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 340 RRGLALIPEDrqreglvqvLSIASNLTlaslgrftrlfhidrgaeksaIRDAirdLSIKApnpdfEVTSMSGGNQQKVVI 419
Cdd:cd03213 81 RKIIGYVPQD---------DILHPTLT---------------------VRET---LMFAA-----KLRGLSGGERKRVSI 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFST-SDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIhQPSSEIFELFDKLLLLSQGRVI 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
275-488 |
5.84e-18 |
|
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: 87.20 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGLALIP-EDRQRE 353
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP-ASLRRQIGVVLqDVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 GlvqvlSIASNLTLASLGrfTRLFHIDRGAEKSAIRDAIRDLsikapnP---DFEV----TSMSGGNQQKVVIGKALMTN 426
Cdd:COG2274 563 G-----TIRENITLGDPD--ATDEEIIEAARLAGLHDFIEAL------PmgyDTVVgeggSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 427 PKVLLMDEPSRGIDVGAKADVFRTMRRLAAnGLAILFSTSDLeEVMALSDRIAVLSNGQLVA 488
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVE 689
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-497 |
6.36e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 25 IVAVKRANLELRRGAVNVLVGENGAGKS----TLMKII----AGVERPTL-----GRIILDGKPVSFDSPAHAQANGIGM 91
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagGLVQCDKMllrrrSRQVIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQE--LNLFANMSVAENIfarREITRGILGIDHKAQVQKANAFLKRLDAGiEADTMVEDLPI----GQQQLVEIAKAMS 165
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQI---AESIRLHQGASREEAMVEAKRMLDQVRIP-EAQTILSRYPHqlsgGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 166 LNARILIMDEPTSALSA---AEVEILFKVIAELKAQGVaiVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI------ 236
Cdd:PRK10261 185 CRPAVLIADEPTTALDVtiqAQILQLIKVLQKEMSMGV--IFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIfhapqh 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 237 -DTRWIVRS------MIGSD-------------AKDFAKSVDHAV--GAEVFRAENISLPRPT-GGL---------SVND 284
Cdd:PRK10261 263 pYTRALLAAvpqlgaMKGLDyprrfplislehpAKQEPPIEQDTVvdGEPILQVRNLVTRFPLrSGLlnrvtrevhAVEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrarDT-----TRRIRRGLALIPED-------RQR 352
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI---DTlspgkLQALRRDIQFIFQDpyasldpRQT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 353 EGlvqvLSIASNLtlaslgRFTRLFHIDRGAEKSAIrdAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:PRK10261 420 VG----DSIMEPL------RVHGLLPGKAAAARVAW--LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 433 DEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNEATE 497
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-227 |
6.37e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.28 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSG-IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAhaqANGIGM 91
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENI--------FARREITRgilGIDHKAQVQKANAFLKRLDAgieadtmveDLPIGQQQLVEIAKA 163
Cdd:PRK11650 81 VFQNYALYPHMSVRENMayglkirgMPKAEIEE---RVAEAARILELEPLLDRKPR---------ELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 164 MSLNARILIMDEPTSALSAA-----EVEILfKVIAELKAQGvaiVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKlrvqmRLEIQ-RLHRRLKTTS---LYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
282-502 |
6.45e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPED----RQreglvq 357
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYLPQEasifRK------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 vLSIASNLtLASLgrftRLFHIDRGAEKSAIRDAIRDLSI------KAPnpdfevtSMSGGNQQKVVIGKALMTNPKVLL 431
Cdd:COG1137 93 -LTVEDNI-LAVL----ELRKLSKKEREERLEELLEEFGIthlrksKAY-------SLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAvfdrnEATEEAIIA 502
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLA-----EGTPEEILN 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
267-487 |
8.27e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRA--RDTTRRIRRGLA 344
Cdd:COG2884 3 RFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkRREIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 345 LIPEDRQregLVQVLSIASNLTLAslgrfTRLfhidRGAEKSAIRDAIRD------LSIKApnpDFEVTSMSGGNQQKVV 418
Cdd:COG2884 83 VVFQDFR---LLPDRTVYENVALP-----LRV----TGKSRKEIRRRVREvldlvgLSDKA---KALPHELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 419 IGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-227 |
9.07e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVE--RPTLGRIILDGKPVSFDSP---AHAqanGIGMIFQ---ElnlFANMS 103
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPderARA---GIFLAFQypvE---IPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 104 VAEniFARREIT-RGILGIDHKAQVQKANAFLKRLdaGIEADtMV-----EDLPIGQQQLVEIAKAMSLNARILIMDEPT 177
Cdd:COG0396 94 VSN--FLRTALNaRRGEELSAREFLKLLKEKMKEL--GLDED-FLdryvnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 178 SALSAAEVEILFKVIAELKAQGVAIVYISH--RLEELMRIgDYITVLRDGQV 227
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRSPDRGILIITHyqRILDYIKP-DFVHVLVDGRI 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-220 |
1.04e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 7 QKDDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSP-AHAQ 85
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 AngIGMIFQELNLFANmSVAENIFARREITRgilgidhkaQVQKANAFLKRLDAGIEADTM----VEDLPIGQQQLVEIA 161
Cdd:PRK10247 82 Q--VSYCAQTPTLFGD-TVYDNLIFPWQIRN---------QQPDPAIFLDDLERFALPDTIltknIAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 162 KAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYIT 220
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVIT 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-230 |
1.07e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.28 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGK--PVSFDSPAHAQANGIGMIFQELNLFANMSVAENI- 108
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 FARREITRGILGIDHKAQVQKANAFLKRLdagiEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEIL 188
Cdd:PRK11831 107 YPLREHTQLPAPLLHSTVMMKLEAVGLRG----AAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 189 FKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGE 230
Cdd:PRK11831 183 VKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
282-489 |
1.13e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 84.38 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhvraRDTTRrirrglaLIPEDR------QREGL 355
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-----RDVTG-------LPPEKRnvgmvfQDYAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASN----LTLaslgrftrlfhidRGAEKSAIRDAIRD------LSikapnpDFE---VTSMSGGNQQKVVIGKA 422
Cdd:COG3842 89 FPHLTVAENvafgLRM-------------RGVPKAEIRARVAEllelvgLE------GLAdryPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 423 LMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-239 |
1.28e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSG-IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSpAHAQANGIG 90
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-IREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNlfanmsvaENIFA---RREITRGI--LGIDHKAQVQKANAFLKRLdaGIEA--DTMVEDLPIGQQQLVEIAKA 163
Cdd:PRK13652 82 LVFQNPD--------DQIFSptvEQDIAFGPinLGLDEETVAHRVSSALHML--GLEElrDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR 239
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-209 |
1.62e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 20 KVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGI-------GMI 92
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrqlrqhvGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGIlgiDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEGPVIVKGE---PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRL 209
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-209 |
1.72e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVY----------SGIV-AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS 77
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgrtVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 78 FDSPA-------HAQangigMIFQE----LNlfANMSVAENIfarREITRgILGIDHKAQVQ-KANAFLKRLdaGIEADT 145
Cdd:COG4608 84 GLSGRelrplrrRMQ-----MVFQDpyasLN--PRMTVGDII---AEPLR-IHGLASKAERReRVAELLELV--GLRPEH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 146 MvEDLPI----GQQQLVEIAKAMSLNARILIMDEPTSALsaaEVEILFKVI---AELKAQ-GVAIVYISHRL 209
Cdd:COG4608 151 A-DRYPHefsgGQRQRIGIARALALNPKLIVCDEPVSAL---DVSIQAQVLnllEDLQDElGLTYLFISHDL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
264-488 |
2.04e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 81.67 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 264 EVFRAENISLPRptGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFEcVIGRHTHSTgkifiDGKHVRARDTtrriRRG 342
Cdd:COG1119 2 PLLELRNVTVRR--GGKTIlDDISWTVKPGEHWAILGPNGAGKSTLLS-LITGDLPPT-----YGNDVRLFGE----RRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 343 LALIPEDRQREGLV---QVLSIASNLTL---------ASLGRFTRLFHIDRgaekSAIRDAIRDLSI--KApnpDFEVTS 408
Cdd:COG1119 70 GEDVWELRKRIGLVspaLQLRFPRDETVldvvlsgffDSIGLYREPTDEQR----ERARELLELLGLahLA---DRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 409 MSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANG-LAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
.
gi 499968440 488 A 488
Cdd:COG1119 223 A 223
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-226 |
2.08e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.42 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 25 IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERP----TLGRIILDGKPVSFDSPA---HAQANGIGMIFQELN 97
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRerrKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 98 lfANMSVAENIFarREITRGILGID--------HKAQVQKANAFLKRLdaGIEADTMVED-----LPIGQQQLVEIAKAM 164
Cdd:COG4170 100 --SCLDPSAKIG--DQLIEAIPSWTfkgkwwqrFKWRKKRAIELLHRV--GIKDHKDIMNsypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 165 SLNARILIMDEPTSAL-SAAEVEIlFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:COG4170 174 ANQPRLLIADEPTNAMeSTTQAQI-FRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQ 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
280-506 |
2.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALIPE--DRQREGLVQ 357
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-SKENLKEIRKKIGIIFQnpDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTlaslgrftrlfhiDRGAEKSAIRDAIRDLSIKAPNPDF---EVTSMSGGNQQKVVIGKALMTNPKVLLMDE 434
Cdd:PRK13632 102 EDDIAFGLE-------------NKKVPPKKMKDIIDDLAKKVGMEDYldkEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 435 PSRGIDVGAKADVFRTMRRLAANGLAILFS-TSDLEEVMaLSDRIAVLSNGQLVAVFDRNEATEEAIIAASAK 506
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAK 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-230 |
3.51e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSPAHAQA--NGIGMIFQELNLFANMSV 104
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSkLSSAAKAELrnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 AENIFARREItrgilGIDHKAQVQ-KANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAA 183
Cdd:PRK11629 105 LENVAMPLLI-----GKKKPAEINsRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 184 EVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITvLRDGQVTGE 230
Cdd:PRK11629 180 NADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-227 |
3.79e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.30 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 4 AEAQKDDVILRldDVSKVYSG--IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSP 81
Cdd:PRK11176 335 IERAKGDIEFR--NVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 82 AHAQANGIGMIFQELNLFaNMSVAENI-FARREI-TRGilGIDHKAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQ 155
Cdd:PRK11176 412 LASLRNQVALVSQNVHLF-NDTIANNIaYARTEQySRE--QIEEAARMAYAMDFINKMDNGL--DTVIGEngvlLSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 156 QLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVyISHRLEELMRiGDYITVLRDGQV 227
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEI 556
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-228 |
3.81e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILdGKPVS---FDspahaqa 86
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKigyFD------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 ngigmifQEL-NLFANMSVAENIfarREITRGilgidhkAQVQKANAFLKRLD-AGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:COG0488 385 -------QHQeELDPDKTVLDEL---RDGAPG-------GTEQEVRGYLGRFLfSGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAELKaqGVAIVyISHRLEELMRIGDYITVLRDGQVT 228
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFP--GTVLL-VSHDRYFLDRVATRILEFEDGGVR 508
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-227 |
4.52e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.97 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 11 VILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIG 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAM------ 164
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVV----AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-238 |
5.60e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSpAHAQANGIGMI 92
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGILGI---DHKAQVQKAnafLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTwteTDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDT 238
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-226 |
6.22e-17 |
|
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: 79.46 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 24 GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQanGIGMIFQELNLFANMS 103
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 104 VAENI-FARReitrgilgIDHKAQVQKAnafLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA 182
Cdd:cd03231 90 VLENLrFWHA--------DHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499968440 183 AEVEILFKVIAELKAQGVAIVYISHrlEELMRIGDYITVLRDGQ 226
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTH--QDLGLSEAGARELDLGF 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
282-487 |
6.75e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.07 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR----IRRGLALIPEdrqreglvq 357
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdicmVFQSYALFPH--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 vLSIASNLtlaslGRFTRLFHIDRGAEKSAIRDAIR--DLSikapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:PRK11432 93 -MSLGENV-----GYGLKMLGVPKEERKQRVKEALElvDLA------GFEdryVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 433 DEPSRGIDvgakADVFRTMR---RLAANGLAI--LFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11432 161 DEPLSNLD----ANLRRSMRekiRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
269-486 |
7.17e-17 |
|
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: 79.37 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRA--RDTTRRIRRGLALI 346
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PEDRQregLVQVLSIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEvTSMSGGNQQKVVIGKALMTN 426
Cdd:cd03292 84 FQDFR---LLPDRNVYENVAFA-----LEVTGVPPREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 427 PKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-207 |
7.22e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA-------HAQ 85
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachylgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 AngigmifqelnLFANMSVAENIfarrEITRGILGiDHKAQVQKAnafLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:PRK13539 83 A-----------MKPALTVAENL----EFWAAFLG-GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISH 207
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
281-488 |
7.39e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 79.56 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGLALIPEDrqreglVQVL- 359
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQD------VTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 -SIASNLTLAslgrftRLFHIDRGAEKSAIRDAIRDLSIKAPNP-DFEV----TSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:cd03245 92 gTLRDNITLG------APLADDERILRAAELAGVTDFVNKHPNGlDLQIgergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 434 EPSRGIDVGAKADVFRTMRRLAAnGLAILFSTSDLeEVMALSDRIAVLSNGQLVA 488
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVA 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
283-486 |
8.59e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.75 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRirrglalipEDRQREGLV-QVLSI 361
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER---------LIRQEAGMVfQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLASLGRFTRLfHIdRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRG 438
Cdd:PRK09493 89 FPHLTALENVMFGPL-RV-RGASKEEAEKQARELLAKvglAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 439 IDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-236 |
9.07e-17 |
|
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: 82.93 E-value: 9.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 5 EAQKDDVILRLDDVSKVY----SGIV-AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRII-------LD 72
Cdd:TIGR03269 272 EVEVGEPIIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 73 GKPVSFDSPAHAQANgIGMIFQELNLFANMSVAENI-----------FARRE--ITRGILGIDHKaqvqKANAFLkrlda 139
Cdd:TIGR03269 352 MTKPGPDGRGRAKRY-IGILHQEYDLYPHRTVLDNLteaiglelpdeLARMKavITLKMVGFDEE----KAEEIL----- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 140 gieaDTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA-AEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDY 218
Cdd:TIGR03269 422 ----DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
250 260
....*....|....*....|..
gi 499968440 219 ITVLRDGQV--TG--EAMVRDI 236
Cdd:TIGR03269 498 AALMRDGKIvkIGdpEEIVEEL 519
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
282-489 |
9.11e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 81.73 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGK----HVRARDttRRIrrGL-----ALIPEdrqr 352
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftNLPPRE--RRV--GFvfqhyALFPH---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 353 eglvqvLSIASNLtlaslgrftrLFHID-RGAEKSAIRDAIRDLsIKApnpdFEVTSM--------SGGNQQKVVIGKAL 423
Cdd:COG1118 90 ------MTVAENI----------AFGLRvRPPSKAEIRARVEEL-LEL----VQLEGLadrypsqlSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-228 |
9.94e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.68 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 22 YSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMIF-QELNLFA 100
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR--IGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 101 NMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSAL 180
Cdd:cd03267 109 DLPVIDSF----YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 181 SAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-227 |
1.16e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.82 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGV-----ERPTLGRIILDGKPVSfdSPAHAQA 86
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIY--SPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 N---GIGMIFQELNLFAnMSVAEN-IFARReitrgILGIDHKAqvqkanaflkRLDAGIEADTM-------VED------ 149
Cdd:PRK14239 83 DlrkEIGMVFQQPNPFP-MSIYENvVYGLR-----LKGIKDKQ----------VLDEAVEKSLKgasiwdeVKDrlhdsa 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 150 --LPIGQQQLVEIAKAMSLNARILIMDEPTSAL---SAAEVEilfKVIAELKAQgVAIVYISHRLEELMRIGDYITVLRD 224
Cdd:PRK14239 147 lgLSGGQQQRVCIARVLATSPKIILLDEPTSALdpiSAGKIE---ETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLD 222
|
...
gi 499968440 225 GQV 227
Cdd:PRK14239 223 GDL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-238 |
1.39e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVY--SGIVA-------VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA 82
Cdd:PRK10419 3 LLNVSGLSHHYahGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQA--NGIGMIFQE----LNlfANMSVAENIfarREITRGILGIDHKAQVQKANAFLKRLDAGIE-ADTMVEDLPIGQQ 155
Cdd:PRK10419 83 QRKAfrRDIQMVFQDsisaVN--PRKTVREII---REPLRHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 156 QLVEIAKAMSLNARILIMDEptsALSAAEVEILFKVIAELKA----QGVAIVYISHRLEELMRIGDYITVLRDGQVTGEA 231
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDE---AVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
....*..
gi 499968440 232 MVRDIDT 238
Cdd:PRK10419 235 PVGDKLT 241
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-227 |
1.64e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 78.81 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYS-GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGM 91
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-EVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFaNMSVAENI-FARREITrgilgidhKAQVQKAnAFLKRLDAGIEA-----DTMVED----LPIGQQQLVEIA 161
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIrYGRPDAT--------DEEVIEA-AKAAQIHDKIMRfpdgyDTIVGErglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 162 KAMSLNARILIMDEPTSAL-SAAEVEILfKVIAELkAQGVAIVYISHRLEELMRiGDYITVLRDGQV 227
Cdd:cd03253 150 RAILKNPPILLLDEATSALdTHTEREIQ-AALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
282-484 |
1.89e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 78.66 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRglalipedrQREGLVQVLSI 361
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---------QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLAslgrFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:TIGR01184 72 RENIALA----VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499968440 442 GAKADVF-RTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNG 484
Cdd:TIGR01184 148 LTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-227 |
2.95e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTlGRIILDGKPVSfDSPAHAQA-----------NGIGM-IFQELNLF 99
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLS-DWSAAELArhraylsqqqsPPFAMpVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 100 --ANMSVAENIFARREITRGiLGIDHKaqvqkanafLKRldagieadtMVEDLPIGQQQLVEIAKAM-----SLN--ARI 170
Cdd:COG4138 94 qpAGASSEAVEQLLAQLAEA-LGLEDK---------LSR---------PLTQLSGGEWQRVRLAAVLlqvwpTINpeGQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
278-487 |
3.05e-16 |
|
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: 77.62 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGeILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTrrIRRGLALIPEDrqreglvq 357
Cdd:cd03264 12 KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK--LRRRIGYLPQE-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 vLSIASNLT-LASLGRFTRLFHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:cd03264 81 -FGVYPNFTvREFLDYIAWLKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 437 RGIDVGAKAdVFRTM-RRLAANGLAILfSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:cd03264 159 AGLDPEERI-RFRNLlSELGEDRIVIL-STHIVEDVESLCNQVAVLNKGKLV 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
283-489 |
3.10e-16 |
|
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: 78.10 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhvraRDTTRRIRRGLALIpedRQREGLV-QV--- 358
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG-----QDITGLSEKELYEL---RRRIGMLfQGgal 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 ---LSIASNLTLAsLGRFTRLfhidrgaEKSAIRDAIRD-LSI--------KAPNpdfevtSMSGGNQQKVVIGKALMTN 426
Cdd:COG1127 94 fdsLTVFENVAFP-LREHTDL-------SEAEIRELVLEkLELvglpgaadKMPS------ELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 427 PKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-227 |
4.98e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHaQANGIGMIFQELNLFANmsvae 106
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRIRMIFQDPSTSLN----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 107 nifARREITRgIL--------GIDHKAQVQKANAFLKRLdaGIEADTMV---EDLPIGQQQLVEIAKAMSLNARILIMDE 175
Cdd:PRK15112 102 ---PRQRISQ-ILdfplrlntDLEPEQREKQIIETLRQV--GLLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 176 PTSALSAAEVEILFKVIAELKA-QGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-230 |
5.21e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 75.81 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY--SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdSPAHAQANGIG 90
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFaNMSVAENIFARreitrgilgidhkaqvqkanaflkrldagieadtmvedLPIGQQQLVEIAKAMSLNARI 170
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNLGRR--------------------------------------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 171 LIMDEPTSALSA-AEVEILFKVIAELKaqGVAIVYISHRLEELMRIgDYITVLRDGQVTGE 230
Cdd:cd03247 120 VLLDEPTVGLDPiTERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
27-259 |
5.39e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVE----RPTLGRIILDGKPVSFDSPAHAQ---ANGIGMIFQELNlf 99
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 100 ANMSVAENIfaRREITRGILGIDHKAQ--------VQKANAFLKRLDAGIEADTMVE---DLPIGQQQLVEIAKAMSLNA 168
Cdd:PRK15093 100 SCLDPSERV--GRQLMQNIPGWTYKGRwwqrfgwrKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI-------DTRW 240
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELvttphhpYTQA 257
|
250
....*....|....*....
gi 499968440 241 IVRSMigsdaKDFAKSVDH 259
Cdd:PRK15093 258 LIRAI-----PDFGSAMPH 271
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-242 |
5.68e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.24 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQaNG 88
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR-SK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 89 IGMIFQELN--LFAnMSVAENI-FARREitrgiLGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS 165
Cdd:PRK13647 81 VGLVFQDPDdqVFS-STVWDDVaFGPVN-----MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 166 LNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIV 242
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-227 |
8.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 8 KDDVILRLDDVSKVYSG-----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRI----ILDGKPVSF 78
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 79 DSPAHAQANG-----------IGMIFQ--ELNLFANMsvaenifARREITRG--ILGIDHKAQVQKANAFLKRLDAGiea 143
Cdd:PRK13631 97 HELITNPYSKkiknfkelrrrVSMVFQfpEYQLFKDT-------IEKDIMFGpvALGVKKSEAKKLAKFYLNKMGLD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 144 DTMVEDLPI----GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYI 219
Cdd:PRK13631 167 DSYLERSPFglsgGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEV 246
|
....*...
gi 499968440 220 TVLRDGQV 227
Cdd:PRK13631 247 IVMDKGKI 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-236 |
9.46e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.53 E-value: 9.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVY--SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERP---TLGRIILDGKPVSFDSPAHA 84
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QANgIGMIFQEL-NLFANMSVAENIFARREiTRGILGIDHKAQVQKANAFLKRLDAgieADTMVEDLPIGQQQLVEIAKA 163
Cdd:PRK13640 83 REK-VGIVFQNPdNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDY---IDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEElMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
282-489 |
1.27e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.19 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhvraRDTTRrirrglaLIPEDRqreGLVQV--- 358
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG-----RDVTD-------LPPKDR---NIAMVfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 ------LSIASNLTLAsLgrftRLfhidRGAEKSAIRDAIRD----LSIKA-----PnpdfevTSMSGGNQQKVVIGKAL 423
Cdd:COG3839 84 yalyphMTVYENIAFP-L----KL----RKVPKAEIDRRVREaaelLGLEDlldrkP------KQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQV 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
275-487 |
1.27e-15 |
|
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: 76.37 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRrIRRGLALIpedrQREG 354
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW-LRRQVGVV----LQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 LVQVLSIASNLTLASLGRFTRlfHIDRGAEKSAIRDAIRDLSIKAPNPDFEV-TSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:cd03252 86 VLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFISELPEGYDTIVGEQgAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499968440 434 EPSRGIDVGAKADVFRTMRRLAANGLAILFSTSdLEEVMAlSDRIAVLSNGQLV 487
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHR-LSTVKN-ADRIIVMEKGRIV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-488 |
1.77e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 75.22 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLAlipedrQREGLVQVLSIAS 363
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF------QENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 364 NLTLASLGRFtRLFHIDRGA-EKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVG 442
Cdd:cd03298 90 NVGLGLSPGL-KLTAEDRQAiEVALARVGLAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 443 AKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03298 163 LRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-247 |
1.86e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.56 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAqANGIGMI 92
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV-ARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 173 MDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIG 247
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
284-487 |
1.89e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIfidgkHVRARDTTRRirrGLALIPEDRQR----------- 352
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-----HYRMRDGQLR---DLYALSEAERRrllrtewgfvh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 353 ----EGLVQVLSIASNL--TLASLGrftrlfhiDR--GAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALM 424
Cdd:PRK11701 96 qhprDGLRMQVSAGGNIgeRLMAVG--------ARhyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 425 TNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-207 |
2.07e-15 |
|
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: 74.70 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQanGIGMI 92
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--NILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENI-FARReitrgilgiDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:TIGR01189 79 GHLPGLKPELSALENLhFWAA---------IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISH 207
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-227 |
2.35e-15 |
|
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: 79.67 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 23 SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMIFQELNLFANM 102
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS--LGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 103 SVAENIFARREITrgilGIDHKAQVQKANAFLKrlDAGI--EADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSAL 180
Cdd:TIGR01257 1019 TVAEHILFYAQLK----GRSWEEAQLEMEAMLE--DTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 181 SAAEVEILFKVIAELKAqGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-236 |
2.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSG------IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA 82
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 83 HAQANGIGMIFQELNlfaNMSVA-----------ENifarreitrgiLGIDHKaqvqkanAFLKRLDAGIEADTMVED-- 149
Cdd:PRK13633 81 WDIRNKAGMVFQNPD---NQIVAtiveedvafgpEN-----------LGIPPE-------EIRERVDESLKKVGMYEYrr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 150 -----LPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRiGDYITVLR 223
Cdd:PRK13633 140 haphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMD 218
|
250
....*....|...
gi 499968440 224 DGQVTGEAMVRDI 236
Cdd:PRK13633 219 SGKVVMEGTPKEI 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-227 |
2.72e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYS---GIVA----VKRAN---LELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFD 79
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrGLFKperlVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 80 SPAHAQA--NGIGMIFQelNLFANMSvaenifARREItRGILG--------IDHKAQVQKANAFLKRLDAGIE-ADTMVE 148
Cdd:PRK11308 83 DPEAQKLlrQKIQIVFQ--NPYGSLN------PRKKV-GQILEepllintsLSAAERREKALAMMAKVGLRPEhYDRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 149 DLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA---AEVEILFkviAELKAQ-GVAIVYISHRLEELMRIGDYITVLRD 224
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVsvqAQVLNLM---MDLQQElGLSYVFISHDLSVVEHIADEVMVMYL 230
|
...
gi 499968440 225 GQV 227
Cdd:PRK11308 231 GRC 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
278-488 |
2.76e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLAlipedR--QREGL 355
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV-----RtfQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASNLTLA-----SLGRFTRLFHID--RGAEKSAIRDA--------IRDLSIKapnpdfEVTSMSGGNQQKVVIG 420
Cdd:PRK11300 92 FREMTVIENLLVAqhqqlKTGLFSGLLKTPafRRAESEALDRAatwlervgLLEHANR------QAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 421 KALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-241 |
2.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAN---GIGMIFQ--ELNLFANMSVAE 106
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkKVSLVFQfpEAQLFENTVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 107 NIFARREitrgiLGIDHKAQVQKANAFLKRLdaGIEADTMVE---DLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAA 183
Cdd:PRK13641 107 VEFGPKN-----FGFSEDEAKEKALKWLKKV--GLSEDLISKspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 184 EVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI--DTRWI 241
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIfsDKEWL 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-231 |
4.42e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 33 LELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSPAHAQ--ANGIGMIFQELNLFANMSVAENIf 109
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqMDEEARAKlrAKHVGFVFQSFMLIPTLNALENV- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 110 arrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILF 189
Cdd:PRK10584 110 ---ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 190 KVIAEL-KAQGVAIVYISHRLEELMRIGDYITvLRDGQVTGEA 231
Cdd:PRK10584 187 DLLFSLnREHGTTLILVTHDLQLAARCDRRLR-LVNGQLQEEA 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
282-485 |
4.47e-15 |
|
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: 73.19 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRaRDTTRRIRRGLALIPEDrqreglvqvlsi 361
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIAYVPQD------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 asnltlaslgrfTRLFHidrgaekSAIRDAIrdlsikapnpdfevtsMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03228 85 ------------PFLFS-------GTIRENI----------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499968440 442 GAKADVFRTMRRLaANGLAILFSTSDLEEVMaLSDRIAVLSNGQ 485
Cdd:cd03228 130 ETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
281-487 |
4.54e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT--RRIRRGLALIPEDrqreglvqv 358
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewRAVRSDIQMIFQD--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 lsiasnlTLASLG-RFT---------RLFHIDrgAEKSAIRDAIRDLSIKA---PN-----P-DFevtsmSGGNQQKVVI 419
Cdd:PRK15079 107 -------PLASLNpRMTigeiiaeplRTYHPK--LSRQEVKDRVKAMMLKVgllPNlinryPhEF-----SGGQCQRIGI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
285-486 |
4.92e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR-ARDTT-----------RRIRRGLALIPE---- 348
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlVRDKDgqlkvadknqlRLLRTRLTMVFQhfnl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 -------DRQREGLVQVLSIASnltlaSLGRFTRLFHIDrgaeKSAIRDAIRDlsiKAPnpdfevTSMSGGNQQKVVIGK 421
Cdd:PRK10619 104 wshmtvlENVMEAPIQVLGLSK-----QEARERAVKYLA----KVGIDERAQG---KYP------VHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 422 ALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-227 |
4.96e-15 |
|
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: 77.42 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSG-----------IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVErPTLGRIILDGKPVSF 78
Cdd:COG4172 273 PPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 79 DSPAHAQA--NGIGMIFQE----LNlfANMSVAEnIfarreITRGIL----GIDHKAQVQKANAFLKrlDAGIEADTMvE 148
Cdd:COG4172 352 LSRRALRPlrRRMQVVFQDpfgsLS--PRMTVGQ-I-----IAEGLRvhgpGLSAAERRARVAEALE--EVGLDPAAR-H 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 149 DLPI----GQQQLVEIAKAMSLNARILIMDEPTSALsaaEVEILFKVIAELKA----QGVAIVYISHRLEELMRIGDYIT 220
Cdd:COG4172 421 RYPHefsgGQRQRIAIARALILEPKLLVLDEPTSAL---DVSVQAQILDLLRDlqreHGLAYLFISHDLAVVRALAHRVM 497
|
....*..
gi 499968440 221 VLRDGQV 227
Cdd:COG4172 498 VMKDGKV 504
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-227 |
6.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 26 VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDG-----KPVSFDSPAHAqangIGMIFQ--ELNL 98
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIRKK----VGLVFQypEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 99 FANmSVAENIfARREITRGILGIDHKAQVQKANAFLKrLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTS 178
Cdd:PRK13637 97 FEE-TIEKDI-AFGPINLGLSEEEIENRVKRAMNIVG-LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 179 ALS-AAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK13637 174 GLDpKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
273-494 |
7.45e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.54 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 273 LPRPTGGL-SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT--RRIRRGLALIPED 349
Cdd:COG4608 24 FGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelRPLRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 -------RQREGlvqvlsiasnltlASLGRFTRLFHIDRGAEKsaiRDAIRD-LSIKAPNPDF------EVtsmSGGNQQ 415
Cdd:COG4608 104 pyaslnpRMTVG-------------DIIAEPLRIHGLASKAER---RERVAElLELVGLRPEHadryphEF---SGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 416 KVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
278-487 |
7.77e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.87 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT-RRIRRGLA-------LIPE 348
Cdd:COG1126 12 GDLEVlKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVGmvfqqfnLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 drqreglvqvLSIASNLTLASLgrftRLFHIDRgaeKSAIRDAIR-----DLSIKA---PNpdfevtSMSGGNQQKVVIG 420
Cdd:COG1126 92 ----------LTVLENVTLAPI----KVKKMSK---AEAEERAMEllervGLADKAdayPA------QLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 421 KALMTNPKVLLMDEPSRGID---VGakaDVFRTMRRLAANGLAILFSTSDLE---EVmalSDRIAVLSNGQLV 487
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGRIV 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
269-487 |
7.89e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.61 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVN---DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT--RRIRRGL 343
Cdd:PRK11153 5 KNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALIpedRQREGLVQVLSIASN----LTLAslgrftrlfhidrGAEKSAIRD------AIRDLSIKApnpDFEVTSMSGGN 413
Cdd:PRK11153 85 GMI---FQHFNLLSSRTVFDNvalpLELA-------------GTPKAEIKArvtellELVGLSDKA---DRYPAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 414 QQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTM----RRLaanGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdinREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-239 |
2.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQaNGIGMIFQEL-NLFANMSVAENIFARREITrgilGI 121
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR-HKIGMVFQNPdNQFVGATVEDDVAFGLENK----GI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 122 DHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GV 200
Cdd:PRK13650 113 PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQM 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 499968440 201 AIVYISHRLEELMrIGDYITVLRDGQVTGEAMVRDIDTR 239
Cdd:PRK13650 193 TVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-227 |
4.09e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.00 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 16 DDVSKVYSGIV-AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDG---KPVSFDSPAHAqangIGM 91
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRN----IAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFaNMSVAENIFARR------EITRGilgidhkAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIA 161
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGRpdatdeEMRAA-------AERAQAHDFIERKPDGY--DTVVGErgrqLSGGERQRLAIA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 162 KAMSLNARILIMDEPTSALSaAEVEIlfKVIAELKA--QGVAIVYISHRLEELmRIGDYITVLRDGQV 227
Cdd:PRK13657 484 RALLKDPPILILDEATSALD-VETEA--KVKAALDElmKGRTTFIIAHRLSTV-RNADRILVFDNGRV 547
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
283-484 |
4.26e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGK---HVRARDttRRIrrGLALipedrQREGLVQVL 359
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARD--RKV--GFVF-----QHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLT--LASLGRFTRLfhidrgaEKSAIRDAIRDL---------SIKAPnpdfevTSMSGGNQQKVVIGKALMTNPK 428
Cdd:PRK10851 90 TVFDNIAfgLTVLPRRERP-------NAAAIKAKVTQLlemvqlahlADRYP------AQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 429 VLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNG 484
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-227 |
4.26e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVY-SGIVAVKRANLEL-RRGAVnVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdSPAHAQ-ANGIGM 91
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS--SLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANmSVAENIFARREITrgilgiDHK-----AQVQKAnAFLKRLDAGIEadTMV----EDLPIGQQQLVEIAK 162
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDIS------EEQvwqalETVQLA-ELARSLPDGLY--TPLgeqgNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 163 AMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVyISHRLEELMRiGDYITVLRDGQV 227
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV-IAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-218 |
4.39e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.13 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMIFQELNLFANMSVAEN 107
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ--LCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 108 IFARREITRGILGIDHKAQVQKANAFLkrldagieaDTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEI 187
Cdd:PRK13540 95 CLYDIHFSPGAVGITELCRLFSLEHLI---------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180 190
....*....|....*....|....*....|.
gi 499968440 188 LFKVIAELKAQGVAIVYISHRLEELMRiGDY 218
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQDLPLNK-ADY 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
43-227 |
4.76e-14 |
|
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: 74.86 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPA--HAQangIGMIFQELNLFaNMSVAENI-FARREITRgil 119
Cdd:COG5265 389 IVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAA---IGIVPQDTVLF-NDTIAYNIaYGRPDASE--- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 120 gidhkAQVQKAnAFLKRLDAGIEA-----DTMVED----LPIGQQQLVEIAKAMSLNARILIMDEPTSAL-SAAEVEILf 189
Cdd:COG5265 462 -----EEVEAA-ARAAQIHDFIESlpdgyDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALdSRTERAIQ- 534
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499968440 190 kviAELK--AQGVAIVYISHRLEELMRiGDYITVLRDGQV 227
Cdd:COG5265 535 ---AALRevARGRTTLVIAHRLSTIVD-ADEILVLEAGRI 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
43-227 |
5.23e-14 |
|
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: 71.37 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANmSVAENIFARREITRG-ILGI 121
Cdd:cd03244 35 IVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQDPVLFSG-TIRSNLDPFGEYSDEeLWQA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 122 DHKAQVQKA-NAFLKRLDAGIEADTmvEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAElKAQGV 200
Cdd:cd03244 113 LERVGLKEFvESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDC 189
|
170 180
....*....|....*....|....*....
gi 499968440 201 AIVYISHRLEELMrigDY--ITVLRDGQV 227
Cdd:cd03244 190 TVLTIAHRLDTII---DSdrILVLDKGRV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
281-487 |
6.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDG-----KHVRARDttrrIRRGLALI---PEDRQR 352
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSD----IRKKVGLVfqyPEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 353 EGLVQVlSIA---SNLTLASLGRFTRLFHIDR--GAEKSAIRDairdlsiKAPnpdFEvtsMSGGNQQKVVIGKALMTNP 427
Cdd:PRK13637 98 EETIEK-DIAfgpINLGLSEEEIENRVKRAMNivGLDYEDYKD-------KSP---FE---LSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
285-488 |
7.84e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHStGKIFIDGKHVRARDTtrrirRGLAlipedRQREGLVQVLSIASN 364
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSA-----AELA-----RHRAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 365 ------LTLaslgrftrlfHIDRGAEKSAIRDAIRD------LSIKAPNPdfeVTSMSGGNQQKVVIGKALM-----TNP 427
Cdd:PRK03695 84 mpvfqyLTL----------HQPDKTRTEAVASALNEvaealgLDDKLGRS---VNQLSGGEWQRVRLAAVVLqvwpdINP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 428 --KVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-218 |
1.07e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMK-------IIAG--VErptlGRIILDGKPVsFDS 80
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGfrVE----GKVTFHGKNL-YAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 ---PAHAQANgIGMIFQELNLFANmSVAENI-FARReitrgILGI--DHKAQVQKAnafLKRLDAGIEADTMVED----L 150
Cdd:PRK14243 83 dvdPVEVRRR-IGMVFQKPNPFPK-SIYDNIaYGAR-----INGYkgDMDELVERS---LRQAALWDEVKDKLKQsglsL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 151 PIGQQQLVEIAKAMSLNARILIMDEPTSAL---SAAEVEILFKviaELKAQgVAIVYISHRLEELMRIGDY 218
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALdpiSTLRIEELMH---ELKEQ-YTIIIVTHNMQQAARVSDM 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
264-487 |
1.24e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 264 EVFRAENISL--PRPTgglsVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIG------RHTHstGKIFIDGKHVRARDt 335
Cdd:PRK10418 3 QQIELRNIALqaAQPL----VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGilpagvRQTA--GRVLLDGKPVAPCA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 336 trrIR-RGLALIPEDrQREGLVQVLSIASNL--TLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKApnpdFEvtsMSGG 412
Cdd:PRK10418 76 ---LRgRKIATIMQN-PRSAFNPLHTMHTHAreTCLALGKPADDATLTAALEAVGLENAARVLKLYP----FE---MSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 413 NQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAA-NGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
269-504 |
1.31e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdTTRRIRRGLALI-- 346
Cdd:PRK13647 8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE-NEKWVRSKVGLVfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 -PEDrqreglvQVLS--IASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIGKAL 423
Cdd:PRK13647 87 dPDD-------QVFSstVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPY------HLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNEATEEAIIAA 503
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
.
gi 499968440 504 S 504
Cdd:PRK13647 234 A 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-227 |
1.37e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 22 YSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVeRPTLGRIILDGKPVSFDSPAHAQANgIGMIFQELNLFAN 101
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 102 mSVAENI-FARREITRGILgidhKAQVQKANA--FLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSLNARILIMD 174
Cdd:PRK11174 438 -TLRDNVlLGNPDASDEQL----QQALENAWVseFLPLLPQGL--DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 175 EPTSALSAAEVEilfKVIAELK--AQGVAIVYISHRLEELMRIgDYITVLRDGQV 227
Cdd:PRK11174 511 EPTASLDAHSEQ---LVMQALNaaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-228 |
1.39e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVeRPTLGRIILDGKPVSfDSPAHAQAN-----------GIGM-IFQELNLF 99
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLE-AWSAAELARhraylsqqqtpPFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 100 --ANMSVAENIFARREITRgILGIDHKaqvqkanafLKRldagieadtMVEDLPIGQQQLVEIAKAM-----SLN--ARI 170
Cdd:PRK03695 94 qpDKTRTEAVASALNEVAE-ALGLDDK---------LGR---------SVNQLSGGEWQRVRLAAVVlqvwpDINpaGQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 171 LIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-487 |
1.53e-13 |
|
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: 69.83 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDG---KHVRARDttrrIRRGLALIPEDrq 351
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGLHD----LRSRISIIPQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 352 reglVQVLS--IASNltLASLGRFT--RLFHIdrgAEKSAIRDAIRDLSIKApnpDFEVTS----MSGGNQQKVVIGKAL 423
Cdd:cd03244 87 ----PVLFSgtIRSN--LDPFGEYSdeELWQA---LERVGLKEFVESLPGGL---DTVVEEggenLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRlAANGLAILFSTSDLEEVMAlSDRIAVLSNGQLV 487
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-227 |
1.61e-13 |
|
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: 69.12 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAG-VERPTL-GRIILDGKPVSFDSPAHAqangIGMIFQELNLFANMSVA 105
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 106 ENI-FARReiTRGILGidhkaqvqkanaflkrldagieadtmvedlpiGQQQLVEIAKAMSLNARILIMDEPTSALSAAE 184
Cdd:cd03213 101 ETLmFAAK--LRGLSG--------------------------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499968440 185 VEILFKVIAELKAQGVAIVYISHRL-EELMRIGDYITVLRDGQV 227
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-226 |
1.74e-13 |
|
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: 67.86 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIldgkpvsfdspaHAQANGIGmi 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------WGSTVKIG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 fqelnLFANMSvaenifarreitrGilgidhkaqvqkanaflkrldagieadtmvedlpiGQQQLVEIAKAMSLNARILI 172
Cdd:cd03221 67 -----YFEQLS-------------G-----------------------------------GEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499968440 173 MDEPTSALSAAEVEILfkvIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:cd03221 94 LDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
267-481 |
2.16e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 72.32 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRiRRGLALI 346
Cdd:TIGR02857 323 EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PedrQREGLVQVlSIASNLTLAslgrftrlfhiDRGAEKSAIRDAIR-----DLSIKAPNP-DFEV----TSMSGGNQQK 416
Cdd:TIGR02857 402 P---QHPFLFAG-TIAENIRLA-----------RPDASDAEIREALEragldEFVAALPQGlDTPIgeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLaANGLAILFSTSDLeEVMALSDRIAVL 481
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
268-499 |
2.52e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 268 AENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtrrirrglALIp 347
Cdd:PRK13639 4 TRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKK--------SLL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 348 EDRQREGLV------QVL--SIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVI 419
Cdd:PRK13639 75 EVRKTVGIVfqnpddQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA------VFDRN 493
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkeVFSDI 228
|
....*.
gi 499968440 494 EATEEA 499
Cdd:PRK13639 229 ETIRKA 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
267-491 |
2.62e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGG---LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtrriRRGL 343
Cdd:COG4525 5 TVRHVSVRYPGGGqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----DRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALipedrQREGLVQVLSIASNLTLAslgrfTRLfhidRGAEKSAIRDAIRDLSIKAPNPDFE---VTSMSGGNQQKVVIG 420
Cdd:COG4525 81 VF-----QKDALLPWLNVLDNVAFG-----LRL----RGVPKAERRARAEELLALVGLADFArrrIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 421 KALMTNPKVLLMDEPsrgidVGAkADVF--RTMRRL-----AANGLAILFSTSDLEEVMALSDRIAVLSN--GQLVAVFD 491
Cdd:COG4525 147 RALAADPRFLLMDEP-----FGA-LDALtrEQMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLE 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
280-489 |
2.79e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.60 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR--ARDTTRRIRRglalipedRQREGLVQ 357
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRR--------KKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTLASLGRF-TRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEvTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK10070 114 SFALMPHMTVLDNTAFgMELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499968440 437 RGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-227 |
3.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILrlDDVSKVYSG-----IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDgkpvSFDSPAHA 84
Cdd:PRK13645 6 DIIL--DNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG----DYAIPANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QA--------NGIGMIFQ--ELNLFAnmsvaENIfaRREITRGI--LGIDHKAQVQKANAFLKRLDAGIE-ADTMVEDLP 151
Cdd:PRK13645 80 KKikevkrlrKEIGLVFQfpEYQLFQ-----ETI--EKDIAFGPvnLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 152 IGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
282-481 |
3.37e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIfidgkhvrARDTTRRIrrglalipedrqreGLV-QVLS 360
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLRI--------------GYVpQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLaSLGRFTRLfhiDRGAEKSAIRDAIRDLSiKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK09544 78 LDTTLPL-TVNRFLRL---RPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499968440 441 VGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVL 481
Cdd:PRK09544 153 VNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-228 |
3.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVY-SGIVAVKRA----NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAN-- 87
Cdd:PRK13649 5 LQNVSYTYqAGTPFEGRAlfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 -GIGMIFQ--ELNLFANMSVAENIFARREitrgiLGIDHKAQVQKANAFLKRLdaGIEADTMVE---DLPIGQQQLVEIA 161
Cdd:PRK13649 85 kKVGLVFQfpESQLFEETVLKDVAFGPQN-----FGVSQEEAEALAREKLALV--GISESLFEKnpfELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 162 KAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-236 |
3.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.15 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDS------PAHAQangIGMIFQ--ELNLFANMS 103
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKK---VGVVFQfpESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 104 VAENIFARREitrgiLGIDhKAQVQKANAflKRLDAGIEADTMVEDLPI----GQQQLVEIAKAMSLNARILIMDEPTSA 179
Cdd:PRK13643 103 LKDVAFGPQN-----FGIP-KEKAEKIAA--EKLEMVGLADEFWEKSPFelsgGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 180 LS-AAEVEILfKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK13643 175 LDpKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-231 |
3.77e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 22 YSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLG-----RIILDGKPVSFDSPAHAQANGIGMIFQEL 96
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 97 NLFAnMSVAENIFA---------RREItRGIlgidhkaqvqkANAFLKRLDAGIEADTMVEDLPI----GQQQLVEIAKA 163
Cdd:PRK14271 111 NPFP-MSIMDNVLAgvrahklvpRKEF-RGV-----------AQARLTEVGLWDAVKDRLSDSPFrlsgGQQQLLCLART 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 164 MSLNARILIMDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEA 231
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
282-491 |
4.48e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTT--RRIRRGLALIPedrQREGLvqvL 359
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAARRKIGMIF---QHFNL---L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 S-------IASNLTLAslgrftrlfhidrGAEKSAIRDAIRD------LSIKAPN-PDfevtSMSGGNQQKVVIGKALMT 425
Cdd:COG1135 95 SsrtvaenVALPLEIA-------------GVPKAEIRKRVAEllelvgLSDKADAyPS----QLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLaaN---GLAILFSTSDLEEVMALSDRIAVLSNGQLV---AVFD 491
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDI--NrelGLTIVLITHEMDVVRRICDRVAVLENGRIVeqgPVLD 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
281-486 |
4.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.38 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkHVRARDTTRRIRR--GLALIPEDRQREGLVQV 358
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHkiGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 LSIAsnLTLASLGrftrlfhIDRGAEKSAIRDAIRDLSIKapnpDF---EVTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:PRK13650 101 DDVA--FGLENKG-------IPHEEMKERVNEALELVGMQ----DFkerEPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 436 SRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVmALSDRIAVLSNGQL 486
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-236 |
5.70e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 14 RLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIF 93
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 QELNLFANMSVAENI-FARREITRGILGIDHKAQVQKANAFLKRLDAgieADTMVEDLPIGQQQLVEIAKAMSLNARILI 172
Cdd:COG4604 82 QENHINSRLTVRELVaFGRFPYSKGRLTAEDREIIDEAIAYLDLEDL---ADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 173 MDEPTSAL----SAAEVEILFKVIAELkaqGVAIVYISHRLEELMRIGDYITVLRDGQV-----TGEAMVRDI 236
Cdd:COG4604 159 LDEPLNNLdmkhSVQMMKLLRRLADEL---GKTVVIVLHDINFASCYADHIVAMKDGRVvaqgtPEEIITPEV 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
268-487 |
8.61e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 268 AENISLPRPTGGLS--------VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR- 338
Cdd:PRK10419 6 VSGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 339 -IRRGLALIPED-------RQREGlvqvlsiasnltlASLGRFTR-LFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVTSM 409
Cdd:PRK10419 86 aFRRDIQMVFQDsisavnpRKTVR-------------EIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 410 SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-222 |
1.04e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 6 AQKDDVILRLDDVsKVYSGIV--------------AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIL 71
Cdd:PRK15079 2 TEGKKVLLEVADL-KVHFDIKdgkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 72 DGKPVS--FDSPAHAQANGIGMIFQE----LNlfANMSVAENIFARREITRGILgidHKAQV-QKANAFLKRLdaGIEAD 144
Cdd:PRK15079 81 LGKDLLgmKDDEWRAVRSDIQMIFQDplasLN--PRMTIGEIIAEPLRTYHPKL---SRQEVkDRVKAMMLKV--GLLPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 145 tMVEDLPI----GQQQLVEIAKAMSLNARILIMDEPTSALsaaEVEILFKVIAELKA----QGVAIVYISHRLEELMRIG 216
Cdd:PRK15079 154 -LINRYPHefsgGQCQRIGIARALILEPKLIICDEPVSAL---DVSIQAQVVNLLQQlqreMGLSLIFIAHDLAVVKHIS 229
|
....*.
gi 499968440 217 DYITVL 222
Cdd:PRK15079 230 DRVLVM 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
408-488 |
1.04e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
..
gi 499968440 487 VA 488
Cdd:PRK11144 208 KA 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
284-492 |
1.11e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.05 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDtTRRIRRGLALIPEDrqreglvQVL---S 360
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQD-------PTLfsgT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLtlaslgrftrlfhiDRGAEKSAiRDAIRDLSIKAPNPDFevtsmSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:cd03369 98 IRSNL--------------DPFDEYSD-EEIYGALRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 441 VGAKADVFRTMRRLAANGlAILFSTSDLEEVmALSDRIAVLSNGQlVAVFDR 492
Cdd:cd03369 158 YATDALIQKTIREEFTNS-TILTIAHRLRTI-IDYDKILVMDAGE-VKEYDH 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-484 |
1.18e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.81 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 277 TGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRArdTTRRIRRGLALIPedrQREGLV 356
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--NISDVHQNMGYCP---QFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSIASNLTLaslgrFTRLfhidRGAEKSAIrDAIRDLSIKAPN----PDFEVTSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:TIGR01257 2025 DLLTGREHLYL-----YARL----RGVPAEEI-EKVANWSIQSLGlslyADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499968440 433 DEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNG 484
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
285-499 |
1.32e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKhvrARDTTRR----IRRGLALIPEDRQREGLVQVLS 360
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRgllaLRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLASLG----RFTRlfhidRGAEKSAIRDA--IRDLSIKApnpdfevtsMSGGNQQKVVIGKALMTNPKVLLMDE 434
Cdd:PRK13638 97 SDIAFSLRNLGvpeaEITR-----RVDEALTLVDAqhFRHQPIQC---------LSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 435 PSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA------VFDRNEATEEA 499
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILThgapgeVFACTEAMEQA 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-211 |
1.55e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIV--AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfdspahaqANGI 89
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIFARRE---ITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREhlyLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEE 211
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEE 2132
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
264-506 |
1.77e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 67.73 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 264 EVFRAENISLPRP-TGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKhVRARDTTRRIRR- 341
Cdd:PRK13635 4 EIIRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEETVWDVRRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 342 -GLALIPEDRQREGLVQVLSIAsnLTLASLGrFTRLFHIDRgaeksaIRDAIRDLSIKapnpDF---EVTSMSGGNQQKV 417
Cdd:PRK13635 83 vGMVFQNPDNQFVGATVQDDVA--FGLENIG-VPREEMVER------VDQALRQVGME----DFlnrEPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 418 VIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFS-TSDLEEVmALSDRIAVLSNGQLVAvfdrnEAT 496
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILE-----EGT 223
|
250
....*....|
gi 499968440 497 EEAIIAASAK 506
Cdd:PRK13635 224 PEEIFKSGHM 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
265-502 |
1.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 265 VFRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRR--G 342
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 343 LALIPEDRQREGLVQVLSIA---SNLTLASLGRFTRlfhIDRGAEKSAIrDAIRDLSIKapnpdfevtSMSGGNQQKVVI 419
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAfgpENLCLPPIEIRKR---VDRALAEIGL-EKYRHRSPK---------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMAlSDRIAVLSNGQLVAvfdrnEATEEA 499
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVL-----EGEPEN 221
|
...
gi 499968440 500 IIA 502
Cdd:PRK13644 222 VLS 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
282-485 |
2.00e-12 |
|
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: 66.69 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR---ARDTTRRIrrgLALipedRQRE-GLV- 356
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlAQASPREI---LAL----RRRTiGYVs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSI-----ASNLTLASLgrftrlfhIDRGAEKSAIRDAIRD----LSIK------APnpdfevTSMSGGNQQKVVIGK 421
Cdd:COG4778 100 QFLRViprvsALDVVAEPL--------LERGVDREEARARAREllarLNLPerlwdlPP------ATFSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 422 ALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
295-488 |
2.02e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 295 LGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALI---PEDrqreglvQVLSIASNLTLA--- 368
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENIREVRKFVGLVfqnPDD-------QIFSPTVEQDIAfgp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 369 -SLGrftrlfhIDRGAEKSAIRDAIRDLSI-----KAPNpdfevtSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVG 442
Cdd:PRK13652 105 iNLG-------LDEETVAHRVSSALHMLGLeelrdRVPH------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 443 AKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK13652 172 GVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
267-487 |
2.08e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.44 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkHVRARDTTRRI---RRGL 343
Cdd:PRK10908 3 RFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG-HDITRLKNREVpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALIPEDRQregLVQVLSIASNLTL------ASLGRFTRlfHIDRGAEKSAIRDAIRDLSIKapnpdfevtsMSGGNQQKV 417
Cdd:PRK10908 82 GMIFQDHH---LLMDRTVYDNVAIpliiagASGDDIRR--RVSAALDKVGLLDKAKNFPIQ----------LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 418 VIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
286-488 |
2.43e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 286 SLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrardttrrirrgLALIPEDR------QREGLVQVL 359
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL------------TALPPAERpvsmlfQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLA---SLgRFTRlfhidrgAEKSAIRDAIRDLSIKA-----PNpdfevtSMSGGNQQKVVIGKALMTNPKVLL 431
Cdd:COG3840 87 TVAQNIGLGlrpGL-KLTA-------EQRAQVEQALERVGLAGlldrlPG------QLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
276-487 |
2.62e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.18 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 276 PTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR-ARDTTRRIRRGLALIPEDRQReg 354
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRESVGMVFQDPDN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 lvQVLSiASNLTLASLGRftrlfhIDRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLL 431
Cdd:PRK13636 94 --QLFS-ASVYQDVSFGA------VNLKLPEDEVRKRVDNALKRtgiEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-207 |
2.92e-12 |
|
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: 69.06 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMIFQELNLFANM----SVAEN 107
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL-FSAVFSDFHLFDRLlgldGEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 108 IFARREITRgiLGIDHKAQVQKaNAFL---------KRLdAGIEAdtMVEDLPIgqqqlveiakamslnariLIMDEpts 178
Cdd:COG4615 431 ARARELLER--LELDHKVSVED-GRFSttdlsqgqrKRL-ALLVA--LLEDRPI------------------LVFDE--- 483
|
170 180 190
....*....|....*....|....*....|....*
gi 499968440 179 alSAAEVEILFK------VIAELKAQGVAIVYISH 207
Cdd:COG4615 484 --WAADQDPEFRrvfyteLLPELKARGKTVIAISH 516
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-502 |
3.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR-ARDTTR----RIRRGLALIpedRQREGLV 356
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDIFQidaiKLRKEVGMV---FQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSIASNLTLASLGRFTRlfhiDRGAEKSAIRDAIRDLSIKAPNPD---FEVTSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIK----EKREIKKIVEECLRKVGLWKEVYDrlnSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 434 EPSRGIDVGAKADVFRTMRRLaANGLAILFSTSDLEEVMALSDRIAVLSNGQLV------AVFD--RNEATEEAIIA 502
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVewgssnEIFTspKNELTEKYVIG 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
266-488 |
3.49e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLPRPtGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFEcVIGRH-THSTGKIFIDGKHVRARDTtRRIRRGLA 344
Cdd:PRK10575 12 FALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHqPPSEGEILLDAQPLESWSS-KAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 345 LIPED-RQREGLV--QVLSIASNLTLASLGRFTRlfhidrgAEKSAIRDAIRDLSIKaPNPDFEVTSMSGGNQQKVVIGK 421
Cdd:PRK10575 89 YLPQQlPAAEGMTvrELVAIGRYPWHGALGRFGA-------ADREKVEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 422 ALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLA-ANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-227 |
3.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 22 YSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKI---------IAGVErptlGRIILDGKPV-SFDSPAHAQANGIGM 91
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneEARVE----GEVRLFGRNIySPDVDPIEVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIfarreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVED-----------LPIGQQQLVEI 160
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNV---------AIGVKLNGLVKSKKELDERVEWALKKAALWDEvkdrlndypsnLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 161 AKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQgVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
264-488 |
3.60e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.33 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 264 EVFRAENISLPRptGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRg 342
Cdd:PRK13548 1 AMLEARNLSVRL--GGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 343 LAlipedrqreglvqVLSIASNLTLA-------SLGRFTRLFHIDRGAEksAIRDAIR--DLSikapnpDFE---VTSMS 410
Cdd:PRK13548 78 RA-------------VLPQHSSLSFPftveevvAMGRAPHGLSRAEDDA--LVAAALAqvDLA------HLAgrdYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 411 GGNQQKVVIGKALM------TNPKVLLMDEPSRGIDVGAKADVFRTMRRLA-ANGLAILFSTSDLEEVMALSDRIAVLSN 483
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
....*
gi 499968440 484 GQLVA 488
Cdd:PRK13548 217 GRLVA 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
282-488 |
3.91e-12 |
|
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: 66.20 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhVRARDTTRRIRRGLALIPEdrQREGLVQVLSI 361
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVVFG--QKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgrFTRLFHIDRgAEKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03267 113 IDSFYL-----LAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 442 GAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:cd03267 187 VAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
282-481 |
3.98e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.95 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIfidgkhvrardtTRRIRRGLALIPedrQREGLVQVLSI 361
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVP---QRSEVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 aSNLTLASLGRFTR--LFHIDRGAEKSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:NF040873 73 -TVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGLA----DLAgrqLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 437 RGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMAlSDRIAVL 481
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
267-487 |
6.95e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLsVNDVSLSVKAGEILGIYGLMGAGRSEFFECvIGRHTHSTGKIFIDGKH-------VRARDTTRRI 339
Cdd:PRK14258 9 KVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVeffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 340 RRGLALIpedRQREGLVQvLSIASNLT--LASLGRFTRLfHIDrGAEKSAIRDAirDLSIKAPNPDFE-VTSMSGGNQQK 416
Cdd:PRK14258 87 RRQVSMV---HPKPNLFP-MSVYDNVAygVKIVGWRPKL-EID-DIVESALKDA--DLWDEIKHKIHKsALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANG-LAILFSTSDLEEVMALSDRIAVLSN-----GQLV 487
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLV 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-454 |
7.47e-12 |
|
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: 67.65 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAV-KRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPtlgriildgkpvsFDSPAHAQAN-GI 89
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD-------------FNGEARPQPGiKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQELNLFANMSVAENIFARREITRGILG-------------------IDHKAQVQ------KANAFLKRLDAGIEA- 143
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaepdadfdklAAEQAELQeiidaaDAWDLDSQLEIAMDAl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 144 -----DTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLE-------E 211
Cdd:TIGR03719 151 rcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDnvagwilE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 212 LMR------IGDYITVL-----------RDGQVTGEAMVRDIDtrWIVRSMIGSDAK--------------DFAKSVDHA 260
Cdd:TIGR03719 231 LDRgrgipwEGNYSSWLeqkqkrleqeeKEESARQKTLKRELE--WVRQSPKGRQAKskarlaryeellsqEFQKRNETA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 261 ---------VGAEVFRAENISlpRPTGG-LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIdGKHV 330
Cdd:TIGR03719 309 eiyippgprLGDKVIEAENLT--KAFGDkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 331 RardttrrirrgLALIpeDRQREGLvqvlsiASNLTL---ASLGrftrLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEVT 407
Cdd:TIGR03719 386 K-----------LAYV--DQSRDAL------DPNKTVweeISGG----LDIIKLGKREIPSRAYVGRFNFKGSDQQKKVG 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVgakadvfRTMRRL 454
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV-------ETLRAL 482
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
267-494 |
8.07e-12 |
|
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: 67.47 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 267 RAENISLPRPTGGLSV---------------NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVR 331
Cdd:COG4618 318 EPERMPLPRPKGRLSVenltvvppgskrpilRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 332 ARDTtRRIRRGLALIPEDrqreglVQVL--SIASNLtlaslGRFTRlfhID-----RGAEKSAIRDAIRDLsikapnP-- 402
Cdd:COG4618 398 QWDR-EELGRHIGYLPQD------VELFdgTIAENI-----ARFGD---ADpekvvAAAKLAGVHEMILRL------Pdg 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 403 -DFEV----TSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLeEVMALSDR 477
Cdd:COG4618 457 yDTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDK 535
|
250
....*....|....*..
gi 499968440 478 IAVLSNGQLVAVFDRNE 494
Cdd:COG4618 536 LLVLRDGRVQAFGPRDE 552
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-209 |
8.70e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 67.39 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSG-IVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQAN 87
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 88 GIGMIFQELNLFANmSVAENI-FARREITRGILGiDHKAQVQKANaFLKRLDAGIEADtMVED---LPIGQQQLVEIAKA 163
Cdd:TIGR02868 410 RVSVCAQDAHLFDT-TVRENLrLARPDATDEELW-AALERVGLAD-WLRALPDGLDTV-LGEGgarLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 164 MSLNARILIMDEPTSALSA-AEVEILFKVIAELkaQGVAIVYISHRL 209
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAeTADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
282-485 |
8.81e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhvraRDTTRrirrglaLIPEDR------QREGL 355
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-----QDITH-------VPAENRhvntvfQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASNLTLAslgrfTRLFHIDRGAEKSAIRDAIR-----DLSIKAPnpdfevTSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:PRK09452 98 FPHMTVFENVAFG-----LRMQKTPAAEITPRVMEALRmvqleEFAQRKP------HQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 431 LMDEPSRGIDVGAKadvfRTM--------RRLaanGLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:PRK09452 167 LLDESLSALDYKLR----KQMqnelkalqRKL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-236 |
8.89e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 1 MTTAEAQKDDVILRLDDVSKVYS---GIV-AVKRANLELRRGAVNVLVGENGAGKS----TLMKIIAGVERPTlGRIILD 72
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFStpdGDVtAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 73 GKPVsFDSPAHA----QANGIGMIFQE----LNLFanMSVAENIFarrEITrgilgIDHKAqVQKANAF---LKRLDA-- 139
Cdd:PRK09473 80 GREI-LNLPEKElnklRAEQISMIFQDpmtsLNPY--MRVGEQLM---EVL-----MLHKG-MSKAEAFeesVRMLDAvk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 140 GIEADTMVEDLPI----GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMR 214
Cdd:PRK09473 148 MPEARKRMKMYPHefsgGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAG 227
|
250 260
....*....|....*....|..
gi 499968440 215 IGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK09473 228 ICDKVLVMYAGRTMEYGNARDV 249
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
265-488 |
9.24e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 265 VFRAENISLPRpTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHS--------TGKIFIDGKHVRARDTT 336
Cdd:PRK13547 1 MLTADHLHVAR-RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 337 RRIRRgLALIPEDRQREGLVQVLSIASnltlasLGRFTrlfHIDRGAEKS----AIRDAIRDLSIKAPNPDFEVTSMSGG 412
Cdd:PRK13547 80 RLARL-RAVLPQAAQPAFAFSAREIVL------LGRYP---HARRAGALThrdgEIAWQALALAGATALVGRDVTTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 413 NQQKVVIGKAL---------MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLS 482
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLA 229
|
....*.
gi 499968440 483 NGQLVA 488
Cdd:PRK13547 230 DGAIVA 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
28-231 |
1.03e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGveRP----TLGRIILDGKPV-SFDSPAHAQAnGIGMIFQ---ELNLF 99
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESIlDLEPEERAHL-GIFLAFQypiEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 100 ANMSVAENIFARREITRGILGID---------HKAQVQKANA-FLKRldagieadTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:CHL00131 100 SNADFLRLAYNSKRKFQGLPELDplefleiinEKLKLVGMDPsFLSR--------NVNEGFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISH--RLEELMrIGDYITVLRDGQV--TGEA 231
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYI-KPDYVHVMQNGKIikTGDA 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-480 |
1.10e-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: 67.12 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 35 LRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIildGKPVSFDspahaqangigmifQELNLFANmSVAENIFarREI 114
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWD--------------EVLKRFRG-TELQDYF--KKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 115 TRGILGIDHKAQ-VQ--------KANAFLKRLDAGIEADTMVEDLPI-------------GQQQLVEIAKAMSLNARILI 172
Cdd:COG1245 156 ANGEIKVAHKPQyVDlipkvfkgTVRELLEKVDERGKLDELAEKLGLenildrdiselsgGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 173 MDEPTSAL------SAAeveilfKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRD-----GQVTGEAMVRD-IDTrW 240
Cdd:COG1245 236 FDEPSSYLdiyqrlNVA------RLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGepgvyGVVSKPKSVRVgINQ-Y 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 241 I--------VRsmIGSDAKDFAKsvdHAVGAEVFRAENISLPRPTggLSVNDVSLSVKAG-----EILGIYGLMGAGRSE 307
Cdd:COG1245 309 LdgylpeenVR--IRDEPIEFEV---HAPRREKEEETLVEYPDLT--KSYGGFSLEVEGGeiregEVLGIVGPNGIGKTT 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 308 FFECVIGRHTHSTGKIFIDGKhvrardttrrirrgLALIPedrqreglvQVLSIASNLTLASLGRFTRLFHIDRGAEKSA 387
Cdd:COG1245 382 FAKILAGVLKPDEGEVDEDLK--------------ISYKP---------QYISPDYDGTVEEFLRSANTDDFGSSYYKTE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 388 IrdaIRDLSIKaPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTS 466
Cdd:COG1245 439 I---IKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH 514
|
490
....*....|....
gi 499968440 467 DLEEVMALSDRIAV 480
Cdd:COG1245 515 DIYLIDYISDRLMV 528
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-253 |
1.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTlGRIILDGKPVSFDSPAHAQA------ 86
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNIYERRvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 -NGIGMIFQELNLFAnMSVAENIfarrEITRGILGIDHKAQVQK-ANAFLKRLDAGIEADTMVE----DLPIGQQQLVEI 160
Cdd:PRK14258 87 rRQVSMVHPKPNLFP-MSVYDNV----AYGVKIVGWRPKLEIDDiVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 161 AKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQG-VAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTR 239
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTK 241
|
250
....*....|....
gi 499968440 240 WIVRSMIGSDAKDF 253
Cdd:PRK14258 242 KIFNSPHDSRTREY 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
280-484 |
1.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTrrirrglalipEDRQREGLVqvL 359
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-----------KLRKHIGIV--F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLASLGRFTRLFHIDRGA-----EKSAIRDAIRDLSIKApNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDE 434
Cdd:PRK13648 90 QNPDNQFVGSIVKYDVAFGLENHAvpydeMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 435 PSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMAlSDRIAVLSNG 484
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-207 |
1.48e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGM 91
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARREITRG---ILGIDHKAQVQkanaflkrldagieaDTMVEDLPIGQQQLVEIAKAMSLNA 168
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANPALVEKwleRLKMAHKLELE---------------DGRISNLKLSKGQKKRLALLLALAE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 169 R--ILIMDEptsalSAAEVEILF------KVIAELKAQGVAIVYISH 207
Cdd:PRK10522 467 ErdILLLDE-----WAADQDPHFrrefyqVLLPLLQEMGKTIFAISH 508
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
271-487 |
1.50e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 271 ISLPRPTGGLSVND-VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTgKIFIDGKHVRARDTT------RR--IRR 341
Cdd:COG4170 11 IEIDTPQGRVKAVDrVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVTADRFRWNGIDLLklspreRRkiIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 342 GLALIPEDRQR---------EGLVQVLSiASNLTlaslGRF-TRLFHIDRGAEKSAIRDAIRD-LSIKAPNPdFEVTSms 410
Cdd:COG4170 90 EIAMIFQEPSScldpsakigDQLIEAIP-SWTFK----GKWwQRFKWRKKRAIELLHRVGIKDhKDIMNSYP-HELTE-- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 411 gGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG4170 162 -GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
278-506 |
1.56e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.01 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRR----IRRGLALIP----ED 349
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinmMFQSYALFPhmtvEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 RQREGLVQVlSIASNLTLASLGRFTRLFHIDRGAEKSairdairdlsikaPNpdfevtSMSGGNQQKVVIGKALMTNPKV 429
Cdd:PRK11607 111 NIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK-------------PH------QLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 430 LLMDEPSRGIDVGAK----ADVFRTMRRLaanGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNEATEEAIIAASA 505
Cdd:PRK11607 171 LLLDEPMGALDKKLRdrmqLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
.
gi 499968440 506 K 506
Cdd:PRK11607 248 E 248
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-488 |
1.56e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 66.71 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 260 AVGAEVFRAENISLPRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRr 338
Cdd:COG4987 328 APGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 339 IRRGLALIPEDrqreglVQVL--SIASNLTLAslgrftrlfhiDRGAEKSAIRDAIR-----DLSIKAPNP-DFEV---- 406
Cdd:COG4987 407 LRRRIAVVPQR------PHLFdtTLRENLRLA-----------RPDATDEELWAALErvglgDWLAALPDGlDTWLgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 407 TSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGlAILFSTSDLEEvMALSDRIAVLSNGQL 486
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAG-LERMDRILVLEDGRI 547
|
..
gi 499968440 487 VA 488
Cdd:COG4987 548 VE 549
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-227 |
1.58e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.70 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRiILDGKpvsfdSPAHAQANGIGMI 92
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT-----APLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQELNLFANMSVAENifarreITRGILGiDHKAQVQKAnaflkrLDAGIEADTMVE---DLPIGQQQLVEIAKAMSLNAR 169
Cdd:PRK11247 87 FQDARLLPWKKVIDN------VGLGLKG-QWRDAALQA------LAAVGLADRANEwpaALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
283-487 |
1.60e-11 |
|
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: 64.10 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRS-------EFFECvigrhthSTGKIFIDGKHVRARDttrrirrglalIPEDRQREGL 355
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKStvvslleRFYDP-------TSGEILLDGVDIRDLN-----------LRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQ---VL---SIASNLtlaSLGRFTR-LFHIDRGAEKSAIRDAIRDLsikaPNP-DFEV----TSMSGGNQQKVVIGKAL 423
Cdd:cd03249 82 VSqepVLfdgTIAENI---RYGKPDAtDEEVEEAAKKANIHDFIMSL----PDGyDTLVgergSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAI-----LFSTSDleevmalSDRIAVLSNGQLV 487
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLSTIRN-------ADLIAVLQNGQVV 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-226 |
1.63e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 63.64 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 19 SKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKpVSFDSpahaqangigmifQELNL 98
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVS-------------QEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 99 FaNMSVAENI-FARReitrgilgIDHK--AQVQKANAF---LKRLDAGIEadTMVED----LPIGQQQLVEIAKAMSLNA 168
Cdd:cd03250 78 Q-NGTIRENIlFGKP--------FDEEryEKVIKACALepdLEILPDGDL--TEIGEkginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 169 RILIMDEPTSALSAAEVEILF-KVIAELKAQGVAIVYISHRLEELMRIgDYITVLRDGQ 226
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
281-486 |
1.79e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFEcvigrhtHSTGKIFID---GKHV--------RARDTTRRIRRGLALIPED 349
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLR-------HLSGLITGDksaGSHIellgrtvqREGRLARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 RQREGLVQVLSIASNLTLASLGRF----TRLFHIDRGAEKSAIRDAIRDLSIKAPNPdfEVTSMSGGNQQKVVIGKALMT 425
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIGALGSTpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQ--RVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
200-488 |
2.25e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 66.34 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 200 VAIVYISHRL-EELMRIGDYITVLRDGQVTGEAMVRDIDTRwivrsmigSDAKDFAKSVDHAVGAEVFRAENISLPRPTG 278
Cdd:COG1132 281 VAFILYLLRLfGPLRQLANVLNQLQRALASAERIFELLDEP--------PEIPDPPGAVPLPPVRGEIEFENVSFSYPGD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 279 GLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGLALIPEDrqreglVQV 358
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL-ESLRRQIGVVPQD------TFL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 L--SIASNLTL----ASLGRftrlfhIDRGAEKSAIRDAIRDLsikaPN-PDFEV----TSMSGGNQQKVVIGKALMTNP 427
Cdd:COG1132 426 FsgTIRENIRYgrpdATDEE------VEEAAKAAQAHEFIEAL----PDgYDTVVgergVNLSGGQRQRIAIARALLKDP 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAIL----FSTsdleeVMAlSDRIAVLSNGQLVA 488
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGRTTIViahrLST-----IRN-ADRILVLDDGRIVE 554
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-486 |
2.30e-11 |
|
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: 62.23 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 266 FRAENISLpRPTGG--LSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGL 343
Cdd:cd03246 1 LEVENVSF-RYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 344 ALIPEDRQreglvqvlsiasnltlaslgrftrLFhidrgaeKSAIRDAIrdlsikapnpdfevtsMSGGNQQKVVIGKAL 423
Cdd:cd03246 79 GYLPQDDE------------------------LF-------SGSIAENI----------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLeEVMALSDRIAVLSNGQL 486
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-231 |
2.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMIFQEL-NLFANMSVAENIfa 110
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVFQNPdNQFVGATVEDDV-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 111 rreitrgILGIDHKAQVQKAnaFLKRLDAGIEADTMVE-------DLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAA 183
Cdd:PRK13642 104 -------AFGMENQGIPREE--MIKRVDEALLAVNMLDfktrepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 184 EVEILFKVIAELKAQ-GVAIVYISHRLEELMRiGDYITVLRDGQVTGEA 231
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-500 |
2.45e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFEcVIGR------HTHSTGKIFIDGKHVRARDTTRrIRRGLALIpedRQREGLVQV 358
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLR-VFNRlielypEARVSGEVYLDGQDIFKMDVIE-LRRRVQMV---FQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 LSIASNLTLA-SLGRFTR----LFHIDRGA-EKSAIRDAIRDlSIKAPnpdfeVTSMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:PRK14247 97 LSIFENVALGlKLNRLVKskkeLQERVRWAlEKAQLWDEVKD-RLDAP-----AGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 433 DEPSRGIDVGAKADVFRTMRRLAANgLAILFSTSDLEEVMALSDRIAVLSNGQLVA------VFD--RNEATEEAI 500
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEwgptreVFTnpRHELTEKYV 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
282-485 |
2.61e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGR-HTHS-TGKIFIDGkhvraRDTTRRIRRGLALIPEDrqrEGLVQVL 359
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiQGNNfTGTILANN-----RKPTKQILKRTGFVTQD---DILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLASLGRFTRlfHIDRGAEKSAIRDAIRDLSI-KAPNP---DFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:PLN03211 156 TVRETLVFCSLLRLPK--SLTKQEKILVAESVISELGLtKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 436 SRGIDVGAKADVFRTMRRLAANGLAILFSTSD-LEEVMALSDRIAVLSNGQ 485
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
43-227 |
2.65e-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: 63.20 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANmSVAENIFARREITrgilgid 122
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQDPTLFSG-TIRSNLDPFDEYS------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 123 hKAQVQKAnafLKRLDAGieadtmvEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELkAQGVAI 202
Cdd:cd03369 110 -DEEIYGA---LRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREE-FTNSTI 177
|
170 180
....*....|....*....|....*..
gi 499968440 203 VYISHRLEElmrIGDY--ITVLRDGQV 227
Cdd:cd03369 178 LTIAHRLRT---IIDYdkILVMDAGEV 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
43-207 |
2.68e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPV----SFDSPAHAQ-------ANGIGMIFQELNLFANMSV------A 105
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlQQDPPRNVEgtvydfvAEGIEEQAEYLKRYHDISHlvetdpS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 106 ENIFARREITRGILgiDHKAQVQ---KANAFLKRLdaGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA 182
Cdd:PRK11147 114 EKNLNELAKLQEQL--DHHNLWQlenRINEVLAQL--GLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
170 180
....*....|....*....|....*..
gi 499968440 183 AEVEIL--FkviaeLKAQGVAIVYISH 207
Cdd:PRK11147 190 ETIEWLegF-----LKTFQGSIIFISH 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-209 |
2.69e-11 |
|
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: 63.58 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 34 ELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdSPAHAQANGIGMIFQELnlfanmsvaenifarRE 113
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQYIKADYEGTVRDLL---------------SS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 114 ITRgilgiDHKAQVQKANAFLKRLdaGIEA--DTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKV 191
Cdd:cd03237 85 ITK-----DFYTHPYFKTEIAKPL--QIEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180
....*....|....*....|....*....
gi 499968440 192 IAE--LKAQGVAIV---------YISHRL 209
Cdd:cd03237 158 IRRfaENNEKTAFVvehdiimidYLADRL 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-486 |
3.43e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 276 PTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRArdTTRRIRRGLALIPedrQREGL 355
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAVRQSLGMCP---QHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASNLTLaslgrFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDfEVTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:TIGR01257 1015 FHHLTVAEHILF-----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 436 SRGIDVGAKADVFRTMRRLAAnGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
275-487 |
3.58e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLsVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHST---GKIFIDGKHVrardTTRRIRRGLALIpedRQ 351
Cdd:TIGR00955 35 RPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI----DAKEMRAISAYV---QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 352 REGLVQVLSIASNLTlaslgrFTRLFHIDRGAEKS----AIRDAIRDLS--------IKAPNpdfEVTSMSGGNQQKVVI 419
Cdd:TIGR00955 107 DDLFIPTLTVREHLM------FQAHLRMPRRVTKKekreRVDEVLQALGlrkcantrIGVPG---RVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFS----TSdleEVMALSDRIAVLSNGQLV 487
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSS---ELFELFDKIILMAEGRVA 246
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
281-503 |
3.59e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHS---TGKIF----IDGKHVRARDTTRRIRRGLALIPEDRQrE 353
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvTADRMrfddIDLLRLSPRERRKLVGHNVSMIFQEPQ-S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 GLVQVLSIASNLTLA-----SLGRFTRLFHIDRgaeKSAI----RDAIRDLSIKAPNPDFEVTSmsgGNQQKVVIGKALM 424
Cdd:PRK15093 101 CLDPSERVGRQLMQNipgwtYKGRWWQRFGWRK---RRAIellhRVGIKDHKDAMRSFPYELTE---GECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 425 TNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVavfdrNEATEEAIIAA 503
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTV-----ETAPSKELVTT 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-213 |
4.71e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIldgkpvsfdspaHAQANGIGM 91
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIFARReitrgilgidhKAQVQKANAF--LKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNAR 169
Cdd:PRK09544 72 VPQKLYLDTTLPLTVNRFLRL-----------RPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 170 ILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELM 213
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVM 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-227 |
4.94e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 9 DDVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIL---DGKPVSFDSPAHAQ 85
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 86 ----------------ANGIGMifqelNLFANMSVAENIFArreitrgiLGIDHKAQV-QKANAFLKRLDagIEADTMvE 148
Cdd:PRK11701 83 rrrllrtewgfvhqhpRDGLRM-----QVSAGGNIGERLMA--------VGARHYGDIrATAGDWLERVE--IDAARI-D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 149 DLPI----GQQQLVEIAKAMSLNARILIMDEPTSAL----SAAEVEILFKVIAELkaqGVAIVYISHRLEELMRIGDYIT 220
Cdd:PRK11701 147 DLPTtfsgGMQQRLQIARNLVTHPRLVFMDEPTGGLdvsvQARLLDLLRGLVREL---GLAVVIVTHDLAVARLLAHRLL 223
|
....*..
gi 499968440 221 VLRDGQV 227
Cdd:PRK11701 224 VMKQGRV 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
281-485 |
8.12e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIG---RHTHSTGKIFIDGKHV---RARDTTRRIRRGLALIPED----- 349
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREIlnlPEKELNKLRAEQISMIFQDpmtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 ----RQREGLVQVLsiasnltlaslgrftrLFHidRGAEKS-AIRDAIRDL-SIKAPNPDFEVT----SMSGGNQQKVVI 419
Cdd:PRK09473 111 npymRVGEQLMEVL----------------MLH--KGMSKAeAFEESVRMLdAVKMPEARKRMKmyphEFSGGMRQRVMI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 420 GKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
283-489 |
1.17e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKhvRARDttrrirrglaLIPEDR------QREGLV 356
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMND----------VPPAERgvgmvfQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSIASN----LTLASLGRFTRLFHIDRGAEKSAIrDAIRDLSIKApnpdfevtsMSGGNQQKVVIGKALMTNPKVLLM 432
Cdd:PRK11000 88 PHLSVAENmsfgLKLAGAKKEEINQRVNQVAEVLQL-AHLLDRKPKA---------LSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 433 DEPSRGID----VGAKADVFRTMRRLaanGLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:PRK11000 158 DEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-209 |
1.30e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 2 TTAEAQKDDVILRLDDVSKVYSGI-VAVKRAnlELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKpVSFdS 80
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGFsLEVEGG--EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISY-K 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 PahaqangigmifQELNLFANMSVAENIfaRREITRGILGIDHKAQVqkanafLKRLdaGIEA--DTMVEDLPIGQQQLV 158
Cdd:COG1245 407 P------------QYISPDYDGTVEEFL--RSANTDDFGSSYYKTEI------IKPL--GLEKllDKNVKDLSGGELQRV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 159 EIAKAMSLNARILIMDEPTSALSAAEVEILFKVI---AELKAQGVAIV--------YISHRL 209
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrrfAENRGKTAMVVdhdiylidYISDRL 526
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
280-487 |
1.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.03 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 280 LSVNDVSLSVKAGEILGIYGLMGAGRSeffecVIGRHTH-----STGKIFIDGKHVRARDTTRRIRRGLALI---PEDRQ 351
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKS-----TIAKHMNallipSEGKVYVDGLDTSDEENLWDIRNKAGMVfqnPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 352 REGLVQ--VLSIASNLtlaslgrftrlfhidrGAEKSAIRDAIrDLSIKAPN----PDFEVTSMSGGNQQKVVIGKALMT 425
Cdd:PRK13633 99 VATIVEedVAFGPENL----------------GIPPEEIRERV-DESLKKVGmyeyRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVmALSDRIAVLSNGQLV 487
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVV 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
67-229 |
1.37e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 67 GRIILDGKPVSfDSPAHAQANGIGMIFQELNLFaNMSVAENI-FARREITRgilgidhkAQVQKANAFlKRLDAGIEA-- 143
Cdd:PTZ00265 1277 GKILLDGVDIC-DYNLKDLRNLFSIVSQEPMLF-NMSIYENIkFGKEDATR--------EDVKRACKF-AAIDEFIESlp 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 144 ---DTMV----EDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQG-VAIVYISHRLEELMRi 215
Cdd:PTZ00265 1346 nkyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR- 1424
|
170
....*....|....
gi 499968440 216 GDYITVLRDGQVTG 229
Cdd:PTZ00265 1425 SDKIVVFNNPDRTG 1438
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
269-488 |
1.57e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSV---NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRA--RDTTRRIRR-- 341
Cdd:PRK10535 8 KDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldADALAQLRReh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 342 -GLALipedrQREGLVQVLSIASNLTLASlgrftrlfhIDRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKV 417
Cdd:PRK10535 88 fGFIF-----QRYHLLSHLTAAQNVEVPA---------VYAGLERKQRLLRAQELLQRlglEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 418 VIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDlEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-482 |
1.62e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 35 LRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRiilDGKPVSFDspahaqangigmifQELNLFANmSVAENIFarREI 114
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWD--------------EVLKRFRG-TELQNYF--KKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 115 TRGILGIDHKAQ-VQ--------KANAFLKRLDAGIEADTMVEDLPI-------------GQQQLVEIAKAMSLNARILI 172
Cdd:PRK13409 156 YNGEIKVVHKPQyVDlipkvfkgKVRELLKKVDERGKLDEVVERLGLenildrdiselsgGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 173 MDEPTSALSAAEVEILFKVIAELkAQGVAIVYISHRLEELMRIGDYITVLRD-----GQVTGEAMVRD-IDTrWI----- 241
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIAYGepgayGVVSKPKGVRVgINE-YLkgylp 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 242 ---VRsmIGSDAKDFAKsvdHAVGAEVFRAENISLPRPTGGLsvNDVSLSVKAGEI-----LGIYGLMGAGRSEFFECVI 313
Cdd:PRK13409 314 eenMR--IRPEPIEFEE---RPPRDESERETLVEYPDLTKKL--GDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 314 GRHTHSTGKIFIDGKhvrardttrrirrgLALIPedrqreglvQVLSIASNLTLASLgrftrLFHIDRGAEKSAIR-DAI 392
Cdd:PRK13409 387 GVLKPDEGEVDPELK--------------ISYKP---------QYIKPDYDGTVEDL-----LRSITDDLGSSYYKsEII 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 393 RDLSIKaPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEV 471
Cdd:PRK13409 439 KPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMI 517
|
490
....*....|.
gi 499968440 472 MALSDRIAVLS 482
Cdd:PRK13409 518 DYISDRLMVFE 528
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
283-487 |
1.68e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrarDTTRRI--RRGLALipedRQREGLV--QV 358
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF---DFSQKPseKAIRLL----RQKVGMVfqQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 -----LSIASNLTLAS---LGrFTRLFHIDRgAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:COG4161 92 nlwphLTVMENLIEAPckvLG-LSKEQAREK-AMKLLARLRLTDKADRFPL------HLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 431 LMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
282-487 |
1.80e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrarDTTRRIRRGLALIPEDRQREGLV-QVLS 360
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTARSLSQQKGLIRQLRQHVGFVfQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLasLGRFTRLFHIDRGAEKSAIRDAIRDLSIK---APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSR 437
Cdd:PRK11264 96 LFPHRTV--LENIIEGPVIVKGEPKEEATARARELLAKvglAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499968440 438 GIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-227 |
1.94e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 15 LDDVSKVY-SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdspAHAQANGIGMIF 93
Cdd:PRK15056 9 VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 Q--ELNLFANMSVAENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARIL 171
Cdd:PRK15056 85 QseEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 172 IMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYiTVLRDGQV 227
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTV 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
284-488 |
2.36e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRaRDTTRRIRRGLALIPEDRQREGLVQVLSIAS 363
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 364 NLTLASLGRFTRLFHIDRGAEKSAIR-DAIRDLSIKApnpdfeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVG 442
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKAMQaTGITHLADQS------VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 443 AKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK10253 178 HQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-291 |
2.36e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdsPAHAQAN------GIGMIFQ--ELNL 98
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT---AGKKNKKlkplrkKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 99 FANmSVAENI-FARREitrgiLGIDHKAQVQKANAFLKRLdaGIEADTMVE---DLPIGQQQLVEIAKAMSLNARILIMD 174
Cdd:PRK13634 99 FEE-TVEKDIcFGPMN-----FGVSEEDAKQKAREMIELV--GLPEELLARspfELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 175 EPTSALSAAEVEILFKVIAEL-KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI--DTRWIVRsmIGSDAK 251
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEA--IGLDLP 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499968440 252 D---FAKSVDHAVGaevfraenISLPRPTggLSVNDVSLSVKA 291
Cdd:PRK13634 249 EtvkFKRALEEKFG--------ISFPKPC--LTLEELAHEVVQ 281
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
278-488 |
2.40e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 278 GGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRardttRRIRRGL-ALIPEDRQREGLV 356
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLvAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSiasnLTLASLGRFTRLFHIDRGAEKSaiRDAIRDLSIKAPNPDF---EVTSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:PRK15056 94 PVLV----EDVVMMGRYGHMGWLRRAKKRD--RQIVTAALARVDMVEFrhrQIGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 434 EPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDrIAVLSNGQLVA 488
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLA 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
282-487 |
2.47e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.21 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECvIGR------HTHSTGKIFIDGKHVRARDTTrrirrglalIPEDRQREGL 355
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRmndlipGARVEGEILLDGEDIYDPDVD---------VVELRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 V-QV-----LSIASNLTLAslgrfTRLFHIDRGAEKSAI-RDAIRDLSIkapnPDfEV--------TSMSGGNQQKVVIG 420
Cdd:COG1117 97 VfQKpnpfpKSIYDNVAYG-----LRLHGIKSKSELDEIvEESLRKAAL----WD-EVkdrlkksaLGLSGGQQQRLCIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 421 KALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANgLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
284-484 |
2.89e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtrriRRGLALipedrQREGLVQVLSIAS 363
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVF-----QNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 364 NLTLAslgrfTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGA 443
Cdd:PRK11248 90 NVAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499968440 444 KADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNG 484
Cdd:PRK11248 164 REQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
282-504 |
4.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRR-GLALIPEDRQREGLVQVLS 360
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKiGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLASLGRFTRLFHIDRGAEksairdAIRDLSIKAPNPdfevTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALL------AVNMLDFKTREP----ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 441 VGAKADVFRTMRRLAAN-GLAILFSTSDLEEVmALSDRIAVLSNGQLVavfdrNEATEEAIIAAS 504
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEII-----KEAAPSELFATS 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-227 |
4.36e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 26 VAVKRANLELRRGAVNVLVGENGAGKST----LMKIIAgverpTLGRIILDGKPV-SFDS----PAHAQangIGMIFQEL 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhNLNRrqllPVRHR---IQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 97 N--LFANMSVAENIFARREITRGILGIDHK-AQVQKANAflkrlDAGIEADTMVE---DLPIGQQQLVEIAKAMSLNARI 170
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGLRVHQPTLSAAQReQQVIAVME-----EVGLDPETRHRypaEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 171 LIMDEPTSALS-AAEVEILfkviAELKA----QGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK15134 447 IILDEPTSSLDkTVQAQIL----ALLKSlqqkHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
409-502 |
4.41e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 409 MSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|....
gi 499968440 489 VFDRNEATEEAIIA 502
Cdd:PRK10938 216 TGEREEILQQALVA 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
275-487 |
4.45e-10 |
|
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: 59.94 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdTTRRIRRGLALIPEDrqreg 354
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQIGLVSQD----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 lvQVL---SIASNLTLAslgrftrlfhiDRGAEKSAIRDAIR-----DLSIKAPNP-DFEV----TSMSGGNQQKVVIGK 421
Cdd:cd03251 85 --VFLfndTVAENIAYG-----------RPGATREEVEEAARaanahEFIMELPEGyDTVIgergVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 422 ALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN--GLAILFSTSDLEEvmalSDRIAVLSNGQLV 487
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAHRLSTIEN----ADRIVVLEDGKIV 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
281-494 |
4.79e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECvIGR------HTHSTGKIFIDGKHVRARDT-TRRIRRGLALI------- 346
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRmndlnpEVTITGSIVYNGHNIYSPRTdTVDLRKEIGMVfqqpnpf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PedrqreglvqvLSIASN----LTLASLGRFTRLfhiDRGAEKSAIRDAIRDlSIKAPNPDFEVtSMSGGNQQKVVIGKA 422
Cdd:PRK14239 99 P-----------MSIYENvvygLRLKGIKDKQVL---DEAVEKSLKGASIWD-EVKDRLHDSAL-GLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 423 LMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLaANGLAILFSTSDLEEVMALSDRIAVLSNGQLVAVFDRNE 494
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
283-487 |
5.28e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHT--HSTGKIFIDGKhvrardttrrirrglaLIPEDRQRE-GLVQVL 359
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR----------------PLDKNFQRStGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIAS-NLTLASLGRFtrlfhidrgaekSAirdAIRDLSIKapnpdfevtsmsggNQQKVVIGKALMTNPKVLLMDEPSRG 438
Cdd:cd03232 88 DVHSpNLTVREALRF------------SA---LLRGLSVE--------------QRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 439 IDVGAKADVFRTMRRLAANGLAILFSTSD-LEEVMALSDRIAVL-SNGQLV 487
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTIHQpSASIFEKFDRLLLLkRGGKTV 189
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
281-487 |
5.68e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.19 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRgLALIPED-------RQRE 353
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR-IRMIFQDpstslnpRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 GlvQVLSIASNLTlaslgrfTRLFHIDRgaEKsAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMD 433
Cdd:PRK15112 107 S--QILDFPLRLN-------TDLEPEQR--EK-QIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 434 EPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
281-487 |
5.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGK--HVRARDT-TRRIRRGLALI---PEDR---- 350
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItiTHKTKDKyIRPVRKRIGMVfqfPESQlfed 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 351 --QREGLVQVLSIASNLTLASLGRFTRLfhIDRGAEksairdaiRDLSIKAPnpdFEvtsMSGGNQQKVVIGKALMTNPK 428
Cdd:PRK13646 102 tvEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFS--------RDVMSQSP---FQ---MSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 429 VLLMDEPSRGIDVGAKADVFRTMRRLAA-NGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
276-487 |
7.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 276 PTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRrglalipEDRQREGL 355
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIK-------QIRKKVGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 V------QVLSiasNLTLASLGRFTRLFHIDR-GAEKSAiRDAIRDLSIKAP----NPdFEvtsMSGGNQQKVVIGKALM 424
Cdd:PRK13649 90 VfqfpesQLFE---ETVLKDVAFGPQNFGVSQeEAEALA-REKLALVGISESlfekNP-FE---LSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 425 TNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-227 |
8.30e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 22 YSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQAngIGMIF-QELNLFA 100
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR--IGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 101 NMSVAENiFarrEITRGILGIDhkaqvqkANAFLKRLDAGIEA-------DTMVEDLPIGQQQLVEIAKAMSLNARILIM 173
Cdd:COG4586 110 DLPAIDS-F---RLLKAIYRIP-------DAEYKKRLDELVELldlgellDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 174 DEPTSALSA-AEVEILfKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:COG4586 179 DEPTIGLDVvSKEAIR-EFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-236 |
1.99e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 21 VYSGIVAVKRANLELRRGAVNVLVGENGAGKS-----TLMKIIAGVERpTLGRIILDGKPVsfdSPAHAQANGIGMIFQE 95
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPV---APCALRGRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 96 ----LNLFANMS--VAENIFArreitRGILGIDhkaqvqkaNAFLKRLDA-GIEADTMVEDL-PI----GQQQLVEIAKA 163
Cdd:PRK10418 88 prsaFNPLHTMHthARETCLA-----LGKPADD--------ATLTAALEAvGLENAARVLKLyPFemsgGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 164 MSLNARILIMDEPTS---ALSAAEVEILFKVIAELKAQGVAIVyiSHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK10418 155 LLCEAPFIIADEPTTdldVVAQARILDLLESIVQKRALGMLLV--THDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-226 |
2.04e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQ-------ANGIGmifQEL----NLFA 100
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylghQPGIK---TELtaleNLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 101 NMSVAENifARREITRGILgidhkAQVqkanaflkrldaGIEAdtmVEDLPI-----GQQQLVEIAKAMSLNARILIMDE 175
Cdd:PRK13538 98 YQRLHGP--GDDEALWEAL-----AQV------------GLAG---FEDVPVrqlsaGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 176 PTSALSAAEVEILFKVIAELKAQGVAIVYISHRleELMRIGDYITVLRDGQ 226
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLRLGQ 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
269-487 |
2.20e-09 |
|
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: 57.62 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARdTTRRIRRGLALIPE 348
Cdd:cd03254 6 ENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 DrqreglvQVL---SIASNLtlaslgRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNP-DFEV----TSMSGGNQQKVVIG 420
Cdd:cd03254 85 D-------TFLfsgTIMENI------RLGRPNATDEEVIEAAKEAGAHDFIMKLPNGyDTVLgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 421 KALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFS--TSDLEEvmalSDRIAVLSNGQLV 487
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAhrLSTIKN----ADKILVLDDGKII 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-227 |
2.36e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQA--NGIG 90
Cdd:PRK10261 325 LRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQE--LNLFANMSVAENIFARREItRGILgiDHKAQVQKANAFLKRLDAGIE-ADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:PRK10261 405 FIFQDpyASLDPRQTVGDSIMEPLRV-HGLL--PGKAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 168 ARILIMDEPTSALsaaEVEILFKVIAEL----KAQGVAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:PRK10261 482 PKVIIADEAVSAL---DVSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
254-487 |
2.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 254 AKSVDHAvgAEVFRAENISLPRpTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECV------IGRHTHStGKIFIDG 327
Cdd:PRK14271 12 AADVDAA--APAMAAVNLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYS-GDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 328 KHVRARDTTRRIRRGLALI---PEDRQREGLVQVLSIASNLTLASLGRFtrlfhidRGAEKS-----AIRDAIRDLSIKA 399
Cdd:PRK14271 88 RSIFNYRDVLEFRRRVGMLfqrPNPFPMSIMDNVLAGVRAHKLVPRKEF-------RGVAQArltevGLWDAVKDRLSDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 400 PnpdfevTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLaANGLAILFSTSDLEEVMALSDRIA 479
Cdd:PRK14271 161 P------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAA 233
|
....*...
gi 499968440 480 VLSNGQLV 487
Cdd:PRK14271 234 LFFDGRLV 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
269-483 |
3.34e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.72 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLsVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHT---HSTGKIFIDGKHVRARDTTRRirrGLAL 345
Cdd:COG4136 5 ENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAEQR---RIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 346 IPEDrqrEGLVQVLSIASNLTLASLGRftrlfhIDRGAEKSAIRDAIRDLSIkapnPDFE---VTSMSGGNQQKVVIGKA 422
Cdd:COG4136 81 LFQD---DLLFPHLSVGENLAFALPPT------IGRAQRRARVEQALEEAGL----AGFAdrdPATLSGGQRARVALLRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 423 LMTNPKVLLMDEPSRGIDVGAKAD----VFRTMRRLaanGLAILFSTSDLEEVMALSdRIAVLSN 483
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQfrefVFEQIRQR---GIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-219 |
3.48e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILdGKPVSfdspahaqangI 89
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIFQEL-NLFANMSVAENIFARREITRgiLGidhKAQVQkANAFLKRLD-AGIEADTMVEDLPIGQQQLVEIAKAMSLN 167
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEISGGLDIIK--LG---KREIP-SRAYVGRFNfKGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 168 ARILIMDEPTSALsaaEVEILFKV-IAELKAQGVAIVyISHRLEELMRIGDYI 219
Cdd:TIGR03719 462 GNVLLLDEPTNDL---DVETLRALeEALLNFAGCAVV-ISHDRWFLDRIATHI 510
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
282-487 |
3.72e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSeffecVIGR-----HTHSTGKIFIDGKHVR--ARDTTRRIRRGLALIPED----- 349
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKS-----TLARlltmiETPTGGELYYQGQDLLkaDPEAQKLLRQKIQIVFQNpygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 --RQREG--LVQVLSIASNLTLAslgrftrlfhiDRgAEKsaIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMT 425
Cdd:PRK11308 106 npRKKVGqiLEEPLLINTSLSAA-----------ER-REK--ALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-440 |
3.77e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGvERPtlgriILDGKPV-SFDSPAH----AQANGIGMIFQELNlfANM-SVA 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-ELP-----LLSGERQsQFSHITRlsfeQLQKLVSDEWQRNN--TDMlSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 106 ENIFAR--REITRgiLGIDHKAQVQKANAFLkrldaGIEA--DTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALS 181
Cdd:PRK10938 95 EDDTGRttAEIIQ--DEVKDPARCEQLAQQF-----GITAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 182 AAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSDakdfaksvdhav 261
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSE------------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 262 gaevfRAENISLPRP-------------------TGGLSVND------VSLSVKAGEILGIYGLMGAGRSEFFECVIGRH 316
Cdd:PRK10938 236 -----QLEGVQLPEPdepsarhalpaneprivlnNGVVSYNDrpilhnLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 317 THS-TGKIFIDGKhvrardttrriRRGLA-LIPEDRQREGLV--------QVLSIASNLTLA----SLGRFtrlfhidrg 382
Cdd:PRK10938 311 PQGySNDLTLFGR-----------RRGSGeTIWDIKKHIGYVssslhldyRVSTSVRNVILSgffdSIGIY--------- 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 383 aekSAIRDAIRDLS--------IKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK10938 371 ---QAVSDRQQKLAqqwldilgIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
4.07e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 2 TTAEAQKDDVILRLDDVSKVY--SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-F 78
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 79 DSPAHAQAngIGMIFQELNLFANmSVAEN-IFARREITRGILgIDHKAQV--QKANAFLKRLDAGI-EADtmvEDLPIGQ 154
Cdd:PRK11160 408 SEAALRQA--ISVVSQRVHLFSA-TLRDNlLLAAPNASDEAL-IEVLQQVglEKLLEDDKGLNAWLgEGG---RQLSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 155 QQLVEIAKAMSLNARILIMDEPTSALSAA-EVEILfKVIAELkAQGVAIVYISHRLEELMRIgDYITVLRDGQV 227
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAEtERQIL-ELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-203 |
4.17e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 45 GENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAH--AQANGIGMIFQELNLFANMSVAENIFARReitrgilgid 122
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRfmAYLGHLPGLKADLSTLENLHFLCGLHGRR---------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 123 hkAQVQKANAFLKRLDAGIEaDTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVI-AELKAQGVA 201
Cdd:PRK13543 114 --AKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIsAHLRGGGAA 190
|
..
gi 499968440 202 IV 203
Cdd:PRK13543 191 LV 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-208 |
4.67e-09 |
|
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: 55.62 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSkVYS--GIVAVKRANLELRRGAvNVLV-GENGAGKSTLMKIIAGVERPTLGRIILdgkpvsfdsPAHAqangi 89
Cdd:cd03223 1 IELENLS-LATpdGRVLLKDLSFEIKPGD-RLLItGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGE----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 90 GMIF--QelnlfanmsvaenifaRREITRGILgidhKAQVqkANAFLKRLDAGieadtmvedlpigQQQLVEIAKAMSLN 167
Cdd:cd03223 65 DLLFlpQ----------------RPYLPLGTL----REQL--IYPWDDVLSGG-------------EQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499968440 168 ARILIMDEPTSALSaaeVEILFKVIAELKAQGVAIVYISHR 208
Cdd:cd03223 110 PKFVFLDEATSALD---EESEDRLYQLLKELGITVISVGHR 147
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-228 |
4.81e-09 |
|
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: 56.12 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 35 LRRGAVNVLVGENGAGKSTLMKIIAGVERPTL---GRIILDGKPVS-FDSPAHAQAngigmIF--QELNLFANMSVAENI 108
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKeFAEKYPGEI-----IYvsEEDVHFPTLTVRETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 -FARR----EITRGILGidhkaqvqkanaflkrldagieadtmvedlpiGQQQLVEIAKAMSLNARILIMDEPTSAL-SA 182
Cdd:cd03233 105 dFALRckgnEFVRGISG--------------------------------GERKRVSIAEALVSRASVLCWDNSTRGLdSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 183 AEVEILfKVIAEL--KAQGVAIVYISHRLEELMRIGDYITVLRDGQVT 228
Cdd:cd03233 153 TALEIL-KCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
284-487 |
5.42e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRrIRRGLALipedRQREGLV--QV--- 358
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS-DKAIREL----RRNVGMVfqQYnlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 --LSIASNLTLASLgRFTRLfhidrgAEKSAIRDAIRDLSIK--APNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDE 434
Cdd:PRK11124 95 phLTVQQNLIEAPC-RVLGL------SKDQALARAEKLLERLrlKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 435 PSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
274-487 |
6.24e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 274 PRPTGGLsvNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTR---RIRRGLALI---P 347
Cdd:PRK13641 17 PMEKKGL--DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkKLRKKVSLVfqfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 348 EDRQREGLV--QVLSIASNLTLAslgrftrlfhiDRGAEKSAIRDAIR-----DLSIKAPnpdFEvtsMSGGNQQKVVIG 420
Cdd:PRK13641 95 EAQLFENTVlkDVEFGPKNFGFS-----------EDEAKEKALKWLKKvglseDLISKSP---FE---LSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 421 KALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-225 |
6.47e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.84 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANmSVAEN 107
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPLHTLRSRLSIILQDPILFSG-SIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 108 IFARREITRGILGidHKAQVQKANAFLKRLDAGIeaDTMV----EDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAA 183
Cdd:cd03288 115 LDPECKCTDDRLW--EALEIAQLKNMVKSLPGGL--DAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499968440 184 EVEILFKVIAELKAQGvAIVYISHRLEELMRiGDYITVLRDG 225
Cdd:cd03288 191 TENILQKVVMTAFADR-TVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
281-487 |
6.67e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHStGKIFIDGKHVRARDTTRrirrglalIPEdRQREGLV--QV 358
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQR--------ISE-KERRNLVgaEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 359 LSIASNlTLASLGR-FTRLFHI------DRGAEKSAIRDAIRDL----SIKAPNPDFEVT--SMSGGNQQKVVIGKALMT 425
Cdd:PRK11022 92 AMIFQD-PMTSLNPcYTVGFQImeaikvHQGGNKKTRRQRAIDLlnqvGIPDPASRLDVYphQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 426 NPKVLLMDEPSRGIDVGAKADVFRTMRRLA-ANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-222 |
6.81e-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: 56.61 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 36 RRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRiiLDGKPVSFDSPAHAQANGIGMIFQELnLFANMSVAENIFARREIT 115
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFRGSELQNYFTKL-LEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 116 RGILG-----IDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFK 190
Cdd:cd03236 101 KAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|..
gi 499968440 191 VIAELKAQGVAIVYISHRLEELMRIGDYITVL 222
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
282-488 |
7.38e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECvIGR-HTHSTGKIFIDGKHVRARDTTRRIRRgLALipedrqregLVQVLS 360
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSM-ISRlLPPDSGEVLVDGLDVATTPSRELAKR-LAI---------LRQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLT---LASLGRF----TRLFHIDRgaekSAIRDAIRDLSIKapnpDFE---VTSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:COG4604 86 INSRLTvreLVAFGRFpyskGRLTAEDR----EIIDEAIAYLDLE----DLAdryLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 431 LMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVA 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
282-488 |
7.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIG---RHTHSTGKIFIDGKHVRArDTTRRIRR--GLALIPEDRQREGLV 356
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTA-KTVWDIREkvGIVFQNPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 357 QVLSIAsnltlasLGRFTRlfHIDRGAEKSAIRDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK13640 102 VGDDVA-------FGLENR--AVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499968440 437 RGIDVGAKADVFRTMRRLAA-NGLAILFSTSDLEEVmALSDRIAVLSNGQLVA 488
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLA 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
276-488 |
7.61e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 276 PTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRI---RRGLALI---PED 349
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIkpvRKKVGVVfqfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 350 RQREGLVqvlsiasnltLASLGRFTRLFHIDR------GAEKSAIRDAIRDLSIKAPnpdFEvtsMSGGNQQKVVIGKAL 423
Cdd:PRK13643 96 QLFEETV----------LKDVAFGPQNFGIPKekaekiAAEKLEMVGLADEFWEKSP---FE---LSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-227 |
8.66e-09 |
|
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: 58.42 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANmSVAEN 107
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-KIGLHDLRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 108 I-----FARREITRGIlgidhkaQVQKANAFLKRLDAGI--EADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSAL 180
Cdd:TIGR00957 1380 LdpfsqYSDEEVWWAL-------ELAHLKTFVSALPDKLdhECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 181 SaAEVEILFKVIAELKAQGVAIVYISHRLEELMrigDY--ITVLRDGQV 227
Cdd:TIGR00957 1453 D-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIM---DYtrVIVLDKGEV 1497
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
283-488 |
1.07e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.84 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGR--HTHSTGKIFIDGKHVRARDTTRRIRRGLAL-------IPedrqre 353
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLafqypveIP------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 G--LVQVLSIASNLTlaslgrftRLFHIDRGAEKSAIRDAIRDLSIkapNPDF---EV-TSMSGGNQQKVVIGKALMTNP 427
Cdd:COG0396 91 GvsVSNFLRTALNAR--------RGEELSAREFLKLLKEKMKELGL---DEDFldrYVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSD---LEEVMAlsDRIAVLSNGQLVA 488
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGRIVK 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
282-487 |
1.11e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKI---FIDGKHVRARDTT----------RRIRRGLALIPE 348
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKekvleklviqKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 DRQREGLV------QVL--SIASNLTLA--SLGrftrlfhIDRGAEKSAIRDAIR----DLSIKAPNPdFEvtsMSGGNQ 414
Cdd:PRK13651 103 IRRRVGVVfqfaeyQLFeqTIEKDIIFGpvSMG-------VSKEEAKKRAAKYIElvglDESYLQRSP-FE---LSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 415 QKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-227 |
1.11e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 55.74 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 31 ANLELRRGAVNVLVGENGAGKSTLMKIIAGVERP---TLGRIILDGKPVSfdsPAHAQANgIGMIFQELNLFANMSVAE- 106
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQKC-VAYVRQDDILLPGLTVREt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 107 ----NIFARREITRgilgidhKAQVQKANAFLKRLDAGIE--ADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSAL 180
Cdd:cd03234 102 ltytAILRLPRKSS-------DAIRKKRVEDVLLRDLALTriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 181 SAAEVEILFKVIAELKAQG-VAIVYISHRLEELMRIGDYITVLRDGQV 227
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNrIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
281-489 |
1.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRAR----DTTRRIRRGLALI---PEDRqre 353
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkiKEVKRLRKEIGLVfqfPEYQ--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 gLVQVlSIASNLTLASlgrftrlfhIDRGAEKSAIRDAI----------RDLSIKAPnpdFEvtsMSGGNQQKVVIGKAL 423
Cdd:PRK13645 103 -LFQE-TIEKDIAFGP---------VNLGENKQEAYKKVpellklvqlpEDYVKRSP---FE---LSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
285-465 |
1.37e-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: 54.81 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV-RARDTtrrIRRGLALIPedrQREGLVQVLSIAS 363
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDS---IARGLLYLG---HAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 364 NLtlaslgRFTRLFHIDrgaekSAIRDAIRDLSIKAPNpDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGA 443
Cdd:cd03231 93 NL------RFWHADHSD-----EQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|..
gi 499968440 444 KADVFRTMRRLAANGLAILFST 465
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTT 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-178 |
1.51e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 26 VAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVsfDSPAHAQANGIGMIFQELNLFANMSVA 105
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDIATRRRVGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 106 ENIF--ARreitrgILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTS 178
Cdd:NF033858 358 QNLElhAR------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-208 |
1.64e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSkVYS--GIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAG--------VERPTLGRII-LDGKP------ 75
Cdd:COG4178 363 LALEDLT-LRTpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVLfLPQRPylplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 76 ----VSFdsPAHAQAngigmifqelnlfanmsvaeniFARREItRGILgidHKAQVQkanAFLKRLDAgiEAD-TMVedL 150
Cdd:COG4178 442 lreaLLY--PATAEA----------------------FSDAEL-REAL---EAVGLG---HLAERLDE--EADwDQV--L 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 151 PIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAElKAQGVAIVYISHR 208
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR 543
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
258-441 |
1.69e-08 |
|
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: 55.17 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 258 DHAVGAEVFRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtR 337
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 338 RIRRGLALIPEDRQREGLVQVLSIASNLTLASLGRFTRLfhidrgAEKSAIRDAIRDLsikAPNPDFEV----TSMSGGN 413
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEA------AQKAHAHSFISEL---ASGYDTEVgekgSQLSGGQ 155
|
170 180
....*....|....*....|....*...
gi 499968440 414 QQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDA 183
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-210 |
1.73e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 39 AVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfdspaHAQANGIGMIFQELNLFANMSVAENIFARREITRGI 118
Cdd:PRK13541 27 AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-----NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 119 LGIDHKAQVQKANAFLkrldagieaDTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAeLKAQ 198
Cdd:PRK13541 102 ETLYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKAN 171
|
170
....*....|..
gi 499968440 199 GVAIVYISHRLE 210
Cdd:PRK13541 172 SGGIVLLSSHLE 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-111 |
2.28e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRI-ILDGkpvSFDSPAHAQANG-- 88
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGG---DMADARHRRAVCpr 77
|
90 100
....*....|....*....|....*..
gi 499968440 89 IGMIFQEL--NLFANMSVAENI--FAR 111
Cdd:NF033858 78 IAYMPQGLgkNLYPTLSVFENLdfFGR 104
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
281-488 |
2.40e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 281 SVNDVSLSVKAGEILGIYGLMGAGRSEffecvigrhthstGKIfidGKHVRARDTTRRIRRGLALIPEDRQ--------- 351
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**R-------------GAL---PAHV*GPDAGRRPWRF*TWCANRRAlrrtig*hr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 352 --REGLVQVLSIASNLTLasLGRFTRLFHIDRGAEKSAI--RDAIRDLSIKApnpdfeVTSMSGGNQQKVVIGKALMTNP 427
Cdd:NF000106 92 pvR*GRRESFSGRENLYM--IGR*LDLSRKDARARADELleRFSLTEAAGRA------AAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLVA 488
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
275-487 |
2.61e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALIPedrqreg 354
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-AKFGLTDLRRVLSIIP------- 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 lvQVLSIASNLTLASLGRFTRlfHIDRGAEKSAIRDAIRDLSIKAP-NPDFEVT----SMSGGNQQKVVIGKALMTNPKV 429
Cdd:PLN03232 1317 --QSPVLFSGTVRFNIDPFSE--HNDADLWEALERAHIKDVIDRNPfGLDAEVSeggeNFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 430 LLMDEPSRGIDVGAKADVFRTMRRlAANGLAILFSTSDLEEVMAlSDRIAVLSNGQLV 487
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-224 |
3.62e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 29 KRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMIFQELNLFANmSVAENI 108
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 -------------------------------FARREITRGILGI-------DHKAQVQKANAFLKRLDA-GIEADTMVED 149
Cdd:PTZ00265 481 kyslyslkdlealsnyynedgndsqenknkrNSCRAKCAGDLNDmsnttdsNELIEMRKNYQTIKDSEVvDVSKKVLIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 150 -------------------LPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAI-VYISHRL 209
Cdd:PTZ00265 561 fvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRL 640
|
250
....*....|....*
gi 499968440 210 EELmRIGDYITVLRD 224
Cdd:PTZ00265 641 STI-RYANTIFVLSN 654
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-209 |
3.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 34 ELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKpVSFdSPahaqangigmifQELNLFANMSVAENIfarRE 113
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISY-KP------------QYIKPDYDGTVEDLL---RS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 114 ITRGILGIDHKAQVqkanafLKRLdaGIEA--DTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKV 191
Cdd:PRK13409 424 ITDDLGSSYYKSEI------IKPL--QLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180
....*....|....*....|....*....
gi 499968440 192 I---AELKAQGVAIV--------YISHRL 209
Cdd:PRK13409 496 IrriAEEREATALVVdhdiymidYISDRL 524
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-210 |
4.85e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 29 KRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSpahaqangigmifqelnlfaNMSVAENI 108
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR--------------------EASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 109 FARREITRGIlGIDHKAQVQKANAFLKRLDAgieadtmvedLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEIL 188
Cdd:COG2401 107 GRKGDFKDAV-ELLNAVGLSDAVLWLRRFKE----------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 499968440 189 FKVIAEL-KAQGVAIVYISHRLE 210
Cdd:COG2401 176 ARNLQKLaRRAGITLVVATHHYD 198
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-236 |
5.35e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKS----TLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQ---ANGIGMIFQE--LN 97
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvGAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 98 LFANMSVAENIFarrEITRGILGIDHKAQVQKANAFLKRL---DAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMD 174
Cdd:PRK11022 102 LNPCYTVGFQIM---EAIKVHQGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 175 EPTSALsaaEVEILFKVIAEL----KAQGVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK11022 179 EPTTAL---DVTIQAQIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-227 |
7.76e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVS-FDSPAHAQAngIGMIFQELNLFANmSVAENI--FARREiTRGIL 119
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkFGLTDLRRV--LSIIPQSPVLFSG-TVRFNIdpFSEHN-DADLW 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 120 GIDHKAQVQKAnafLKRLDAGIEADTMV--EDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAElKA 197
Cdd:PLN03232 1343 EALERAHIKDV---IDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE-EF 1418
|
170 180 190
....*....|....*....|....*....|
gi 499968440 198 QGVAIVYISHRLEELMRIgDYITVLRDGQV 227
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIIDC-DKILVLSSGQV 1447
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
282-497 |
1.17e-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: 52.14 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTH--STGKIFIDGKHVrardttrrirrgLALIPEDRQREGLvqvl 359
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDI------------TDLPPEERARLGI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 siasnlTLAslgrFTRLFHIdrgaEKSAIRDAIRDLsikapNPDFevtsmSGGNQQKVVIGKALMTNPKVLLMDEPSRGI 439
Cdd:cd03217 80 ------FLA----FQYPPEI----PGVKNADFLRYV-----NEGF-----SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 440 DVGAKADVFRTMRRLAANGLAILFSTSdLEEVMAL--SDRIAVLSNGQLVAVFDRNEATE 497
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKELALE 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
247-468 |
1.28e-07 |
|
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: 54.29 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 247 GSDAKDFAKSVDHAVGAEVFRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFID 326
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 327 GKHVRARDTTRrIRRGLALIPEDRQreglVQVLSIASNLTLASLGRFTRlfHIDRGAEKSAIRDAIRDLsikapnPDFEV 406
Cdd:TIGR02868 396 GVPVSSLDQDE-VRRRVSVCAQDAH----LFDTTVRENLRLARPDATDE--ELWAALERVGLADWLRAL------PDGLD 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 407 TSM-------SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRlAANGLAILFSTSDL 468
Cdd:TIGR02868 463 TVLgeggarlSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
275-491 |
1.77e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 275 RPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALIPEDRqreg 354
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-AKIGLHDLRFKITIIPQDP---- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 355 lvQVLSIASNLTLASLGRFTRLfHIDRGAEKSAIRDAIRDLSIKApnpDFEVT----SMSGGNQQKVVIGKALMTNPKVL 430
Cdd:TIGR00957 1370 --VLFSGSLRMNLDPFSQYSDE-EVWWALELAHLKTFVSALPDKL---DHECAeggeNLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 431 LMDEPSRGIDVGAKaDVFRTMRRLAANGLAILFSTSDLEEVMALSdRIAVLSNGQlVAVFD 491
Cdd:TIGR00957 1444 VLDEATAAVDLETD-NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE-VAEFG 1501
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-225 |
1.79e-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: 51.95 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 23 SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANGIGMI--FQELNLFA 100
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVayAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 101 NMSVAENIfarreitrgILGIDHKAQvqkanaflkRLDAGIEADTMVEDLPI------------------GQQQLVEIAK 162
Cdd:cd03290 92 NATVEENI---------TFGSPFNKQ---------RYKAVTDACSLQPDIDLlpfgdqteigerginlsgGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 163 AMSLNARILIMDEPTSALSAAEVEILFK--VIAELKAQGVAIVYISHRLEELMRiGDYITVLRDG 225
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-236 |
2.24e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGvERP---------TLGRIILDGKPVS-FDSPAHA-------QANGIGMIF- 93
Cdd:PRK13547 21 SLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTgggaprgarVTGDVTLNGEPLAaIDAPRLArlravlpQAAQPAFAFs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 94 -QELNLFANMSVAENIFARREITRGIlgidhkaqvqkANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMS------- 165
Cdd:PRK13547 100 aREIVLLGRYPHARRAGALTHRDGEI-----------AWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 166 --LNARILIMDEPTSALSAAEVEILFKVIAELKAQ-GVAIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDI 236
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-227 |
2.92e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSfDSPAHAQANGIGMIFQELNLFANmSVAE 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 107 NI-FARREITRgiLGIDHKAQVQKANAFLKRLDAGIeaDTMVED----LPIGQQQLVEIAKAMSLNARILIMDEptsALS 181
Cdd:PRK10789 408 NIaLGRPDATQ--QEIEHVARLASVHDDILRLPQGY--DTEVGErgvmLSGGQKQRISIARALLLNAEILILDD---ALS 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 182 AAEVEILFKVIAELK--AQGVAIVYISHRLEELMRiGDYITVLRDGQV 227
Cdd:PRK10789 481 AVDGRTEHQILHNLRqwGEGRTVIISAHRLSALTE-ASEILVMQHGHI 527
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-489 |
3.01e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 384 EKSAIRDAIRD-LSIKAPNpdfevtsMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLaANGLAIL 462
Cdd:PRK14267 131 KKAALWDEVKDrLNDYPSN-------LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIV 202
|
90 100
....*....|....*....|....*..
gi 499968440 463 FSTSDLEEVMALSDRIAVLSNGQLVAV 489
Cdd:PRK14267 203 LVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
254-447 |
3.13e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 254 AKSVDHAVGAEVFraENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVraR 333
Cdd:PRK13657 325 AIDLGRVKGAVEF--DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI--R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 334 DTTRR-IRRGLALIpedRQREGLVQvLSIASNLtlaSLGRFTRlfhIDRGAEKSAIRDAIRDLSIKAPNP-DFEV----T 407
Cdd:PRK13657 401 TVTRAsLRRNIAVV---FQDAGLFN-RSIEDNI---RVGRPDA---TDEEMRAAAERAQAHDFIERKPDGyDTVVgergR 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADV 447
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
283-482 |
3.17e-07 |
|
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: 51.64 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAG-----EILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrardttrrirrglALIPedrqreglvQ 357
Cdd:cd03237 11 GEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-------------SYKP---------Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 VLSIASNLTLASLgrftrLFHIDRGAEKSA--IRDAIRDLSIKaPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:cd03237 69 YIKADYEGTVRDL-----LSSITKDFYTHPyfKTEIAKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 436 SRGIDVGAKADVFRTMRRLAANGLAILFsTSDLEEVMA--LSDRIAVLS 482
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAF-VVEHDIIMIdyLADRLIVFE 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-238 |
3.22e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVY-----SGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRII-------LDGKPVSFDS 80
Cdd:PRK13651 3 IKVKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 81 PAHA------------QANGI----GMIFQ--ELNLFANMSVAENIFARREitrgiLGIDHKAQVQKANAFLKRLDAGIE 142
Cdd:PRK13651 83 VLEKlviqktrfkkikKIKEIrrrvGVVFQfaEYQLFEQTIEKDIIFGPVS-----MGVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 143 -ADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEELMRIGDYITV 221
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*..
gi 499968440 222 LRDGQVtgeamVRDIDT 238
Cdd:PRK13651 238 FKDGKI-----IKDGDT 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
409-487 |
4.43e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 4.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 409 MSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
272-488 |
4.69e-07 |
|
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: 50.90 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 272 SLPRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDttrriRRGLALIPEDR 350
Cdd:COG4181 17 TVGTGAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-----EDARARLRARH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 351 -----QREGLVQVLSIASN----LTLASlgrftrlfhiDRGAEKSAiRDAIRDLSIKA-----PNpdfevtSMSGGNQQK 416
Cdd:COG4181 92 vgfvfQSFQLLPTLTALENvmlpLELAG----------RRDARARA-RALLERVGLGHrldhyPA------QLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 417 VVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDlEEVMALSDRIAVLSNGQLVA 488
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
410-487 |
5.03e-07 |
|
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: 50.34 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 410 SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLA-ANGLAILFSTSDL-EEVMALSDRIAVLSNGQLV 487
Cdd:cd03233 120 SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
319-503 |
6.54e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 319 STGKIFIDGkhVRARDTTRRIRRGLALIPedrQREGLVQVLSIASNLtlaslgRFTR----LFHIDRGAEKSAIRDAIRD 394
Cdd:PTZ00265 1275 NSGKILLDG--VDICDYNLKDLRNLFSIV---SQEPMLFNMSIYENI------KFGKedatREDVKRACKFAAIDEFIES 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 395 LsikaPNP-DFEV----TSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLE 469
Cdd:PTZ00265 1344 L----PNKyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
170 180 190
....*....|....*....|....*....|....
gi 499968440 470 EVMALSDRIAVLSNGQLVAVFDRNEATEEAIIAA 503
Cdd:PTZ00265 1420 ASIKRSDKIVVFNNPDRTGSFVQAHGTHEELLSV 1453
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
401-501 |
6.55e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 401 NPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVgakadvfRTMRRLAA-----NGlAILFSTSDLEEVMALS 475
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGflktfQG-SIIFISHDRSFIRNMA 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499968440 476 DRIAVLSNGQLV------------------------AVFDRNEATEEAII 501
Cdd:PRK11147 221 TRIVDLDRGKLVsypgnydqyllekeealrveelqnAEFDRKLAQEEVWI 270
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
265-494 |
7.44e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 265 VFRAENISLPRPTGgLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECV-----IGRHTHSTGKIFIDGKHVRARDTTrri 339
Cdd:PRK14243 10 VLRTENLNVYYGSF-LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 340 rrglaliP-EDRQREGLV-Q-----VLSIASNLTLASL-----GRFTRLfhIDRGAEKSAIRDAIRDlSIKAPNpdfevT 407
Cdd:PRK14243 86 -------PvEVRRRIGMVfQkpnpfPKSIYDNIAYGARingykGDMDEL--VERSLRQAALWDEVKD-KLKQSG-----L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANgLAILFSTSDLEEVMALSDRIAVLS----- 482
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNvelte 229
|
250
....*....|....*.
gi 499968440 483 ----NGQLVAvFDRNE 494
Cdd:PRK14243 230 gggrYGYLVE-FDRTE 244
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
251-487 |
8.85e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 251 KDFAK-SVDHAVGAEVFRaeNISLPRPTG-GLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGK 328
Cdd:PRK11176 328 KDEGKrVIERAKGDIEFR--NVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 329 HVRARdTTRRIRRGLALIPEDrqreglVQVL--SIASNLTLASLGRFTRlFHIDRGAEKSAIRDAIRDL-----SIKAPN 401
Cdd:PRK11176 406 DLRDY-TLASLRNQVALVSQN------VHLFndTIANNIAYARTEQYSR-EQIEEAARMAYAMDFINKMdngldTVIGEN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 402 PdfevTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAAN--GLAILFSTSDLEEvmalSDRIA 479
Cdd:PRK11176 478 G----VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIEK----ADEIL 549
|
....*...
gi 499968440 480 VLSNGQLV 487
Cdd:PRK11176 550 VVEDGEIV 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-487 |
1.13e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDG--------KHVR-----------------ARDT- 335
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkEFARrigvvfgqrsqlwwdlpAIDSf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 336 --TRRIRRglalIPEDRQREglvqvlsiasnltlaSLGRFTRLFHIDrgaekSAIRDAIRDLS----IKApnpdfEVTSm 409
Cdd:COG4586 118 rlLKAIYR----IPDAEYKK---------------RLDELVELLDLG-----ELLDTPVRQLSlgqrMRC-----ELAA- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 410 sggnqqkvvigkALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQLV 487
Cdd:COG4586 168 ------------ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
403-481 |
1.18e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 1.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499968440 403 DFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVL 481
Cdd:cd03236 134 DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
284-497 |
1.21e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGR----HTHSTGKIFIDGkhVRARDTTRRIRRGLALIPEDrqrEGLVQVL 359
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDG--ITPEEIKKHYRGDVVYNAET---DVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 360 SIASNLTLASLGRF--TRLFHIDRGAEKSAIRD---AIRDLSI----KAPNpDFeVTSMSGGNQQKVVIGKALMTNPKVL 430
Cdd:TIGR00956 154 TVGETLDFAARCKTpqNRPDGVSREEYAKHIADvymATYGLSHtrntKVGN-DF-VRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499968440 431 LMDEPSRGIDVGAKADVFRTMRRLA----ANGLAILFSTSdlEEVMALSDRIAVLSNGQLVAVFDRNEATE 497
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSAnildTTPLVAIYQCS--QDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
269-462 |
1.72e-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: 51.06 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFECVIgRHTHSTGKIFIDGKHVRARdTTRRIRRGLALIP 347
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSV-TLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 348 EDrqreglVQVLSIASNLTLASLGRFTRLfHIDRGAEKSAIRDAIRDLSIKApnpDFEVTS----MSGGNQQKVVIGKAL 423
Cdd:TIGR01271 1299 QK------VFIFSGTFRKNLDPYEQWSDE-EIWKVAEEVGLKSVIEQFPDKL---DFVLVDggyvLSNGHKQLMCLARSI 1368
|
170 180 190
....*....|....*....|....*....|....*....
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAIL 462
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
284-486 |
1.84e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHV-----RARDTTRRIRRGLA-----LIPEDRQRE 353
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAELRNQKLGFIyqfhhLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 354 GLVQVLSIASNLT----------LASLGRFTRLFHidRGAEksairdairdlsikapnpdfevtsMSGGNQQKVVIGKAL 423
Cdd:PRK11629 107 NVAMPLLIGKKKPaeinsralemLAAVGLEHRANH--RPSE------------------------LSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 424 MTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSdRIAVLSNGQL 486
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-203 |
1.95e-06 |
|
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: 48.39 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 26 VAVKRANLEL--------RRGAVNVLVGENGAGKSTLMKIIAGveRPTL----GRIILDGKPV--SFdspahaqANGIGM 91
Cdd:cd03232 13 VPVKGGKRQLlnnisgyvKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLdkNF-------QRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 92 IFQELNLFANMSVAENIfarrEIT---RGiLGIDHKaqvqkanaflKRLDAGIEadtmvedlpigqqqlveiakaMSLNA 168
Cdd:cd03232 84 VEQQDVHSPNLTVREAL----RFSallRG-LSVEQR----------KRLTIGVE---------------------LAAKP 127
|
170 180 190
....*....|....*....|....*....|....*
gi 499968440 169 RILIMDEPTSALSAAEVEILFKVIAELKAQGVAIV 203
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAIL 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
38-226 |
2.54e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 38 GAVNVLVGENGAGKSTLMKIIAGVERPT--LGRIILDGKpvsfdSPAHAQANGIGMIFQELNLFANMSVAEN-IFARREI 114
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR-----KPTKQILKRTGFVTQDDILYPHLTVRETlVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 115 TRGILGIDHKAQVQK---ANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKV 191
Cdd:PLN03211 169 LPKSLTKQEKILVAEsviSELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 499968440 192 IAELKAQGVAIVYISHR-LEELMRIGDYITVLRDGQ 226
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
284-452 |
2.74e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHT--HSTGKIFIDGkHVRARDTTRRI----RRGLALIPEDRQREGLVq 357
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG-FPKKQETFARIsgycEQNDIHSPQVTVRESLI- 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 358 vlsIASNLTLA-SLGRFTRLFHIDRGAEKSAIrDAIRDLSIKAPNpdfeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PLN03140 976 ---YSAFLRLPkEVSKEEKMMFVDEVMELVEL-DNLKDAIVGLPG----VTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170
....*....|....*.
gi 499968440 437 RGIDVGAKADVFRTMR 452
Cdd:PLN03140 1048 SGLDARAAAIVMRTVR 1063
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
43-227 |
2.82e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQANgIGMIFQELNLFANmSVAENIFARRE--------- 113
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-LGIIPQAPVLFSG-TVRFNLDPFNEhndadlwes 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 114 ITRGilgidHKAQVQKANAFlkRLDAgiEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVI- 192
Cdd:PLN03130 1348 LERA-----HLKDVIRRNSL--GLDA--EVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIr 1418
|
170 180 190
....*....|....*....|....*....|....*
gi 499968440 193 AELKAQGVAIvyISHRLEELMRIgDYITVLRDGQV 227
Cdd:PLN03130 1419 EEFKSCTMLI--IAHRLNTIIDC-DRILVLDAGRV 1450
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
282-488 |
3.31e-06 |
|
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: 47.31 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTrrIRRGLALIPedrQREGLVQVlSI 361
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLISVLN---QRPYLFDT-TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgRFtrlfhidrgaeksairdairdlsikapnpdfevtsmSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03247 92 RNNLGR----RF------------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499968440 442 GAKADVFRTMRRlAANGLAILFSTSDLEEVMALsDRIAVLSNGQLVA 488
Cdd:cd03247 132 ITERQLLSLIFE-VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
394-488 |
3.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 394 DLSIKAPnpdFEvtsMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID-VGAKA--DVFRTMRRlaANGLAILFSTSDLEE 470
Cdd:PRK13634 137 ELLARSP---FE---LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpKGRKEmmEMFYKLHK--EKGLTTVLVTHSMED 208
|
90
....*....|....*...
gi 499968440 471 VMALSDRIAVLSNGQLVA 488
Cdd:PRK13634 209 AARYADQIVVMHKGTVFL 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-211 |
4.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGvERP-------TL-GRIILDGKPVsFDSPAHaqangIGMIFQELNLFANMSVAenifARREI 114
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG-DHPqgysndlTLfGRRRGSGETI-WDIKKH-----IGYVSSSLHLDYRVSTS----VRNVI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 115 TRGI---LGIDHK---AQVQKANAFLKRLdaGIE---ADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEV 185
Cdd:PRK10938 360 LSGFfdsIGIYQAvsdRQQKLAQQWLDIL--GIDkrtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
170 180
....*....|....*....|....*..
gi 499968440 186 EILFKVIAELKAQG-VAIVYISHRLEE 211
Cdd:PRK10938 438 QLVRRFVDVLISEGeTQLLFVSHHAED 464
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
408-486 |
5.18e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.14 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRL-AANGLAILFSTSDLEEVMALSDRIAVLSNGQL 486
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-440 |
7.39e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPTLGRIILD-----GKpVSFDSPAHAQANGIGM-IFQELNLFANMSVAENIFARREITR 116
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGK-LRQDQFAFEEFTVLDTvIMGHTELWEVKQERDRIYALPEMSE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 117 --GILGIDHKAQV---------QKANAFLkrLDAGIEAD----TMVEDLPiGQQQLVEIAKAMSLNARILIMDEPTSALS 181
Cdd:PRK15064 111 edGMKVADLEVKFaemdgytaeARAGELL--LGVGIPEEqhygLMSEVAP-GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 182 AAEVEILFKVIAELKAqgvAIVYISHRLEEL--------------MRI--GDY------ITVLRDGQVTG----EAMVRD 235
Cdd:PRK15064 188 INTIRWLEDVLNERNS---TMIIISHDRHFLnsvcthmadldygeLRVypGNYdeymtaATQARERLLADnakkKAQIAE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 236 IDTrwIVR--SMIGSDAKDF---AKSVDHAVGAEV------------------FR----AENISLPRPTGGLsVNDVSLS 288
Cdd:PRK15064 265 LQS--FVSrfSANASKAKQAtsrAKQIDKIKLEEVkpssrqnpfirfeqdkklHRnaleVENLTKGFDNGPL-FKNLNLL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 289 VKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKI-FIDGKHV--RARDTTRRIRRGLAL---IPEDRQREGLVQVLSia 362
Cdd:PRK15064 342 LEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIgyYAQDHAYDFENDLTLfdwMSQWRQEGDDEQAVR-- 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 363 snltlASLGRFtrLFHIDrgaeksairdairdlSIKAPnpdfeVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK15064 420 -----GTLGRL--LFSQD---------------DIKKS-----VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-71 |
9.13e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 9.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 10 DVILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIL 71
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-212 |
1.12e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKP--VSFDSPAHAQANGIgmifqelnlfanmsv 104
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTGI--------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 105 aENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAE 184
Cdd:PRK13545 104 -ENI----ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180
....*....|....*....|....*...
gi 499968440 185 VEILFKVIAELKAQGVAIVYISHRLEEL 212
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
283-462 |
1.24e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHThsTGKIFIDGKHV--RARDTT--RRI---RRGLALIPEDRQREGL 355
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVngRPLDSSfqRSIgyvQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 V--QVLSIASNLTLASLGRFTRlfHIDRGAEKSAIRDAIrdlsIKAPNPDFEVtsmsggNQQK-VVIGKALMTNPKVLL- 431
Cdd:TIGR00956 858 RfsAYLRQPKSVSKSEKMEYVE--EVIKLLEMESYADAV----VGVPGEGLNV------EQRKrLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|.
gi 499968440 432 MDEPSRGIDVGAKADVFRTMRRLAANGLAIL 462
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
269-487 |
1.40e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.79 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrARDTTRRIRRGLALIpe 348
Cdd:PRK10790 344 DNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL-SSLSHSVLRQGVAMV-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 drQREGLVQVLSIASNLTLaslGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNPDFEV-TSMSGGNQQKVVIGKALMTNP 427
Cdd:PRK10790 421 --QQDPVVLADTFLANVTL---GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQgNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 428 KVLLMDEPSRGIDVGAKADVFRTMR--RLAANGLAILFSTSDLEEvmalSDRIAVLSNGQLV 487
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAavREHTTLVVIAHRLSTIVE----ADTILVLHRGQAV 553
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
285-486 |
1.48e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.31 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 285 VSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRGLALIPEDRQREGLVQVLSIASN 364
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 365 LTLASLGRFTRlfhiDRGAEKSAIrDAIRDLSIkAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID--VG 442
Cdd:PRK10584 109 VELPALLRGES----SRQSRNGAK-ALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499968440 443 AK-ADVFRTMRRLAANGLAILfsTSDlEEVMALSDRIAVLSNGQL 486
Cdd:PRK10584 183 DKiADLLFSLNREHGTTLILV--THD-LQLAARCDRRLRLVNGQL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-221 |
1.57e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERpTLGRIILDGkpVSFDSPAHAQ-ANGIGMIFQELNLFA-----NMSVAENiFARREITR 116
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTwRKAFGVIPQKVFIFSgtfrkNLDPYEQ-WSDEEIWK 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 117 GILGIDHKAQVQKanaFLKRLDAGIEADTMVedLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELK 196
Cdd:TIGR01271 1326 VAEEVGLKSVIEQ---FPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
170 180
....*....|....*....|....*
gi 499968440 197 AQGVAIVYiSHRLEELMRIGDYITV 221
Cdd:TIGR01271 1401 SNCTVILS-EHRVEALLECQQFLVI 1424
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-483 |
1.62e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 407 TSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILFSTSDLEEVMALSDRIAVLSN 483
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
284-487 |
2.03e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 284 DVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTtRRIRRGLALIpedrQREGLVQVLSIAS 363
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH-HYLHRQVALV----GQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 364 NLTLASlgRFTRLFHIDRGAEKSAIRDAIRDLsikaPNP-DFEV----TSMSGGNQQKVVIGKALMTNPKVLLMDEPSRG 438
Cdd:TIGR00958 574 NIAYGL--TDTPDEEIMAAAKAANAHDFIMEF----PNGyDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499968440 439 IDVGAKADVFRTMRRLAANGLAILFSTSDLEEvmalSDRIAVLSNGQLV 487
Cdd:TIGR00958 648 LDAECEQLLQESRSRASRTVLLIAHRLSTVER----ADQILVLKKGSVV 692
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-78 |
2.32e-05 |
|
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: 44.87 E-value: 2.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 499968440 34 ELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSF 78
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY 65
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
282-498 |
2.39e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.48 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVrardttrrirrgLALIPED-RQreglvQVLS 360
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI------------STLKPEIyRQ-----QVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 361 IASNLTLASLGRFTRL---FHIDRGA-EKSAIRDAIRDLSIKAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPS 436
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLifpWQIRNQQpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 437 RGIDVGAKADVFRTMRRLAAN-GLAILFSTSDLEEVMALSDRIAVLSNGQlvavfDRNEATEE 498
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQPHAG-----EMQEARYE 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
243-485 |
3.03e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 243 RSMIGSDAKDFAKSVDHAVGAEVFRAENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGK 322
Cdd:COG4178 340 EALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 323 IFI-DGKHV-----RAR---DTTRRirrglALI----PEDRQREGLVQVLsiasnlTLASLGRF-TRLfhiDRGAEKSAI 388
Cdd:COG4178 420 IARpAGARVlflpqRPYlplGTLRE-----ALLypatAEAFSDAELREAL------EAVGLGHLaERL---DEEADWDQV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 389 rdairdlsikapnpdfevtsMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANglAILFSTSDL 468
Cdd:COG4178 486 --------------------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG--TTVISVGHR 543
|
250
....*....|....*..
gi 499968440 469 EEVMALSDRIAVLSNGQ 485
Cdd:COG4178 544 STLAAFHDRVLELTGDG 560
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-226 |
3.45e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 40 VNVLVGENGAGKSTlmkIIAGVERPTLGRIILDGKPVSFD-SPAHAQANG--IGMIFQELN-----LFANMSVAEN-IFA 110
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDpKLIREGEVRaqVKLAFENANgkkytITRSLAILENvIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 111 RREITRGILgIDHkaqvqkanafLKRLDAGieadtmvedlpigQQQLVEI------AKAMSLNARILIMDEPTSALSAAE 184
Cdd:cd03240 101 HQGESNWPL-LDM----------RGRCSGG-------------EKVLASLiirlalAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499968440 185 VEI-LFKVIAELKAQGV-AIVYISHRLEELMRIGDYITVLRDGQ 226
Cdd:cd03240 157 IEEsLAEIIEERKSQKNfQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
269-483 |
4.29e-05 |
|
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: 44.07 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIfidGKHVRArdttrrirrGLALIPe 348
Cdd:cd03223 4 ENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE---------DLLFLP- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 349 drQReglvqvlsiaSNLTLASLgrftrlfhidrgaeksaiRDAIRdlsikapNPDFEVtsMSGGNQQKVVIGKALMTNPK 428
Cdd:cd03223 71 --QR----------PYLPLGTL------------------REQLI-------YPWDDV--LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 429 VLLMDEPSRGIDVGAKADVFRTMRRLaangLAILFSTSDLEEVMALSDRIAVLSN 483
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL----GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-228 |
4.89e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 37 RGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFDSPAHAQangigmifqelnlfaNMSVAENIFARREitr 116
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ---------------NDSLRENILFGKA--- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 117 giLGIDHKAQVQKANAFLKRLDAGIEAD-TMVED----LPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILF-K 190
Cdd:TIGR00957 725 --LNEKYYQQVLEACALLPDLEILPSGDrTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeH 802
|
170 180 190
....*....|....*....|....*....|....*....
gi 499968440 191 VIA-ELKAQGVAIVYISHRLEELMRIgDYITVLRDGQVT 228
Cdd:TIGR00957 803 VIGpEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKIS 840
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
282-485 |
5.12e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDttrrirrglaliPEDR------QREGL 355
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------------PADRdiamvfQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 356 VQVLSIASNLTLASLGRFTRLFHIDRGAEKSAIRDAIRDLSIKAPNpdfevtSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:PRK11650 88 YPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPR------ELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 436 SRGIDvgAKADVfrTMR--------RLAANGlaiLFSTSDLEEVMALSDRIAVLSNGQ 485
Cdd:PRK11650 162 LSNLD--AKLRV--QMRleiqrlhrRLKTTS---LYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
43-227 |
5.65e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.85 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 43 LVGENGAGKSTLMKIIAGVERpTLGRIILDGkpVSFDS-PAHAQANGIGMIFQELNLFANmSVAENI-----FARREITR 116
Cdd:cd03289 35 LLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG--VSWNSvPLQKWRKAFGVIPQKVFIFSG-TFRKNLdpygkWSDEEIWK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 117 GILGIDHKAQVQKanaFLKRLDAGIEADTMVedLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELK 196
Cdd:cd03289 111 VAEEVGLKSVIEQ---FPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAF 185
|
170 180 190
....*....|....*....|....*....|.
gi 499968440 197 AqGVAIVYISHRLEELMRIGDYItVLRDGQV 227
Cdd:cd03289 186 A-DCTVILSEHRIEAMLECQRFL-VIEENKV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
43-108 |
6.09e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 6.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 43 LVGENGAGKSTLMKIIAGVERPtlgriildgkpvsFDSPAHAQAN-GIGMIFQELNLFANMSVAENI 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKE-------------FEGEARPAPGiKVGYLPQEPQLDPEKTVRENV 91
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
33-59 |
7.21e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 44.37 E-value: 7.21e-05
10 20
....*....|....*....|....*..
gi 499968440 33 LELRRgAVNVLVGENGAGKSTLMKIIA 59
Cdd:COG3910 33 LEFHP-PVTFFVGENGSGKSTLLEAIA 58
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-219 |
8.30e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVE--RPTLGRIILDGKPVSFDSPAHAQANGIGMIFQELNLFANMSva 105
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPGVS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 106 eNIFARREITRGILGIDHKAQVQKANaFLKRLDAGIEADTMVEDLPI---------GQQQLVEIAKAMSLNARILIMDEP 176
Cdd:PRK09580 95 -NQFFLQTALNAVRSYRGQEPLDRFD-FQDLMEEKIALLKMPEDLLTrsvnvgfsgGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 177 TSALSAAEVEILFKVIAELKAQGVAIVYISHrleeLMRIGDYI 219
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGKRSFIIVTH----YQRILDYI 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
408-481 |
9.14e-05 |
|
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: 43.33 E-value: 9.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 408 SMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGL-AILFSTSDLEEVMALSDRIAVL 481
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-219 |
9.76e-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: 43.08 E-value: 9.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 150 LPIGQQQLVEIAKAMSLNAR--ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRlEELMRIGDYI 219
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-481 |
1.45e-04 |
|
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: 44.39 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 384 EKSAIRDAIRDLSIKaPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGLAILF 463
Cdd:COG1245 189 ERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLV 267
|
90
....*....|....*...
gi 499968440 464 STSDLEEVMALSDRIAVL 481
Cdd:COG1245 268 VEHDLAILDYLADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
91-306 |
1.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 91 MIFQELNLFANmSVAENIFARREITRGIlgidhKAQVqkanAFLKRLDAG-IEADTMVEDLPIGQQQLVEIAKAM--SLN 167
Cdd:PRK00635 427 MSLQELFIFLS-QLPSKSLSIEEVLQGL-----KSRL----SILIDLGLPyLTPERALATLSGGEQERTALAKHLgaELI 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 168 ARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRlEELMRIGDYITVL--RDGQVTGEAMVRdidtrwivrsm 245
Cdd:PRK00635 497 GITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIgpGAGIFGGEVLFN----------- 564
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499968440 246 iGSDAKDFAKSvdHAVGAEVFRAE-NISLP----RPTGGLSVN--------DVSLSVKAGEILGIYGLMGAGRS 306
Cdd:PRK00635 565 -GSPREFLAKS--DSLTAKYLRQElTIPIPekrtNSLGTLTLSkatkhnlkDLTISLPLGRLTVVTGVSGSGKS 635
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
282-470 |
2.53e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 282 VNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTrrIRRGLALIPedrQREGlvqvlsI 361
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT--YQKQLCFVG---HRSG------I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 362 ASNLTLaslgRFTRLFHIDRGAEKSAIRDAIRDLSIKApNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:PRK13540 86 NPYLTL----RENCLYDIHFSPGAVGITELCRLFSLEH-LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 499968440 442 GAKADVFRTMRRLAANGLAILFST--------SDLEE 470
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTShqdlplnkADYEE 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
410-487 |
2.55e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 43.68 E-value: 2.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499968440 410 SGGNQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRlAANGLAILFSTSDLEEVMALsDRIAVLSNGQLV 487
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-293 |
3.45e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKPVSFdspahaqANGIGMIFqelnlfaNMSVAENIF-- 109
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY-------VPQVSWIF-------NATVRENILfg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 110 ARREITRGILGIDHKAQVQKANAFlkrldAGIEADTMVE---DLPIGQQQLVEIAKAMSLNARILIMDEPTSALSAAEVE 186
Cdd:PLN03232 703 SDFESERYWRAIDVTALQHDLDLL-----PGRDLTEIGErgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 187 ILFKVIAELKAQGVAIVYISHRLEELMRIgDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSDAKDFAKSVDhavgaEVF 266
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQE-----VNT 851
|
250 260
....*....|....*....|....*...
gi 499968440 267 RAENISLPRPTGGLSVNDVSL-SVKAGE 293
Cdd:PLN03232 852 NDENILKLGPTVTIDVSERNLgSTKQGK 879
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-207 |
6.82e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 13 LRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIildgkpvsfdspAHAQANGIGMI 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 93 FQ--------ELNLFANMSVAENIFARREITRGILGidhkaqvqkanaflKRLDAGIEADTMVEDLPIGQQQLVEIAKAM 164
Cdd:PRK15064 388 AQdhaydfenDLTLFDWMSQWRQEGDDEQAVRGTLG--------------RLLFSQDDIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499968440 165 SLNARILIMDEPTSALSAAEVEILfkVIAELKAQGVAIvYISH 207
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESL--NMALEKYEGTLI-FVSH 493
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-71 |
1.07e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 12 ILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIIL 71
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-212 |
1.08e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 7 QKDDVILRLDDVSkvysgivavkranLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRIILDGKpvsfdspahaqa 86
Cdd:PRK13546 32 HKNKTFFALDDIS-------------LKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 87 ngIGMIFQELNLFANMSVAENIfarrEITRGILGIDHKAQVQKANAFLKRLDAGIEADTMVEDLPIGQQQLVEIAKAMSL 166
Cdd:PRK13546 87 --VSVIAISAGLSGQLTGIENI----EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499968440 167 NARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLEEL 212
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQV 206
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-263 |
1.25e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 134 LKRLDAGIEADTMVEDLPI-------------GQQQLVEIAKAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGV 200
Cdd:NF000106 116 LSRKDARARADELLERFSLteaagraaakysgGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499968440 201 AIVYISHRLEELMRIGDYITVLRDGQVTGEAMVRDIDTRWIVRSMIGSDAKdfAKSVDHAVGA 263
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH--AAELDRMVGA 256
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
40-69 |
1.33e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|
gi 499968440 40 VNVLVGENGAGKSTLMKIIAGVERPTLGRI 69
Cdd:COG3950 27 LTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-207 |
1.35e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.14 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 28 VKRANLELRRGaVNVLVGENGAGKSTLMKIIAGVERPTLGRII--------LDGKP------VSFDSP---------AHA 84
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgDDPDLpeieieLTFGSLlsrllrlllKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 85 QANGIGMIFQELN-----LFANMSvaENIFARREITRGILGIDHKAQVQKANAFLKRLDAGIEADTMV--EDLPIGQQQL 157
Cdd:COG3593 93 DKEELEEALEELNeelkeALKALN--ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELplDRLGSGFQRL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499968440 158 VEIA-------KAMSLNARILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISH 207
Cdd:COG3593 171 ILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
409-441 |
1.36e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 39.35 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|...
gi 499968440 409 MSGGNQQKVVIGKALMTNPKVLLMDEPSRGIDV 441
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-488 |
1.55e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.96 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 269 ENISLPRPTGGLSV-NDVSLSVKAGEILGIYGLMGAGRSEFFEcVIGRH-THSTGKIFIDGKHVRARDTTRrIRRGLALI 346
Cdd:PRK11160 342 NNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQ-LLTRAwDPQQGEILLNGQPIADYSEAA-LRQAISVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 347 PedrQReglVQVLS--IASNLTLAS-LGRFTRLFHIDR--GAEK---------SAIRDAIRDLSikapnpdfevtsmsGG 412
Cdd:PRK11160 420 S---QR---VHLFSatLRDNLLLAApNASDEALIEVLQqvGLEKlleddkglnAWLGEGGRQLS--------------GG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 413 NQQKVVIGKALMTNPKVLLMDEPSRGIDVGAKADVFRTMRRLAANGlAILFSTSDLEEvMALSDRIAVLSNGQLVA 488
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLTG-LEQFDRICVMDNGQIIE 553
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-219 |
1.77e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 153 GQQQLVEIAKAMSLNAR---ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLeELMRIGDYI 219
Cdd:TIGR00630 833 GEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYI 901
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-69 |
1.77e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499968440 1 MTTAEAQKDD------VILRLDDVSKVYSGIVAVKRANLELRRGAVNVLVGENGAGKSTLMKIIAGVERPTLGRI 69
Cdd:PRK11147 302 MGTAKMQVEEasrsgkIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
153-219 |
1.82e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 153 GQQQLVEIAKAMSLNAR---ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLeELMRIGDYI 219
Cdd:cd03271 173 GEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWI 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-230 |
2.79e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIAGvERPTL--GRIILDGKPvsfdspahAQANGIGMIFqelnlfaNMSVAENIF 109
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRsdASVVIRGTV--------AYVPQVSWIF-------NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 110 -------ARREITRGILGIDHKAQVQKANAFLKRLDAGIeadtmveDLPIGQQQLVEIAKAMSLNARILIMDEPTSALSA 182
Cdd:PLN03130 701 fgspfdpERYERAIDVTALQHDLDLLPGGDLTEIGERGV-------NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499968440 183 AEVEILFKVIAELKAQGVAIVYISHRLEELMRIgDYITVLRDGQVTGE 230
Cdd:PLN03130 774 HVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEE 820
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
269-334 |
2.96e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.34 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499968440 269 ENISLPRPTGGLSVNDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARD 334
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
153-210 |
3.39e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 3.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 153 GQQQLVEIAKAMSLNAR----ILIMDEPTSALSAAEVEILFKVIAELKAQGVAIVYISHRLE 210
Cdd:cd03227 81 GEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
27-207 |
5.24e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.80 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 27 AVKRANLELRRgaVNVLVGENGAGKSTLMKIIAGVERPTL-----GRI-ILDGKPVSFDSPAHAQANG--IGMIFQEL-N 97
Cdd:COG4938 11 PFKEAELELKP--LTLLIGPNGSGKSTLIQALLLLLQSNFiylpaERSgPARLYPSLVRELSDLGSRGeyTADFLAELeN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 98 LFANMSVAENIFAR-----REITRGILGIDHKAQVQKANafLKRLDAGIEADtmVEDLPIGQQQLVEIAkAMSLNAR--- 169
Cdd:COG4938 89 LEILDDKSKELLEQveewlEKIFPGKVEVDASSDLVRLV--FRPSGNGKRIP--LSNVGSGVSELLPIL-LALLSAAkpg 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499968440 170 -ILIMDEPTSAL-SAAEVEILfKVIAELKAQGVAIVYISH 207
Cdd:COG4938 164 sLLIIEEPEAHLhPKAQSALA-ELLAELANSGVQVIIETH 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
289-440 |
6.67e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.29 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 289 VKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGKHVRARDTTRRIRRgLALIPedrqreGLVQVLSIASNLtla 368
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-LGHLP------GLKADLSTLENL--- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499968440 369 slgRFTRLFHIDRGAEKSAIRDAIRDLsikAPNPDFEVTSMSGGNQQKVVIGKALMTNPKVLLMDEPSRGID 440
Cdd:PRK13543 104 ---HFLCGLHGRRAKQMPGSALAIVGL---AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
32-59 |
7.48e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 7.48e-03
10 20
....*....|....*....|....*...
gi 499968440 32 NLELRRGAVNVLVGENGAGKSTLMKIIA 59
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
283-485 |
8.14e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 37.83 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 283 NDVSLSVKAGEILGIYGLMGAGRSEFFECVIGRHTHSTGKIFIDGkhvrardttrrirrGLALIPEdrqrEGLVQVLSIA 362
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQ----EPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499968440 363 SNLTlaslgrFTRLFHIDRgaEKSAIRDA--IRDLSIkAPNPDF-EV----TSMSGGNQQKVVIGKALMTNPKVLLMDEP 435
Cdd:cd03250 84 ENIL------FGKPFDEER--YEKVIKACalEPDLEI-LPDGDLtEIgekgINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499968440 436 SRGIDVGAKADVF-RTMRRLAANGLAILFSTSDLeEVMALSDRIAVLSNGQ 485
Cdd:cd03250 155 LSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| |
